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Warning Text %XTableStyleMedium2PivotStyleLight16`rx heat-valueSfffP0@nf  S AA@A@   * AccessionSP GeneSymbol Short NameSort-ID# PSMsYWI38-1YWI38-2YWI38-3ISWI38-1ISWI38-2ISWI38-3SWI38-1SWI38-2SWI38-3 YWI38(Ave) ISWI38(Ave) SWI38(Ave) TTEST(IS/Y)log2Ratio(IS/Y)log10TTEST(IS/Y) TTEST(S/Y)log2Ratio(S/Y)log10TTEST(S/Y) Ratio(S/IS) TTEST(S/IS)log2Ratio(S/IS)log10TTEST(S/IS)# AAsMW [kDa]calc. pI Core pathwayComplex_component Complex_orderFunctionLength Pathway(1138)Intramembrane (151)Transmembrane(5186)Subcellular location [CC]"Gene ontology (biological process)"Gene ontology (molecular function)"Gene ontology (cellular component) Function [CC]P60709ACTBActin, cytoplasmic 1 Housekeepingactin SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.de novo' posttranslational protein folding [GO:0051084]; adherens junction organization [GO:0034332]; ATP-dependent chromatin remodeling [GO:0043044]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cellular protein metabolic process [GO:0044267]; chromatin organization [GO:0006325]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; membrane organization [GO:0061024]; movement of cell or subcellular component [GO:0006928]; platelet aggregation [GO:0070527]; protein folding [GO:0006457]; retina homeostasis [GO:0001895]; small GTPase mediated signal transduction [GO:0007264]; substantia nigra development [GO:0021762]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894]; nitric-oxide synthase binding [GO:0050998]; structural constituent of cytoskeleton [GO:0005200]; Tat protein binding [GO:0030957]`blood microparticle [GO:0072562]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dense body [GO:0097433]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; membrane [GO:0016020]; MLL5-L complex [GO:0070688]; myelin sheath [GO:0043209]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; ribonucleoprotein complex [GO:0030529]FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.P62736ACTAActin, aortic smooth muscle.SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.'glomerular mesangial cell development [GO:0072144]; mesenchyme migration [GO:0090131]; muscle contraction [GO:0006936]; positive regulation of gene expression [GO:0010628]; regulation of blood pressure [GO:0008217]; response to virus [GO:0009615]; vascular smooth muscle contraction [GO:0014829]=ATP binding [GO:0005524]; protein kinase binding [GO:0019901],actin cytoskeleton [GO:0015629]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; protein complex [GO:0043234]; smooth muscle contractile fiber [GO:0030485]P68133ACTSActin, alpha skeletal muscleArp2/3 complexcell growth [GO:0016049]; mesenchyme migration [GO:0090131]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; positive regulation of gene expression [GO:0010628]; response to extracellular stimulus [GO:0009991]; response to lithium ion [GO:0010226]; response to mechanical stimulus [GO:0009612]; response to steroid hormone [GO:0048545]; skeletal muscle fiber adaptation [GO:0043503]; skeletal muscle fiber development [GO:0048741]; skeletal muscle thin filament assembly [GO:0030240]ADP binding [GO:0043531]; ATP binding [GO:0005524]; myosin binding [GO:0017022]; structural constituent of cytoskeleton [GO:0005200]factin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; blood microparticle [GO:0072562]; cell body [GO:0044297]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; sarcomere [GO:0030017]; stress fiber [GO:0001725]; striated muscle thin filament [GO:0005865]Q92747ARC1A,Actin-related protein 2/3 complex subunit 1A<SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.Wactin cytoskeleton organization [GO:0030036]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; small GTPase mediated signal transduction [GO:0007264]?actin binding [GO:0003779]; actin filament binding [GO:0051015]~actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]FUNCTION: Probably functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.O15143ARC1B,Actin-related protein 2/3 complex subunit 1BmArp2/3 complex-mediated actin nucleation [GO:0034314]; movement of cell or subcellular component [GO:0006928]3structural constituent of cytoskeleton [GO:0005200]actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]FUNCTION: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.P61160ARP2Actin-related protein 2ySUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9000076}. Cell projection {ECO:0000269|PubMed:9000076}.Arp2/3 complex-mediated actin nucleation [GO:0034314]; asymmetric cell division [GO:0008356]; axon guidance [GO:0007411]; cilium assembly [GO:0042384]; cytoplasmic transport [GO:0016482]; ephrin receptor signaling pathway [GO:0048013]; establishment or maintenance of cell polarity [GO:0007163]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; meiotic chromosome movement towards spindle pole [GO:0016344]; meiotic cytokinesis [GO:0033206]; movement of cell or subcellular component [GO:0006928]; small GTPase mediated signal transduction [GO:0007264]; spindle localization [GO:0051653]MATP binding [GO:0005524]; structural constituent of cytoskeleton [GO:0005200]actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]NFUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. {ECO:0000269|PubMed:9000076}.P61158ARP3Actin-related protein 3SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection. Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).kArp2/3 complex-mediated actin nucleation [GO:0034314]; asymmetric cell division [GO:0008356]; axon guidance [GO:0007411]; cilium morphogenesis [GO:0060271]; ephrin receptor signaling pathway [GO:0048013]; establishment or maintenance of cell polarity [GO:0007163]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087< ]; meiotic chromosome movement towards spindle pole [GO:0016344]; meiotic cytokinesis [GO:0033206]; movement of cell or subcellular component [GO:0006928]; small GTPase mediated signal transduction [GO:0007264]; spindle localization [GO:0051653] actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; brush border [GO:0005903]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; membrane [GO:0016020]FUNCTION: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:9000076}.O15144ARPC2+Actin-related protein 2/3 complex subunit 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}. Cell junction, synapse, synaptosome {ECO:0000250}.Arp2/3 complex-mediated actin nucleation [GO:0034314]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; movement of cell or subcellular component [GO:0006928]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; small GTPase mediated signal transduction [GO:0007264]\actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]FUNCTION: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.O15145ARPC3+Actin-related protein 2/3 complex subunit 3?SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.aArp2/3 complex-mediated actin nucleation [GO:0034314]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; movement of cell or subcellular component [GO:0006928]; small GTPase mediated signal transduction [GO:0007264]actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; membrane [GO:0016020]P59998ARPC4+Actin-related protein 2/3 complex subunit 4ySUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9359840}. Cell projection {ECO:0000269|PubMed:9359840}.tactin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; small GTPase mediated signal transduction [GO:0007264]Penzyme binding [GO:0019899]; structural constituent of cytoskeleton [GO:0005200]{Arp2/3 protein complex [GO:0005885]; cell projection [GO:0042995]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]O15511ARPC5+Actin-related protein 2/3 complex subunit 5Actin-Arp2/3 complex(14)ySUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}.actin cytoskeleton organization [GO:0030036]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; axon guidance [GO:0007411]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; movement of cell or subcellular component [GO:0006928]; small GTPase mediated signal transduction [GO:0007264]actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]P08865RSSA40S ribosomal protein SA40SSUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus (By similarity). Colocalizes with PPP1R16B in the cell membrane. {ECO:0000255|HAMAP-Rule:MF_03016}.\cell adhesion [GO:0007155]; cellular protein metabolic process [GO:0044267]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000461]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit assembly [GO:0000028]; rRNA export from nucleus [GO:0006407]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]laminin receptor activity [GO:0005055]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735]90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:15516338, ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:6300843}.P15880RS240S ribosomal protein S2cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of transferase activity [GO:0051347]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]enzyme binding [GO:0019899]; fibroblast growth factor binding [GO:0017134]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]P23396RS340S ribosomal protein S3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175, ECO:< 0000269|PubMed:18045535, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:21871177}. Nucleus {ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:19460357, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:21871177}. Nucleus, nucleolus {ECO:0000269|PubMed:16314389, ECO:0000269|PubMed:19460357}. Mitochondrion inner membrane {ECO:0000269|PubMed:23911537}; Peripheral membrane protein {ECO:0000269|PubMed:23911537}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23131551}. Note=In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis (By similarity). Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide (PubMed:17560175). Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537). Localizes to the spindle during mitosis (PubMed:23131551). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). {ECO:0000250|UniProtKB:P62908, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17560175, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537}.apoptotic process [GO:0006915]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; gene expression [GO:0010467]; mitotic nuclear division [GO:0007067]; negative regulation of DNA repair [GO:0045738]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of DNA N-glycosylase activity [GO:1902546]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; regulation of translation [GO:0006417]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) lyase activity [GO:0003906]; enzyme binding [GO:0019899]; iron-sulfur cluster binding [GO:0051536]; mRNA binding [GO:0003729]; NF-kappaB binding [GO:0051059]; oxidized purine nucleobase lesion DNA N-glycosylase activity [GO:0008534]; poly(A) RNA binding [GO:0044822]; protein kinase A binding [GO:0051018]; protein kinase binding [GO:0019901]; structural constituent of ribosome [GO:0003735]icytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; ruffle membrane [GO:0032587]; spindle [GO:0005819] FUNCTION: Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408). {ECO:0000269|PubMed:14706345, ECO:0000269|PubMed:14988002, ECO:0000269|PubMed:15518571, ECO:0000269|PubMed:15707971, ECO:0000269|PubMed:17049931, ECO:0000269|PubMed:18045535, ECO:0000269|PubMed:18610840, ECO:0000269|PubMed:18973764, ECO:0000269|PubMed:19656744, ECO:0000269|PubMed:20217897, ECO:0000269|PubMed:20605787, ECO:0000269|PubMed:22510408, ECO:0000269|PubMed:23131551, ECO:0000269|PubMed:23911537, ECO:0000269|PubMed:7775413, ECO:0000269|PubMed:8706699}.P61247RS3A40S ribosomal protein S3aSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:17289661}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03122}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.0cell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; negative regulation of apoptotic process [GO:0043066]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]kpoly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: May play a role during erythropoiesis through regulation of transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.P62701RS4X#40S ribosomal protein S4, X isoformSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.rcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; multicellular organismal development [GO:0007275]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of cell proliferation [GO:0008284]; positive regulation of translation [GO:0045727]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]lpoly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]Lcytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]P46782RS540S ribosomal protein S58cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184];< regulation of translational fidelity [GO:0006450]; ribosomal small subunit assembly [GO:0000028]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; ribonucleoprotein complex [GO:0030529]P62753RS640S ribosomal protein S6activation-induced cell death of T cells [GO:0006924]; cellular protein metabolic process [GO:0044267]; erythrocyte development [GO:0048821]; G1/S transition of mitotic cell cycle [GO:0000082]; gastrulation [GO:0007369]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; mitotic cell cycle checkpoint [GO:0007093]; mitotic nuclear division [GO:0007067]; negative regulation of apoptotic process [GO:0043066]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; oogenesis stage [GO:0022605]; placenta development [GO:0001890]; positive regulation of apoptotic process [GO:0043065]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; T cell differentiation in thymus [GO:0033077]; T cell proliferation involved in immune response [GO:0002309]; TOR signaling [GO:0031929]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]vpoly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; structural constituent of ribosome [GO:0003735]cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; dendrite [GO:0030425]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]; small ribosomal subunit [GO:0015935]FUNCTION: May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.P62081RS740S ribosomal protein S7SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20873783}. Note=Colocalizes with NEK6 in the centrosome.jcell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; neural tube closure [GO:0001843]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; ribosome [GO:0005840]; small-subunit processome [GO:0032040]FFUNCTION: Required for rRNA maturation. {ECO:0000269|PubMed:19061985}.P62241RS840S ribosomal protein S8=cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]Qpoly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]P46781RS940S ribosomal protein S9Jcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of cell proliferation [GO:0008284]; positive regulation of translational fidelity [GO:0045903]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; translation regulator activity [GO:0045182]!cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; ribosome [GO:0005840]P46783RS1040S ribosomal protein S10/SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20159986}. Nucleus, nucleolus {ECO:0000269|PubMed:20159986}. Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit assembly [GO:0000028]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; ribosome [GO:0005840]1FUNCTION: Component of the 40S ribosomal subunit.P62280RS1140S ribosomal protein S11cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; osteoblast differentiation [GO:0001649]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]P25398RS1240S ribosomal protein S12 SUBCELLULAR LOCATION: Cytoplasm.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:< 0019058]; viral process [GO:0016032]; viral transcription [GO:0019083][cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; membrane [GO:0016020]P62277RS1340S ribosomal protein S13cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; negative regulation of RNA splicing [GO:0033119]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribosome [GO:0005840]P62263RS1440S ribosomal protein S146cellular protein metabolic process [GO:0044267]; erythrocyte differentiation [GO:0030218]; gene expression [GO:0010467]; maturation of SSU-rRNA [GO:0030490]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translation [GO:0006417]; ribosomal small subunit assembly [GO:0000028]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]mRNA 5'-UTR binding [GO:0048027]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]; translation regulator activity [GO:0045182]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]P62841RS1540S ribosomal protein S15cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; osteoblast differentiation [GO:0001649]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal small subunit export from nucleus [GO:0000056]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]kDNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]P62244RS15A40S ribosomal protein S15a^cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; response to virus [GO:0009615]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; membrane [GO:0016020]P62249RS1640S ribosomal protein S16cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; small ribosomal subunit [GO:0015935]P08708RS1740S ribosomal protein S17zcellular protein metabolic process [GO:0044267]; erythrocyte homeostasis [GO:0034101]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; ribosome [GO:0005840]P62269RS1840S ribosomal protein S18cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]xFUNCTION: Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA. {ECO:0000250}.P39019RS1940S ribosomal protein S19SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586610, ECO:0000269|PubMed:17517689}. Note=Located more specifically in the nucleoli.cellular protein metabolic process [GO:0044267]; erythrocyte differentiation [GO:0030218]; gene expression [GO:0010467]; maturation of SSU-rRNA [GO:0030490]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; monocyte chemotaxis [GO:0002548]; negative regulation of respiratory burst involved in inflammatory response [GO:0060266]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nucleolus organization [GO:0007000]; positive regulation of cellular component movement [GO:0051272]; positive regulation of respiratory burst involved in inflammatory response [GO:0060265]; protein tetramerization [GO:0051262]; response to extracellular stimulus [GO:0009991]; ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]fibroblast growth factor binding [GO:0017134]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; structural constituent of ribosome [GO:0003735]sFUNCTION: Required for pre-rRNA processing and maturation of 40S ribosomal subunits. {ECO:0000269|PubMed:16990592}.< P60866RS2040S ribosomal protein S20.SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.P63220RS2140S ribosomal protein S21cellular protein metabolic process [GO:0044267]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000461]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit biogenesis [GO:0042274]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]zpoly(A) RNA binding [GO:0044822]; protein N-terminus binding [GO:0047485]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935]P62266RS2340S ribosomal protein S23cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; membrane [GO:0016020]; nucleolus [GO:0005730]; ribosome [GO:0005840]P62847RS2440S ribosomal protein S24cellular protein metabolic process [GO:0044267]; erythrocyte homeostasis [GO:0034101]; gene expression [GO:0010467]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]; translation initiation factor binding [GO:0031369]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; membrane [GO:0016020]; nucleus [GO:0005634]; small ribosomal subunit [GO:0015935]vFUNCTION: Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. {ECO:0000269|PubMed:18230666}.P62851RS2540S ribosomal protein S25:poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribosome [GO:0005840]; small ribosomal subunit [GO:0015935]P62854RS2640S ribosomal protein S26lmRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]; small ribosomal subunit [GO:0015935]Q71UM5RS27L40S ribosomal protein S27-likeactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; mitotic G1 DNA damage checkpoint [GO:0031571]; positive regulation of translation [GO:0045727]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412]cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]; translation activator activity [GO:0008494]Dcytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]P62979RS27A$Ubiquitin-40S ribosomal protein S27aPSUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.activation of MAPK activity [GO:0000187]; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to hypoxia [GO:0071456]; circadian rhythm [GO:0007623]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage response, detection of DNA damage [GO:0042769]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA repair [GO:0006281]; endosomal transport [GO:0016197]; epidermal growth factor receptor signaling pathway [GO:0007173]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; innate immune response [GO:0045087]; intracellular transport of virus [GO:0075733]; ion transmembrane transport [GO:0034220]; JNK cascade [GO:0007254]; membrane organization [GO:0061024]; mitotic cell cycle [GO:0000278]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of type I interferon production [GO:0032480]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of necrotic cell death [GO:0010939]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of type I interferon production [GO:0032479]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; SRP-dependent cotranslatio< nal protein targeting to membrane [GO:0006614]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; translesion synthesis [GO:0019985]; transmembrane transport [GO:0055085]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; viral transcription [GO:0019083]; virion assembly [GO:0019068]qmetal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; endocytic vesicle membrane [GO:0030666]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; small ribosomal subunit [GO:0015935]FUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.; FUNCTION: 40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome.P62857RS2840S ribosomal protein S28ncellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal small subunit biogenesis [GO:0042274]; ribosome biogenesis [GO:0042254]; rRNA export from nucleus [GO:0006407]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; small ribosomal subunit [GO:0015935]P62273RS2940S ribosomal protein S29Nstructural constituent of ribosome [GO:0003735]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; small ribosomal subunit [GO:0015935]P62861RS3040S ribosomal protein S3040S(32)lantibacterial humoral response [GO:0019731]; cellular protein metabolic process [GO:0044267]; defense response to Gram-positive bacterium [GO:0050830]; gene expression [GO:0010467]; innate immune response in mucosa [GO:0002227]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]IRNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; extracellular space [GO:0005615]; small ribosomal subunit [GO:0015935]P39023RL360S ribosomal protein L360SpSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16963496}. Cytoplasm {ECO:0000269|PubMed:16963496}.6cellular protein metabolic process [GO:0044267]; cellular response to interleukin-4 [GO:0071353]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit assembly [GO:0000027]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]VFUNCTION: The L3 protein is a component of the large subunit of cytoplasmic ribosomes.P36578RL460S ribosomal protein L4cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083] cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]P46777RL560S ribosomal protein L5\SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.7}. Nucleus, nucleolus {ECO:0000269|Ref.7}.Tcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit assembly [GO:0000027]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]5S rRNA binding [GO:0008097]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]FUNCTION: Required for rRNA maturation and formation of the 60S ribosomal < subunits. This protein binds 5S RNA. {ECO:0000269|PubMed:19061985}.Q02878RL660S ribosomal protein L6dcellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of transcription, DNA-templated [GO:0006355]; ribosomal large subunit assembly [GO:0000027]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]vFUNCTION: Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I.P18124RL760S ribosomal protein L7cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]DNA binding [GO:0003677]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]!cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]FUNCTION: Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.Q6DKI1RL7L60S ribosomal protein L7-like 1blastocyst formation [GO:0001825]; cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]Fcytosolic large ribosomal subunit [GO:0022625]; nucleolus [GO:0005730]P62424RL7A60S ribosomal protein L7acellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosome biogenesis [GO:0042254]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; polysomal ribosome [GO:0042788]P62917RL860S ribosomal protein L8>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:12962325}.poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]P32969RL960S ribosomal protein L9dRNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribosome [GO:0005840]P27635RL1060S ribosomal protein L10cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit assembly [GO:0000027]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]P62906RL10A60S ribosomal protein L10aanatomical structure morphogenesis [GO:0009653]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]P62913RL1160S ribosomal protein L117SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; protein localization to nucleus [GO:0034504]; protein targeting [GO:0006605]; ribosomal large subunit assembly [GO:0000027]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]FUNCTION: Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). {ECO:0000250}.P30050RL1260S ribosomal protein L12cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]=FUNCTION: Binds directly to 26S ribosomal RNA. {ECO:0000250}.P26373RL1360S ribosomal protein L13cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]P40429RL13A60S ribosomal protein L13a>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14567916}.cellular protein metabolic process [GO:0044267]; cellular response to interferon-gamma [GO:0071346]; gene expression [GO:0010467]; negative regulation of formation of translation preinitiation complex [GO:1901194]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elon< gation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]'cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; focal adhesion [GO:0005925]; GAIT complex [GO:0097452]; large ribosomal subunit [GO:0015934]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]}FUNCTION: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA. {ECO:0000269|PubMed:14567916, ECO:0000269|PubMed:17218275, ECO:0000269|PubMed:17921318, ECO:0000269|PubMed:23071094}.P50914RL1460S ribosomal protein L14%cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; membrane [GO:0016020]P61313RL1560S ribosomal protein L15cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; ribosome [GO:0005840]P18621RL1760S ribosomal protein L17Zcytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; nucleus [GO:0005634]Q07020RL1860S ribosomal protein L18cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]Q02543RL18A60S ribosomal protein L18a[cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; membrane [GO:0016020]P84098RL1960S ribosomal protein L19P46778RL2160S ribosomal protein L21cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; membrane [GO:0016020]; nucleolus [GO:0005730]P35268RL2260S ribosomal protein L22,alpha-beta T cell differentiation [GO:0046632]; cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]heparin binding [GO:0008201]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]Q6P5R6RL22L 60S ribosomal protein L22-like 1$cytoplasmic translation [GO:0002181].cytosolic large ribosomal subunit [GO:0022625]P62829RL2360S ribosomal protein L23 cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal protein import into nucleus [GO:0006610]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]large ribosomal subunit rRNA binding [GO:0070180]; poly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; ribosome [GO:0005840]P62750RL23A60S ribosomal protein L23a&cell proliferation [GO:0008283]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit assembly [GO:0000027]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]; TORC2 complex [GO:0031932]QFUNCTION: This protein binds to a specific region on the 26S rRNA. {ECO:0000250}.P83731RL2460S ribosomal protein L24assembly of large subunit precursor of preribosome [GO:1902626]; cellular protein metabolic process [GO:0044267]; exit from mitosis [GO:0010458]; gene expression [GO:0010467]; mitotic cell cycle checkpoint [GO:0007093]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; optic nerve development [GO:0021554]; retina development in camera-type eye [GO:0060041]; retinal ganglion cell axon guidance [GO:0031290]; ribosomal large subunit assembly [GO:0000027]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; membrane [GO:0016020]Q9UNX3RL26L 60S ribosomal protein L26-like 1-cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit biogenesis [GO:0042273]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]hcytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]P61254RL2660S ribosomal protein L26Kcellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; SRP-dependent cotranslational protein targeting to membran< e [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]P61353RL2760S ribosomal protein L27cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; ribosome [GO:0005840]P46776RL27A60S ribosomal protein L27aP46779RL2860S ribosomal protein L28Tcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of mitochondrion degradation [GO:1903146]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]P47914RL2960S ribosomal protein L29cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; embryo implantation [GO:0007566]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]P62888RL3060S ribosomal protein L30cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]P62899RL3160S ribosomal protein L31P62910RL3260S ribosomal protein L32centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; membrane [GO:0016020]P49207RL3460S ribosomal protein L34cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]P42766RL3560S ribosomal protein L35=cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]P18077RL35A60S ribosomal protein L35alpoly(A) RNA binding [GO:0044822]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049]cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site. {ECO:0000269|PubMed:18535205}.Q9Y3U8RL3660S ribosomal protein L36P83881RL36A60S ribosomal protein L36a[cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; ribosome [GO:0005840]Q969Q0RL36L60S ribosomal protein L36a-like.SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.translation [GO:0006412]/structural constituent of ribosome [GO:0003735]P61927RL3760S ribosomal protein L37metal ion binding [GO:0046872]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]Dcytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]/FUNCTION: Binds to the 23S rRNA. {ECO:0000250}.P61513RL37A60S ribosomal protein L37acytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]P63173RL3860S ribosomal protein L3890S preribosome assembly [GO:0034463]; axial mesoderm development [GO:0048318]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; middle ear morphogenesis [GO:0042474]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; ossification [GO:0001503]; regulation of translation [GO:0006417]; ribonucleoprotein complex assembly [GO:0022618]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; eukaryotic 80S initiation complex [GO:0033291]; focal adhesion [GO:0005925]Q59GN2R39L5)Putative 60S ribosomal protein L39-like 5ribosome [GO:0005840]P62987RL40#Ubiquitin-60S ribosomal protein L40SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm {ECO:0000250}.activation of MAPK activity [GO:0000187]; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; cellular response to hypoxia [GO:0071456]; circadian rhythm [GO:0007623]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage response, detection of DNA damage [GO:0042769]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA repair [GO:0006281]; endosomal transport [GO:0016197]; epidermal growth factor receptor signaling pathway [GO:0007173]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; innate immune response [GO:0045087]; intracellular transport of virus [GO:0075733]; ion transmembrane transport [GO:0034220]; JNK cascade [GO:0007254]; membrane organization [GO:0061024]; mitotic cell cycle [GO:0000278]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epide< rmal growth factor receptor signaling pathway [GO:0042059]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of type I interferon production [GO:0032480]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of necrotic cell death [GO:0010939]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of type I interferon production [GO:0032479]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; translation [GO:0006412]; translational elongation [GO:0006414]; translational initiation [GO:0006413]; translational termination [GO:0006415]; translesion synthesis [GO:0019985]; transmembrane transport [GO:0055085]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; viral transcription [GO:0019083]; virion assembly [GO:0019068]Ycytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; endocytic vesicle membrane [GO:0030666]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ribosome [GO:0005840]yFUNCTION: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.; FUNCTION: 60S ribosomal protein L40: Component of the 60S subunit of the ribosome. Ribosomal protein L40 is essential for translation of a subset of cellular transcripts, and especially for cap-dependent translation of vesicular stomatitis virus mRNAs.P05388RLA060S acidic ribosomal protein P0tSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.&cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]RFUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.P05386RLA160S acidic ribosomal protein P1cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]NFUNCTION: Plays an important role in the elongation step of protein synthesis.P05387RLA260S acidic ribosomal protein P260S(47)Q9BYD6RM01'39S ribosomal protein L1, mitochondrial39S (MT)BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279069}.mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]large ribosomal subunit [GO:0015934]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q5T653RM02'39S ribosomal protein L2, mitochondrial2SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]P09001RM03'39S ribosomal protein L3, mitochondrial$SUBCELLULAR LOCATION: Mitochondrion.mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; translation [GO:0006412]Q9BYD3RM04'39S ribosomal protein L4, mitochondrial@mitochondrial inner membrane [GO:0005743]; ribosome [GO:0005840]Q9BYD2RM09'39S ribosomal protein L9, mitochondrialjmitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]Q7Z7H8RM10(39S ribosomal protein L10, mitochondrial'mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosome biogenesis [GO:0042254]; translation [GO:0006412]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]Q9Y3B7RM11(39S ribosomal protein L11, mitochondrial4mitochondrial translation [GO:003254< 3]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosomal large subunit assembly [GO:0000027]; translation [GO:0006412]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrial ribosome [GO:0005761]P52815RM12(39S ribosomal protein L12, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription from mitochondrial promoter [GO:0006390]; translation [GO:0006412]ymitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]Q9BYD1RM13(39S ribosomal protein L13, mitochondrialQ6P1L8RM14(39S ribosomal protein L14, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11543634, ECO:0000269|PubMed:22829778}.FUNCTION: Forms part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1 intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation (Probable). {ECO:0000305|PubMed:22829778}.Q9P015RM15(39S ribosomal protein L15, mitochondrialQ9NX20RM16(39S ribosomal protein L16, mitochondrialJrRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]CFUNCTION: Component of the large subunit of mitochondrial ribosome.Q9NRX2RM17(39S ribosomal protein L17, mitochondrial2SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.mitochondrial genome maintenance [GO:0000002]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]]protein domain specific binding [GO:0019904]; structural constituent of ribosome [GO:0003735]Q9H0U6RM18(39S ribosomal protein L18, mitochondrial2mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; rRNA import into mitochondrion [GO:0035928]; translation [GO:0006412]M5S rRNA binding [GO:0008097]; structural constituent of ribosome [GO:0003735]extracellular space [GO:0005615]; mitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]FUNCTION: Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA. {ECO:0000269|PubMed:21685364}.P49406RM19(39S ribosomal protein L19, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10600119, ECO:0000269|PubMed:11543634}.mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]Q9BYC9RM20(39S ribosomal protein L20, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosomal large subunit assembly [GO:0000027]Nmitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]Q7Z2W9RM21(39S ribosomal protein L21, mitochondrialQ9NWU5RM22(39S ribosomal protein L22, mitochondrialQ16540RM23(39S ribosomal protein L23, mitochondrialjnucleotide binding [GO:0000166]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]Q96A35RM24(39S ribosomal protein L24, mitochondrial\mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; ribosome [GO:0005840]Q9P0M9RM27(39S ribosomal protein L27, mitochondrialQ13084RM28(39S ribosomal protein L28, mitochondrialcytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q8TCC3RM30(39S ribosomal protein L30, mitochondrialQ9BYC8RM32(39S ribosomal protein L32, mitochondrialO75394RM33(39S ribosomal protein L33, mitochondrialQ9BQ48RM34(39S ribosomal protein L34, mitochondrialQ9NZE8RM35(39S ribosomal protein L35, mitochondrialQ9BZE1RM37(39S ribosomal protein L37, mitochondrialQ96DV4RM38(39S ribosomal protein L38, mitochondrialQ9NYK5RM39(39S ribosomal protein L39, mitochondrialAnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]Q9NQ50RM40(39S ribosomal protein L40, mitochondrialanatomical structure morphogenesis [GO:0009653]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996] poly(A) RNA binding [GO:0044822]mitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]Q8IXM3RM41(39S ribosomal protein L41, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16024796}.>apoptotic process [GO:0006915]; cell cycle [GO:0007049]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; translation [GO:0006412]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. {ECO:0000269|PubMed:16024796, ECO:0000269|PubMed:16256947}.Q9Y6G3RM42(39S ribosomal protein L42, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123}.mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]Q8N983RM43(39S ribosomal protein L43, mitochondrialQ9H9J2RM44(39S ribosomal protein L44, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; RNA processing [GO:0006396]Hpoly(A) RNA binding [GO:0044822]; ribonuclease III activity [GO:0004525]FUNCTION: Component of the 39S subunit of mitochondrial ribosome. May have a function in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome. {ECO:0000269|PubMed:23315540}.Q9BRJ2RM45(39S ribosomal protein L45, mitochondrialQ9H2W6RM46(39S ribosomal protein L46, mitochondrialPhydrolase activity [GO:0016787]; structural constituent of ribosome [GO:0003735]cell junction [GO:0030054]; mitochondrial inner me< mbrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q9HD33RM47(39S ribosomal protein L47, mitochondrialQ96GC5RM48(39S ribosomal protein L48, mitochondrialQ13405RM49(39S ribosomal protein L49, mitochondrialQ8N5N7RM50(39S ribosomal protein L50, mitochondrialQ4U2R6RM51(39S ribosomal protein L51, mitochondrialQ86TS9RM52(39S ribosomal protein L52, mitochondrialQ96EL3RM53(39S ribosomal protein L53, mitochondrialQ6P161RM54(39S ribosomal protein L54, mitochondrialQ7Z7F7RM55(39S ribosomal protein L55, mitochondrial 39S (MT) (47)Q9Y399RT02'28S ribosomal protein S2, mitochondrial28S (MT)activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; mitochondrial translation [GO:0032543]; positive regulation of defense response to virus by host [GO:0002230]; translation [GO:0006412]Nmitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]P82675RT05'28S ribosomal protein S5, mitochondrialymitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]P82932RT06'28S ribosomal protein S6, mitochondrialbsmall ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; small ribosomal subunit [GO:0015935]Q9Y2R9RT07'28S ribosomal protein S7, mitochondrial4mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]]mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]P82933RT09'28S ribosomal protein S9, mitochondrialDNA damage response, detection of DNA damage [GO:0042769]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; translation [GO:0006412]mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]P82664RT10(28S ribosomal protein S10, mitochondrialactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; positive regulation of defense response to virus by host [GO:0002230]P82912RT11(28S ribosomal protein S11, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11402041}.DNA damage response, detection of DNA damage [GO:0042769]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412]mRNA 5'-UTR binding [GO:0048027]; poly(A) RNA binding [GO:0044822]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]O15235RT12(28S ribosomal protein S12, mitochondrialmitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrial small ribosomal subunit [GO:0005763]O60783RT14(28S ribosomal protein S14, mitochondrialmitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]P82914RT15(28S ribosomal protein S15, mitochondrialmitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]Q9Y3D3RT16(28S ribosomal protein S16, mitochondrialcytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]Q9Y2R5RT17(28S ribosomal protein S17, mitochondrialQ9NVS2RT18A)28S ribosomal protein S18a, mitochondrialQ9Y676RT18B)28S ribosomal protein S18b, mitochondrialcell junction [GO:0030054]; mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]P82921RT21(28S ribosomal protein S21, mitochondrialP82650RT22(28S ribosomal protein S22, mitochondrialmitochondrial inner membrane [GO:0005743]; mitochondrial ribosome [GO:0005761]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]Q9Y3D9RT23(28S ribosomal protein S23, mitochondrialintermediate filament cytoskeleton [GO:0045111]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; ribosome [GO:0005840]Q96EL2RT24(28S ribosomal protein S24, mitochondrialP82663RT25(28S ribosomal protein S25, mitochondrialQ9BYN8RT26(28S ribosomal protein S26, mitochondrialQDNA damage response, detection of DNA damage [GO:0042769]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; peptide biosynthetic process [GO:0043043]mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q92552RT27(28S ribosomal protein S27, mitochondrialQ9Y2Q9RT28(28S ribosomal protein S28, mitochondrialP51398RT29(28S ribosomal protein S29, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11162496, ECO:0000269|PubMed:20563667}.Capoptotic mitochondrial changes [GO:0008637]; apoptotic signaling pathway [GO:0097190]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]mitochondrial inner membrane [GO:0005743]; mitochondrial small ribosomal subunit [GO:0005763]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]DFUNCTION: Involved in mediating interferon-gamma-induced cell death.Q9NP92RT30(28S ribosomal protein S30, mitochondrial apoptotic process [GO:0006915]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]Q92665RT31(28S ribosomal protein S31, mitochondrialpoly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; structural constituent of ribosome [GO:0003735]Q9Y291RT33(28S ribosomal protein S33, mitochondrialP82930RT34(28S ribosomal protein S34, mitochondrialFUNCTION: Required for mitochondrial translation, plays a role in maintaining the stability of the small ribosomal subunit and the 12S rRNA that are required for mitoribosome formation. {ECO:0000250|UniProtKB:Q9JIK9}.P82673RT35(28S ribosomal protein S35, mitochondrialCSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q2Y< DF6}.&DNA damage response, detection of DNA damage [GO:0042769]; mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]P82909RT36(28S ribosomal protein S36, mitochondrial 28S (MT)(30)Q96EE3SEH1Nucleoporin SEH1 hNPC -coatYSUBCELLULAR LOCATION: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.&attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; carbohydrate metabolic process [GO:0005975]; cell division [GO:0051301]; cellular protein complex localization [GO:0034629]; cellular protein metabolic process [GO:0044267]; cellular response to amino acid starvation [GO:0034198]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; cytokine production involved in inflammatory response [GO:0002534]; defense response to Gram-positive bacterium [GO:0050830]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic metaphase plate congression [GO:0007080]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; nuclear pore organization [GO:0006999]; positive regulation of TOR signaling [GO:0032008]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; GATOR2 complex [GO:0061700]; nuclear envelope [GO:0005635]; nuclear pore outer ring [GO:0031080]_FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900, ECO:0000269|PubMed:23723238}.Q9BW27NUP85"Nuclear pore complex protein Nup85_SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Nucleus membrane. Note=During mitosis, localizes to the kinetochores and spindle poles. Upon CCl2 stimulation translocates from the cytoplasm to the membrane and colocalizes with CCR2 at the front of migrating cells.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; lamellipodium assembly [GO:0030032]; macrophage chemotaxis [GO:0048246]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore outer ring [GO:0031080]; spindle [GO:0005819]FUNCTION: Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356}.Q12769NU160#Nuclear pore complex protein Nup160oSUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.Tcarbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]3nucleocytoplasmic transporter activity [GO:0005487]tcytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear pore [GO:0005643]; nuclear pore outer ring [GO:0031080]LFUNCTION: Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.P55735SEC13Protein SEC13 homologSUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex. Note=In interphase, localizes at both sides of the NPC.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; mitotic cell cycle [GO:0000278]; mRNA transport [GO:0051028]; positive regulation of TOR signaling [GO:0032008]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small GTPase mediated signal transduction [GO:0007264]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular exosome [GO:0070062]; GATOR2 complex [GO:0061700]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nuclear pore outer ring [GO:0031080]rFUNCTION: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:8972206}.P57740NU107#Nuclear pore complex protein Nup107=SUBCELLULAR LOCATION: Nucleus membrane. Nucleus, nuclear pore complex. Chromosome, centromere, kinetochore. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044< 267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; nuclear pore complex assembly [GO:0051292]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]hnucleocytoplasmic transporter activity [GO:0005487]; structural constituent of nuclear pore [GO:0017056],centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore outer ring [GO:0031080]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. {ECO:0000269|PubMed:12552102, ECO:0000269|PubMed:15229283}.Q8WUM0NU133#Nuclear pore complex protein Nup133SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Chromosome, centromere, kinetochore. Note=Located on both the cytoplasmic and nuclear sides of the nuclear pore. During mitosis, localizes to the kinetochores.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; nuclear pore organization [GO:0006999]; paraxial mesoderm development [GO:0048339]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore outer ring [GO:0031080]Q8NFH4NUP37Nucleoporin Nup37carbohydrate metabolic process [GO:0005975]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; chromosome segregation [GO:0007059]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear pore outer ring [GO:0031080]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]HFUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.Q8NFH3NUP43Nucleoporin Nup43condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear pore outer ring [GO:0031080]Q8N1F7NUP93"Nuclear pore complex protein Nup93 hNPC-adaptorSUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein. Nucleus, nuclear pore complex. Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; nuclear pore complex assembly [GO:0051292]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of defense response to virus by host [GO:0002230]; post-translational protein modification [GO:0043687]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]3structural constituent of nuclear pore [GO:0017056]membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC. {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15703211}.Q92621NU205#Nuclear pore complex protein Nup205SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein. Nucleus, nuclear pore complex. Note=Localized near the center, on both the cytoplasmic and nuclear side, of the NPC core structure.{carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; nuclear pore complex assembly [GO:0051292]; nucleocytoplasmic transport [GO:0006913]; post-translational protein modification [GO:0043687]; protein import into nucleus, docking [GO:0000059]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC. {ECO:0000269|PubMed:15229283}.Q5SRE5NU188Nucleoporin NUP188 homologBSUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000305}.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [< GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]Omembrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear pore [GO:0005643]HFUNCTION: May function as a component of the nuclear pore complex (NPC).O75694NU155#Nuclear pore complex protein Nup155^SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.atrial cardiac muscle cell action potential [GO:0086014]; carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; nuclear envelope organization [GO:0006998]; post-translational protein modification [GO:0043687]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]Vstructural constituent of nuclear pore [GO:0017056]; transporter activity [GO:0005215]nmembrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]FUNCTION: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.Q8NFH5NUP53Nucleoporin NUP53SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein. Note=Tightly associated with the nuclear membrane and lamina.intermediate filament cytoskeleton [GO:0045111]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]oFUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs). Can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC. {ECO:0000269|PubMed:15703211}.P37198NUP62Nuclear pore glycoprotein p62 hNPC-channelSUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, spindle pole. Note=Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle.carbohydrate metabolic process [GO:0005975]; cell aging [GO:0007569]; cell death [GO:0008219]; cell surface receptor signaling pathway [GO:0007166]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; hormone-mediated signaling pathway [GO:0009755]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of programmed cell death [GO:0043069]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of transcription, DNA-templated [GO:0045893]; post-translational protein modification [GO:0043687]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; regulation of Ras protein signal transduction [GO:0046578]; regulation of signal transduction [GO:0009966]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]chromatin binding [GO:0003682]; receptor signaling complex scaffold activity [GO:0030159]; SH2 domain binding [GO:0042169]; structural constituent of nuclear pore [GO:0017056]; thyroid hormone receptor binding [GO:0046966]; ubiquitin binding [GO:0043130]Rcytoplasm [GO:0005737]; Flemming body [GO:0090543]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleocytoplasmic shuttling complex [GO:0031074]; pore complex [GO:0046930]; ribonucleoprotein complex [GO:0030529]; spindle pole [GO:0000922]FUNCTION: Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex.Q7Z3B4NUP54Nucleoporin p54SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter (By similarity). {ECO:0000250}.hcarbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein sumoylation [GO:0016925]; protein targeting [GO:0006605]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. {ECO:0000250}.Q9BVL2NUPL1Nucleoporin p58/p45hcarbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cy< tokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]Wnuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]P49792RBP2E3 SUMO-protein ligase RanBP2hNPC-cyto filaments Protein modificationSUBCELLULAR LOCATION: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments.'carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; negative regulation of glucokinase activity [GO:0033132]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of gluconeogenesis involved in cellular glucose homeostasis [GO:0090526]; regulation of glucose transport [GO:0010827]; response to amphetamine [GO:0001975]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]ligase activity [GO:0016874]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; Ran GTPase binding [GO:0008536]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore cytoplasmic filaments [GO:0044614]; nuclear pore nuclear basket [GO:0044615]xFUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:22194619}.Q99567NUP88"Nuclear pore complex protein Nup884SUBCELLULAR LOCATION: Nucleus, nuclear pore complex.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; post-translational protein modification [GO:0043687]; protein export from nucleus [GO:0006611]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from nucleus [GO:0000056]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]!transporter activity [GO:0005215]Icytosol [GO:0005829]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]6FUNCTION: Essential component of nuclear pore complex.P35658NU214#Nuclear pore complex protein Nup214PSUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Note=Cytoplasmic filaments.wcarbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; post-translational protein modification [GO:0043687]; protein export from nucleus [GO:0006611]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cell cycle [GO:0051726]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]Vnucleocytoplasmic transporter activity [GO:0005487]; transporter activity [GO:0005215]cytosol [GO:0005829]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]tFUNCTION: May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.P78406RAE1LmRNA export factorcSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9256445}. Nucleus {ECO:0000269|PubMed:9256445}.7carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cellular response to organic cyclic compound [GO:0071407]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA export from nucleus [GO:0006406]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]:microtubule binding [GO:0008017]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nuclear envelope [GO:0005635]; nuclear outer membrane [GO:0005640]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton.P52948NUP98(Nuclear pore complex protein Nup98-Nup96 SUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus, nuclear pore complex. Note=Nup96 is localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; DNA replication [GO:0006260]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0< 007077]; mRNA transport [GO:0051028]; nuclear pore complex assembly [GO:0051292]; nuclear pore organization [GO:0006999]; nucleocytoplasmic transport [GO:0006913]; post-translational protein modification [GO:0043687]; protein import into nucleus, docking [GO:0000059]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]tpeptide binding [GO:0042277]; structural constituent of nuclear pore [GO:0017056]; transporter activity [GO:0005215]cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nuclear pore outer ring [GO:0031080]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Nup98 and Nup96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. {ECO:0000269|PubMed:15229283}.Q9BTX1NDC1Nucleoporin NDC1 hNPC- POMsTRANSMEMSUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.mRNA transport [GO:0051028]; nuclear pore complex assembly [GO:0051292]; nuclear pore distribution [GO:0031081]; protein transport [GO:0015031]; spermatogenesis [GO:0007283]; synapsis [GO:0007129]gcytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]FUNCTION: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. {ECO:0000269|PubMed:16600873, ECO:0000269|PubMed:16702233}.A8CG34P121C/Nuclear envelope pore membrane protein POM 121CSUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.;mRNA transport [GO:0051028]; protein transport [GO:0015031]eendoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]'FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}.Q53GS7GLE1Nucleoporin GLE1hNPC -mRNA exportSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12668658}. Cytoplasm {ECO:0000269|PubMed:12668658}. Note=Shuttles between the nucleus and the cytoplasm. Shuttling is essential for its mRNA export function.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus, nuclear pore complex. Note=Shuttles between the nucleus and the cytoplasm. In the nucleus, isoform 1 localizes to the nuclear pore complex and nuclear envelope. Shuttling is essential for its mRNA export function.umRNA export from nucleus [GO:0006406]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein transport [GO:0015031]&identical protein binding [GO:0042802]cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; nuclear pore [GO:0005643]; plasma membrane [GO:0005886]#FUNCTION: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC). {ECO:0000269|PubMed:12668658, ECO:0000269|PubMed:16000379, ECO:0000269|PubMed:9618489}.Q9NUU7DD19A!ATP-dependent RNA helicase DDX19ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils.umRNA export from nucleus [GO:0006406]; protein transport [GO:0015031]; RNA secondary structure unwinding [GO:0010501]dATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; RNA binding [GO:0003723]:FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (By similarity). {ECO:0000250}.Q9UMR2DD19B!ATP-dependent RNA helicase DDX19BSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear pore complex cytoplasmic fibrils.ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; helicase activity [GO:0004386]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]FUNCTION: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.Q9UBU9NXF1Nuclear RNA export factor 1SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus speckle. Cytoplasm. Nucleus {ECO:0000269|PubMed:25662211}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Nucleus; nuclear rim. {ECO:0000269|PubMed:25662211}._gene expression [GO:0010467]; mRNA export from nucleus [GO:0006406]; viral process [GO:0016032]knucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; single-stranded RNA binding [GO:0003727]`cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. {ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:9660949}.Q9NRG9AAASAladinhNPC-nuclear basketRSUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:19782045}.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; fertilization [GO:0009566]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; learning [GO:0007612]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; nucleocytoplasmic transport [GO:0006913]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; regulation of nucleocytoplasmic transport [GO:0046822]; small molecule < metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]^FUNCTION: Plays a role in the normal development of the peripheral and central nervous system.Q9UKX7NUP50"Nuclear pore complex protein Nup50SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:12802065}. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}. Note=Localizes to the nucleoplasmic fibrils of the nuclear pore complex (By similarity). Dissociates from the NPC structure early during prophase of mitosis. Associates to the newly formed nuclear membrane during telophase. {ECO:0000250}.8carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; intracellular transport [GO:0046907]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]jcytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]FUNCTION: Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling. Interacts with multiple transport receptor proteins including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B. {ECO:0000269|PubMed:20016008}.P49790NU153#Nuclear pore complex protein Nup153SUBCELLULAR LOCATION: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Tightly associated with the nuclear membrane and lamina (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000250}.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mRNA transport [GO:0051028]; negative regulation of RNA export from nucleus [GO:0046832]; nuclear pore complex assembly [GO:0051292]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein transport [GO:0015031]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral entry into host cell [GO:0046718]; viral life cycle [GO:0019058]; viral penetration into host nucleus [GO:0075732]; viral process [GO:0016032]; viral transcription [GO:0019083] DNA binding [GO:0003677]; identical protein binding [GO:0042802]; nucleocytoplasmic transporter activity [GO:0005487]; protein anchor [GO:0043495]; structural constituent of nuclear pore [GO:0017056]; transporter activity [GO:0005215]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; nuclear inclusion body [GO:0042405]; nuclear lamina [GO:0005652]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]:FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}.P12270TPRNucleoprotein TPRmSUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus envelope. Nucleus, nuclear pore complex. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (PubMed:7798308). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase (PubMed:18981471). Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore (PubMed:19273613). Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle. {ECO:0000250, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:7798308}.Scarbohydrate metabolic process [GO:0005975]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cellular response to interferon-alpha [GO:0035457]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; MAPK import into nucleus [GO:0000189]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; mitotic spindle assembly checkpoint [GO:0007094]; mRNA export from nucleus in respons< e to heat stress [GO:0031990]; negative regulation of RNA export from nucleus [GO:0046832]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of translational initiation [GO:0045947]; nuclear pore organization [GO:0006999]; positive regulation of heterochromatin assembly [GO:0031453]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein import into nucleus [GO:0042307]; post-translational protein modification [GO:0043687]; protein import into nucleus [GO:0006606]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; regulation of glucose transport [GO:0010827]; regulation of mitotic sister chromatid separation [GO:0010965]; regulation of mitotic spindle assembly [GO:1901673]; response to epidermal growth factor [GO:0070849]; RNA export from nucleus [GO:0006405]; RNA import into nucleus [GO:0006404]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral transcription [GO:0019083]cchromatin binding [GO:0003682]; dynein complex binding [GO:0070840]; heat shock protein binding [GO:0031072]; mitogen-activated protein kinase binding [GO:0051019]; mRNA binding [GO:0003729]; nucleocytoplasmic transporter activity [GO:0005487]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631]cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; extrinsic component of membrane [GO:0019898]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. According to some authors, plays a limited role in the regulation of nuclear protein export (PubMed:22253824 and PubMed:11952838). Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases. {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:9864356}.P62826RANGTP-binding nuclear protein RanRAN-hNPCSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Melanosome. Nucleus envelope {ECO:0000250|UniProtKB:P62827}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Colocalizes with NEMP1 at the nuclear envelope (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P62827}. actin cytoskeleton organization [GO:0030036]; androgen receptor signaling pathway [GO:0030521]; cell division [GO:0051301]; cellular protein complex localization [GO:0034629]; DNA metabolic process [GO:0006259]; gene expression [GO:0010467]; intracellular transport of virus [GO:0075733]; mitotic nuclear division [GO:0007067]; mitotic spindle organization [GO:0007052]; positive regulation of protein binding [GO:0032092]; positive regulation of transcription, DNA-templated [GO:0045893]; pre-miRNA export from nucleus [GO:0035281]; protein export from nucleus [GO:0006611]; protein import into nucleus [GO:0006606]; protein import into nucleus, translocation [GO:0000060]; protein localization to nucleolus [GO:1902570]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from nucleus [GO:0000056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; viral life cycle [GO:0019058]; viral process [GO:0016032]androgen receptor binding [GO:0050681]; chromatin binding [GO:0003682]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713][centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; recycling endosome [GO:0055037]; RNA nuclear export complex [GO:0042565]ZFUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. {ECO:0000250}.; FUNCTION: Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.P46060RAGP1Ran GTPase-activating protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Cytoplasmic during interphase. Targeted to the nuclear rim after sumoylation. During mitosis, associates with mitotic spindles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation.Qcellular response to peptide hormone stimulus [GO:0071375]; mitotic cell cycle [GO:0000278]; negative regulation of protein export from nucleus [GO:0046826]; positive regulation of GTPase activity [GO:0043547]; response to axon injury [GO:0048678]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]&GTPase activator activity [GO:0005096]Dcondensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; mitotic spindle [GO:0072686]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore cytoplasmic filaments [GO:0044614]; perinuclear region of cytoplasm [GO:004< 8471]; spindle pole [GO:0000922]FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.P43487RANG&Ran-specific GTPase-activating proteinintracellular transport [GO:0046907]; regulation of catalytic activity [GO:0050790]; signal transduction [GO:0007165]; viral process [GO:0016032]yGDP-dissociation inhibitor activity [GO:0005092]; GTPase activator activity [GO:0005096]; Ran GTPase binding [GO:0008536]Kcytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nucleus [GO:0005634][FUNCTION: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.Q9H6Z4RANB3Ran-binding protein 3NPC (42)eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19289081}. Nucleus {ECO:0000269|PubMed:19289081}.Dintracellular transport [GO:0046907]; protein transport [GO:0015031]<Ran GTPase binding [GO:0008536]; R-SMAD binding [GO:0070412]Fcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. {ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268, ECO:0000269|PubMed:11932251, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9637251}.P07305H10 Histone H1.0Histones;SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Note=The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes.apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; nucleosome assembly [GO:0006334]; programmed cell death [GO:0012501]Dchromatin DNA binding [GO:0031490]; poly(A) RNA binding [GO:0044822]actin cytoskeleton [GO:0015629]; Golgi apparatus [GO:0005794]; nuclear chromatin [GO:0000790]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division.P10412H14 Histone H1.4SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome assembly [GO:0006334]; nucleosome positioning [GO:0016584]wextracellular exosome [GO:0070062]; nuclear heterochromatin [GO:0005720]; nucleosome [GO:0000786]; nucleus [GO:0005634]FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.Q92522H1X Histone H1x*SUBCELLULAR LOCATION: Nucleus. Chromosome. nucleosome assembly [GO:0006334]:DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]Enucleolus [GO:0005730]; nucleosome [GO:0000786]; nucleus [GO:0005634]kFUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.Q02539H11 Histone H1.1SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:15911621}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:15911621}. Note=Mainly localizes in euchromatin.>nucleosome assembly [GO:0006334]; spermatogenesis [GO:0007283]"chromatin DNA binding [GO:0031490]Ynuclear chromatin [GO:0000790]; nuclear euchromatin [GO:0005719]; nucleosome [GO:0000786]P16403H12 Histone H1.2SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration.nuclear euchromatin [GO:0005719]; nucleosome [GO:0000786]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]P16402H13 Histone H1.3SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin.P16401H15 Histone H1.5SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to PubMed:15911621 more commonly found in heterochromatin. According to PubMed:10997781 associates with actively transcribed chromatin and not heterochromatin.mchromatin organization [GO:0006325]; establishment of protein localization to chromatin [GO:0071169]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome assembly [GO:0006334]; positive regulation of cell growth [GO:0030307]; positive regulation of histone H3-K9 methylation [GO:0051574]; protein stabilization [GO:0050821]nchromatin DNA binding [GO:0031490]; histone deacetylase binding [GO:0042826]; poly(A) RNA binding [GO:0044822]extracellular exosome [GO:0070062]; nuclear chromatin [GO:0000790]; nuclear heterochromatin [GO:0005720]; nucleosome [GO:0000786]P16104H2AX Histone H2AXHSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24429368}. Chromosome.:cellular response to DNA damage stimulus [GO:0006974]; cellular response to gamma radiation [GO:0071480]; cellular senescence [GO:0090398]; cerebral cortex development [GO:0021987]; DNA damage checkpoint [GO:0000077]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; meiotic cell cycle [GO:0051321]; nucleosome assembly [GO:0006334]; positive regulation of DNA repair [GO:0045739]; response to ionizing radiation [GO:0010212]; spermatogenesis [GO:0007283]; viral process [GO:0016032]udamaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; histone binding [GO:0042393]:condensed nuclear chromosome [GO:0000794]; extracellular exosome [GO:0070062]; male germ cell nucleus [GO:0001673]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork [GO:0005657]; site of double-strand break [GO:0035861]; XY body [GO:0001741]OFUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation. {ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:15201865}.Q93077H2A1CHistone H2A type 1-C6negative regulation of cell proliferation [GO:0008285]DNA binding [GO:0003677]Qextracellular ex< osome [GO:0070062]; nucleosome [GO:0000786]; nucleus [GO:0005634]FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.P20671H2A1DHistone H2A type 1-DQ71UI9H2AV Histone H2A.VFSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division (By similarity). {ECO:0000250}.Q16777H2A2CHistone H2A type 2-CO60814H2B1KHistone H2B type 1-Kantibacterial humoral response [GO:0019731]; chromatin organization [GO:0006325]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO:0002227]; nucleosome assembly [GO:0006334]qextracellular space [GO:0005615]; nuclear nucleosome [GO:0000788]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; FUNCTION: Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.Q8N257H2B3BHistone H2B type 3-BEchromatin organization [GO:0006325]; nucleosome assembly [GO:0006334]Onuclear nucleosome [GO:0000788]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]P68431H31 Histone H3.1bblood coagulation [GO:0007596]; chromatin organization [GO:0006325]; chromatin silencing at rDNA [GO:0000183]; DNA methylation on cytosine [GO:0032776]; DNA replication-dependent nucleosome assembly [GO:0006335]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleosome assembly [GO:0006334]; positive regulation of defense response to virus by host [GO:0002230]; protein heterotetramerization [GO:0051290]; regulation of gene expression, epigenetic [GO:0040029]; regulation of gene silencing [GO:0060968]; small GTPase mediated signal transduction [GO:0007264]6DNA binding [GO:0003677]; histone binding [GO:0042393]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; nuclear chromosome [GO:0000228]; nuclear nucleosome [GO:0000788]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; protein complex [GO:0043234]P84243H33 Histone H3.3blood coagulation [GO:0007596]; brain development [GO:0007420]; chromatin silencing at rDNA [GO:0000183]; DNA methylation on cytosine [GO:0032776]; DNA replication-independent nucleosome assembly [GO:0006336]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleosome assembly [GO:0006334]; positive regulation of cell growth [GO:0030307]; regulation of gene expression, epigenetic [GO:0040029]; response to hormone [GO:0009725]; small GTPase mediated signal transduction [GO:0007264]histone binding [GO:0042393]; nucleosomal DNA binding [GO:0031492]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nuclear chromosome [GO:0000228]; nuclear nucleosome [GO:0000788]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15776021, ECO:0000269|PubMed:16258499}.Q71DI3H32 Histone H3.2cblood coagulation [GO:0007596]; chromatin silencing at rDNA [GO:0000183]; DNA methylation on cytosine [GO:0032776]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleosome assembly [GO:0006334]; regulation of gene expression, epigenetic [GO:0040029]; small GTPase mediated signal transduction [GO:0007264]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]P62805H4 Histone H4 Histones(47)CENP-A containing nucleosome assembly [GO:0034080]; chromatin organization [GO:0006325]; chromatin silencing at rDNA [GO:0000183]; DNA methylation on cytosine [GO:0032776]; DNA replication-dependent nucleosome assembly [GO:0006335]; DNA replication-independent nucleosome assembly [GO:0006336]; gene expression [GO:0010467]; histone H4-K20 demethylation [GO:0035574]; mitotic cell cycle [GO:0000278]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of megakaryocyte differentiation [GO:0045653]; nucleosome assembly [GO:0006334]; protein heterotetramerization [GO:0051290]; regulation of gene expression, epigenetic [GO:0040029]; small GTPase mediated signal transduction [GO:0007264]; telomere maintenance [GO:0000723]DNA binding [GO:0003677]; histone binding [GO:0042393]; histone demethylase activity (H4-K20 specific) [GO:0035575]; poly(A) RNA binding [GO:0044822]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; protein complex [GO:0043234]P25786PSA1Proteasome subunit alpha type-1 Proteasome)SUBCELLULAR LOCATION: Cytoplasm. Nucleus.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-p< rotein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]qendopeptidase activity [GO:0004175]; RNA binding [GO:0003723]; threonine-type endopeptidase activity [GO:0004298]4centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; polysome [GO:0005844]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity). {ECO:0000250}.P25787PSA2Proteasome subunit alpha type-2SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body {ECO:0000250}. Note=Colocalizes with TRIM5 in the cytoplasmic bodies. {ECO:0000250}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; response to virus [GO:0009615]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]Wendopeptidase activity [GO:0004175]; threonine-type endopeptidase activity [GO:0004298]3cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.P25788PSA3Proteasome subunit alpha type-3cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. {ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:17499743}.P25789PSA4Proteasome subunit alpha type-4cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.P28066PSA5Proteasome subunit alpha type-5P60900PSA6Proteasome subunit alpha type-6anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of inflammatory response [GO:0050727]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]endopeptidase acti< vity [GO:0004175]; NF-kappaB binding [GO:0051059]; purine ribonucleoside triphosphate binding [GO:0035639]; RNA binding [GO:0003723]; threonine-type endopeptidase activity [GO:0004298]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myofibril [GO:0030016]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; polysome [GO:0005844]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]; sarcomere [GO:0030017]O14818PSA7Proteasome subunit alpha type-7endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; threonine-type endopeptidase activity [GO:0004298]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229}.P20618PSB1Proteasome subunit beta type-1cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]P49721PSB2Proteasome subunit beta type-28anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; response to organic cyclic compound [GO:0014070]; response to organonitrogen compound [GO:0010243]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]<FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit has a trypsin-like activity.P49720PSB3Proteasome subunit beta type-3:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]2threonine-type endopeptidase activity [GO:0004298]"actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]P28070PSB4Proteasome subunit beta type-4^SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.%anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein< catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]endopeptidase activity [GO:0004175]; lipopolysaccharide binding [GO:0001530]; threonine-type endopeptidase activity [GO:0004298]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. {ECO:0000250, ECO:0000269|PubMed:12097147}.P28074PSB5Proteasome subunit beta type-5anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]XFUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity). {ECO:0000250}.P28072PSB6Proteasome subunit beta type-6cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.Q99436PSB7Proteasome subunit beta type-7SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809, ECO:0000269|PubMed:18549262}. Nucleus {ECO:0000269|PubMed:18549262}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]IFUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity.P28062PSB8Proteasome subunit beta type-8_anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; fat cell differentiation [GO:0045444]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic< process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; spermatoproteasome complex [GO:1990111]FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes. {ECO:0000269|PubMed:16423992, ECO:0000269|PubMed:19443843, ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:8163024}.P28065PSB9Proteasome subunit beta type-9FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. {ECO:0000269|PubMed:8163024}.P40306PSB10Proteasome subunit beta type-10Proteasome(17)>anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cell morphogenesis [GO:0000902]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; humoral immune response [GO:0006959]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell proliferation [GO:0042098]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; spermatoproteasome complex [GO:1990111]gFUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.Q13098CSN1"COP9 signalosome complex subunit 1cSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:9535219}.cell cycle [GO:0007049]; cullin deneddylation [GO:0010388]; inactivation of MAPK activity [GO:0000188]; JNK cascade [GO:0007254]; negative regulation of GTPase activity [GO:0034260]&GTPase inhibitor activity [GO:0005095]KCOP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; nucleus [GO:0005634]FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.P61201CSN2"COP9 signalosome complex subunit 2dSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:10207062}._cell proliferation [GO:0008283]; cullin deneddylation [GO:0010388]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of transcription, DNA-templated [GO:0045892]; signal transduction [GO:0007165]; skeletal muscle cell differentiation [GO:0035914]; transcription from RNA polymerase II promoter [GO:0006366]Xsignal transducer activity [GO:0004871]; transcription corepressor activity [GO:0003714]5COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]FUNCTION: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.Q9UNS2CSN3"COP9 signalosome complex subunit 3cullin deneddylation [GO:0010388]; in utero embryonic development [GO:0001701]; response to light stimulus [GO:0009416]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process [GO:0006511]eCOP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]3FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in vari< ous cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.Q9BT78CSN4"COP9 signalosome complex subunit 4cSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle.Ecullin deneddylation [GO:0010388]; protein deneddylation [GO:0000338]cell junction [GO:0030054]; COP9 signalosome [GO:0008180]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptic vesicle [GO:0008021]FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:9535219}.Q92905CSN5"COP9 signalosome complex subunit 5SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Nuclear localization is diminished in the presence of IFIT3.cullin deneddylation [GO:0010388]; exosomal secretion [GO:1990182]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein deneddylation [GO:0000338]; protein deubiquitination [GO:0016579]; regulation of cell cycle [GO:0051726]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; regulation of JNK cascade [GO:0046328]; transcription from RNA polymerase II promoter [GO:0006366]; translation [GO:0006412]; translational initiation [GO:0006413]metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; transcription coactivator activity [GO:0003713]; translation initiation factor activity [GO:0003743]; ubiquitin-specific protease activity [GO:0004843]cell junction [GO:0030054]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; eukaryotic translation initiation factor 3 complex [GO:0005852]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; synaptic vesicle [GO:0008021]FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}.Q7L5N1CSN6"COP9 signalosome complex subunit 6SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region.=cullin deneddylation [GO:0010388]; viral process [GO:0016032]sCOP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes RFWD2/COP1 through reducing RFWD2 auto-ubiquitination and decelerating RFWD2 turnover rate, hence regulates the ubiquitination of RFWD2 targets. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:21625211, ECO:0000269|PubMed:9535219}.Q9H9Q2CSN7B#COP9 signalosome complex subunit 7b!cullin deneddylation [GO:0010388]OCOP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143}.Q9UBW8CSN7A#COP9 signalosome complex subunit 7a0FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:9535219}.Q99627CSN8"COP9 signalosome complex subunit 8COP9 signalosome complexes(9)activation of NF-kappaB-inducing kinase activity [GO:0007250]; cullin deneddylation [GO:0010388]; negative regulation of cell proliferation [GO:0008285]COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO< :0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]P21399ACOCCytoplasmic aconitate hydrataseTCAcellular iron ion homeostasis [GO:0006879]; citrate metabolic process [GO:0006101]; intestinal absorption [GO:0050892]; post-embryonic development [GO:0009791]; regulation of translation [GO:0006417]; response to iron(II) ion [GO:0010040]; tricarboxylic acid cycle [GO:0006099]4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]FUNCTION: Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding. {ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788}.; FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250}.Q99798ACON"Aconitate hydratase, mitochondrial Carbohydrate metabolism cellular metabolic process [GO:0044237]; citrate metabolic process [GO:0006101]; generation of precursor metabolites and energy [GO:0006091]; isocitrate metabolic process [GO:0006102]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron ion binding [GO:0005506]omitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]`FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000250}.O75390CISYCitrate synthase, mitochondrial+SUBCELLULAR LOCATION: Mitochondrion matrix.carbohydrate metabolic process [GO:0005975]; cellular carbohydrate metabolic process [GO:0044262]; cellular metabolic process [GO:0044237]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]Mcitrate (Si)-synthase activity [GO:0004108]; poly(A) RNA binding [GO:0044822]wextracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]P31040SDHAHSuccinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial]SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.-cellular metabolic process [GO:0044237]; nervous system development [GO:0007399]; oxidation-reduction process [GO:0055114]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; succinate metabolic process [GO:0006105]; tricarboxylic acid cycle [GO:0006099]lflavin adenine dinucleotide binding [GO:0050660]; succinate dehydrogenase (ubiquinone) activity [GO:0008177]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209](FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor. {ECO:0000269|PubMed:20484225}.P21912SDHBGSuccinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; succinate metabolic process [GO:0006105]; tricarboxylic acid cycle [GO:0006099]02 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; succinate dehydrogenase (ubiquinone) activity [GO:0008177]; ubiquinone binding [GO:0048039]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739]FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).P07954FUMH!Fumarate hydratase, mitochondrialrSUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.; SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. cellular metabolic process [GO:0044237]; fumarate metabolic process [GO:0006106]; homeostasis of number of cells within a tissue [GO:0048873]; malate metabolic process [GO:0006108]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099](fumarate hydratase activity [GO:0004333]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; tricarboxylic acid cycle enzyme complex [GO:0045239]*FUNCTION: Also acts as a tumor suppressor.P50213IDH3A;Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialcarbohydrate metabolic process [GO:0005975]; cellular metabolic process [GO:0044237]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]sisocitrate dehydrogenase (NAD+) activity [GO:0004449]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]O43837IDH3B:Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial2-oxoglutarate metabolic process [GO:0006103]; cellular metabolic process [GO:0044237]; isocitrate metabolic process [GO:0006102]; NADH metabolic process [GO:0006734]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]electron carrier activity [GO:0009055]; isocitrate dehydrogenase (NAD+) activity [GO:0004449]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]Smitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]P51553IDH3G;Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11256614}.U2-oxoglutarate metabolic process [GO:0006103]; carbohydrate metabolic process [GO:0005975]; cellular metabolic process [GO:0044237]; isocitrate metabolic process [GO:0006102]; NADH metabolic process [GO:0006734]; negative regulation of growth [GO:0045926]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]ATP binding [GO:0005524]; isocitrate dehydrogenase (NAD+) activity [GO:0004449]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]omitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]O75874IDHC+Isocitrate dehydrogenase [NADP] cytoplasmichSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10521434}. Peroxisome {ECO:0000269|PubMed:10521434}.>2-oxoglutarate metabolic process [GO:0006103]; cellular lipid metabolic process [GO:0044255]; female gonad development [GO:0008585]; glutathione metabolic process [GO:0006749]; glyoxylate cycle [GO:0006097]; isocitrate metabolic process [GO:0006102]; NADPH regeneration [GO:0006740]; regulation of phospholipid biosynthetic process [GO:0071071]; regulation of phospholipid catabolic process [GO:0060696]; response to oxidative stress [GO:0006979]; response to steroid hormone [GO:0048545]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracell< ular exosome [GO:0070062]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]P48735IDHP.Isocitrate dehydrogenase [NADP], mitochondrial#2-oxoglutarate metabolic process [GO:0006103]; carbohydrate metabolic process [GO:0005975]; cellular metabolic process [GO:0044237]; glyoxylate cycle [GO:0006097]; isocitrate metabolic process [GO:0006102]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]tisocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.P40925MDHC!Malate dehydrogenase, cytoplasmicactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; positive regulation of defense response to virus by host [GO:0002230]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]diiodophenylpyruvate reductase activity [GO:0047860]; L-malate dehydrogenase activity [GO:0030060]; malic enzyme activity [GO:0004470]; NAD binding [GO:0051287]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]P40926MDHM#Malate dehydrogenase, mitochondrialcarbohydrate metabolic process [GO:0005975]; cellular metabolic process [GO:0044237]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; internal protein amino acid acetylation [GO:0006475]; malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase (NADP+) activity [GO:0046554]; poly(A) RNA binding [GO:0044822]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q02218ODO1+2-oxoglutarate dehydrogenase, mitochondrialcellular metabolic process [GO:0044237]; cellular nitrogen compound metabolic process [GO:0034641]; cerebellar cortex development [GO:0021695]; generation of precursor metabolites and energy [GO:0006091]; glycolytic process [GO:0006096]; hippocampus development [GO:0021766]; lysine catabolic process [GO:0006554]; olfactory bulb mitral cell layer development [GO:0061034]; pyramidal neuron development [GO:0021860]; small molecule metabolic process [GO:0044281]; striatum development [GO:0021756]; tangential migration from the subventricular zone to the olfactory bulb [GO:0022028]; thalamus development [GO:0021794]; tricarboxylic acid cycle [GO:0006099]metal ion binding [GO:0046872]; oxoglutarate dehydrogenase (NAD+) activity [GO:0034602]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976]mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; oxoglutarate dehydrogenase complex [GO:0045252]*FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).P53597SUCABSuccinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialcellular metabolic process [GO:0044237]; small molecule metabolic process [GO:0044281]; succinate metabolic process [GO:0006105]; succinyl-CoA metabolic process [GO:0006104]; tricarboxylic acid cycle [GO:0006099]cofactor binding [GO:0048037]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; succinate-CoA ligase complex (GDP-forming) [GO:0045244]FUNCTION: Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). {ECO:0000250}.Q9P2R7SUCB1=Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrialcellular metabolic process [GO:0044237]; small molecule metabolic process [GO:0044281]; succinate metabolic process [GO:0006105]; succinyl-CoA metabolic process [GO:0006104]; succinyl-CoA pathway [GO:0006781]; tricarboxylic acid cycle [GO:0006099]rATP binding [GO:0005524]; metal ion binding [GO:0046872]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]}extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]hFUNCTION: Catalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA. {ECO:0000250}.Q96I99SUCB2=Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrialTCAs(17)cellular metabolic process [GO:0044237]; small molecule metabolic process [GO:0044281]; succinyl-CoA metabolic process [GO:0006104]; tricarboxylic acid cycle [GO:0006099]lATP binding [GO:0005524]; GTP binding [GO:0005525]; succinate-CoA ligase (GDP-forming) activity [GO:0004776][mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]hFUNCTION: Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA. {ECO:0000250}.P03891NU2M&NADH-ubiquinone oxidoreductase chain 2Complex I -corePSUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein.cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; reactive oxygen species metabolic process [GO:0072593]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]5NADH dehydrogenase (ubiquinone) activity [GO:0008137]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; postsynaptic density [GO:0014069]qFUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.P03897NU3M&NADH-ubiquinone oxidoreductase chain 3fSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.\cellular metabolic process [GO:0044237]; cellular response to glucocorticoid stimulus [GO:0071385]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; response to light intensity [GO:0009642]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]P03915NU5M&NADH-ubiquinone oxidoreductase chain 5lSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.Lcellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]< ; respiratory electron transport chain [GO:0022904]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to organonitrogen compound [GO:0010243]; small molecule metabolic process [GO:0044281]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; neuron projection [GO:0043005]O43678NDUA2<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2Complex I-accessorycellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]?FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.O95167NDUA3<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3QSUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein.integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]O00483NDUA4#Cytochrome c oxidase subunit NDUFA4SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23746447}; Peripheral membrane protein {ECO:0000269|PubMed:23746447}; Matrix side {ECO:0000269|PubMed:23746447}.cellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281][NADH dehydrogenase (ubiquinone) activity [GO:0008137]; protein complex binding [GO:0032403]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]FUNCTION: Cytochrome c oxidase (COX, complex IV) is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. Required for complex IV maintenance. {ECO:0000269|PubMed:22902835}.Q16718NDUA5<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5amitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]P56556NDUA6<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]?FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.O95182NDUA7<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial translation [GO:0032543]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]fNADH dehydrogenase (ubiquinone) activity [GO:0008137]; structural constituent of ribosome [GO:0003735]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial ribosome [GO:0005761]P51970NDUA8<NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21310150}; Peripheral membrane protein {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space {ECO:0000269|PubMed:21310150}.mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]Q16795NDUA9KNADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrialcellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; sodium ion transport [GO:0006814]; ubiquinone-6 biosynthetic process [GO:1901006]coenzyme binding [GO:0050662]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]; protein complex binding [GO:0032403]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; nucleus [GO:0005634]O95299NDUAALNADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrialcellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; response to drug [GO:0042493]; small molecule metabolic process [GO:0044281]xATP binding [GO:0005524]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; nucleoside kinase activity [GO:0019206]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; myelin sheath [GO:0043209]Q86Y39NDUAB=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.cellular metabolic process [GO:0044237]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]^FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). {ECO:0000250}.Q9UI09NDUAC=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12cellular metabolic process [GO:0044237]; respiratory electron transport chain [GO:0022904]; respiratory gaseous exchange [GO:0007585]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]]electron carrier activity [GO:0009055]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]Q9P0J0NDUAD=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. Nucleus. Note=May be translocated into the nucleus upon IFN/RA treatment.+apoptotic signaling pathway [GO:0097190]; cellular metabolic process [GO:0044237]; cellular response to interferon-beta [GO:0035458]; cellular response to retinoic acid [GO:0071300]; negative regulation of cell growth [GO:0030308]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of peptidase activity [GO:0010952]; positive regulation of protein catabolic process [GO:0045732]; protein import into mitochondrial inner membrane [GO:0045039]; reactive oxygen species metabolic process [GO:0072593]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]yATP binding [GO:0005524]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase a< ctivity [GO:0003954]Scytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain [GO:0005746]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes. {ECO:0000269|PubMed:12628925, ECO:0000269|PubMed:12867595, ECO:0000269|PubMed:15753091}.O14561ACPM#Acyl carrier protein, mitochondrialcellular metabolic process [GO:0044237]; fatty acid biosynthetic process [GO:0006633]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; protein lipoylation [GO:0009249]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process [GO:0000036]; calcium ion binding [GO:0005509]; fatty acid binding [GO:0005504]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]AFUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity). {ECO:0000250}.O75438NDUB1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1^SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]O43676NDUB3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3O95168NDUB4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]O43674NDUB5JNADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrialintegral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]O95139NDUB6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]P17568NDUB7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7O95169NDUB8JNADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrialendoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]Q9Y6M9NDUB9;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9Hactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; sensory perception of sound [GO:0007605]; small molecule metabolic process [GO:0044281]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]O96000NDUBA<NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]Q9NX14NDUBBKNADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrialmSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.O95298NDUC2,NADH dehydrogenase [ubiquinone] 1 subunit C2cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]P28331NDUS1<NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial3SUBCELLULAR LOCATION: Mitochondrion inner membrane.apoptotic mitochondrial changes [GO:0008637]; ATP metabolic process [GO:0046034]; cellular metabolic process [GO:0044237]; cellular respiration [GO:0045333]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; reactive oxygen species metabolic process [GO:0072593]; regulation of mitochondrial membrane potential [GO:0051881]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron carrier activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]$FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. {ECO:0000250}.O75306NDUS2DNADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial4 iron, 4 sulfur cluster binding [GO:0051539]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; quinone binding [GO:0048038]; ubiquitin protein ligase binding [GO:0031625]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]O75489NDUS3DNADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrialcellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; negative regulation of cell growth [GO:0030308]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; reactive oxygen species metabolic process [GO:0072593]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]electron carrier activity [GO:0009055]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]O43181NDUS4DNADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial< ?brain development [GO:0007420]; cAMP-mediated signaling [GO:0019933]; cellular metabolic process [GO:0044237]; cellular respiration [GO:0045333]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; positive regulation of fibroblast proliferation [GO:0048146]; reactive oxygen species metabolic process [GO:0072593]; regulation of protein phosphorylation [GO:0001932]; respiratory electron transport chain [GO:0022904]; response to cAMP [GO:0051591]; small molecule metabolic process [GO:0044281]}mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]O43920NDUS55NADH dehydrogenase [ubiquinone] iron-sulfur protein 5SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Mitochondrion intermembrane space {ECO:0000305}. cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]O75380NDUS6DNADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrialcardiovascular system development [GO:0072358]; cellular metabolic process [GO:0044237]; fatty acid metabolic process [GO:0006631]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrion morphogenesis [GO:0070584]; multicellular organismal aging [GO:0010259]; multicellular organism growth [GO:0035264]; muscle contraction [GO:0006936]; reproductive system development [GO:0061458]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]O75251NDUS7DNADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; quinone binding [GO:0048038]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; synaptic membrane [GO:0097060]O00217NDUS8DNADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial8cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; respiratory electron transport chain [GO:0022904]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone. {ECO:0000250}.P49821NDUV1=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrialaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; FMN binding [GO:0010181]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]P19404NDUV2=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial%cardiac muscle tissue development [GO:0048738]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; nervous system development [GO:0007399]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]2 iron, 2 sulfur cluster binding [GO:0051537]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]Q9Y375CIA30;Complex I intermediate-associated protein 30, mitochondrialhmitochondrial electron transport, NADH to ubiquinone [GO:0006120]; protein complex assembly [GO:0006461]%unfolded protein binding [GO:0051082]Ncytoplasm [GO:0005737]; mitochondrial respiratory chain complex I [GO:0005747]FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000250}.Q16762THTRThiosulfate sulfurtransferase Complex I(47)cellular nitrogen compound metabolic process [GO:0034641]; cyanate catabolic process [GO:0009440]; epithelial cell differentiation [GO:0030855]; rRNA import into mitochondrion [GO:0035928]; rRNA transport [GO:0051029]; small molecule metabolic process [GO:0044281]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]; sulfur amino acid catabolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]Q5S rRNA binding [GO:0008097]; thiosulfate sulfurtransferase activity [GO:0004792]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA. {ECO:0000250, ECO:0000269|PubMed:20663881, ECO:0000269|PubMed:21685364}.Q99643C560>Succinate dehydrogenase cytochrome b560 subunit, mitochondrial Complex IIDaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; oxidation-reduction process [GO:0055114]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]electron carrier activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; succinate dehydrogenase activity [GO:0000104]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739]; respiratory chain complex II [GO:0045273]FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).O14521DHSDNSuccinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial Complex II(4)cellular metabolic process [GO:0044237]; cellular response to hypoxia [GO:0071456]; regulation of catecholamine secretion [GO:0050433]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]electron carrier activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; succinate dehydrogenase activity [GO:0000104]; ubiquinone binding [GO:0048039]integral component of membrane [GO:0016021]; mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; mitochondrion [GO:0005739]FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is< involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000250}.P08574CY1*Cytochrome c1, heme protein, mitochondrial Complex IIIeSUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side.cellular metabolic process [GO:0044237]; respiratory electron transport chain [GO:0022904]; response to glucagon [GO:0033762]; small molecule metabolic process [GO:0044281]electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity [GO:0045155]; heme binding [GO:0020037]; metal ion binding [GO:0046872]integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; respiratory chain [GO:0070469]FUNCTION: This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain.P00156CYB Cytochrome bcellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; hyperosmotic salinity response [GO:0042538]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; organ regeneration [GO:0031100]; respiratory electron transport chain [GO:0022904]; response to cadmium ion [GO:0046686]; response to calcium ion [GO:0051592]; response to cobalamin [GO:0033590]; response to copper ion [GO:0046688]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to glucagon [GO:0033762]; response to heat [GO:0009408]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to mercury ion [GO:0046689]; response to toxic substance [GO:0009636]; small molecule metabolic process [GO:0044281]~electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. {ECO:0000250}.P31930QCR10Cytochrome b-c1 complex subunit 1, mitochondrialaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidation-reduction process [GO:0055114]; oxidative phosphorylation [GO:0006119]; protein processing [GO:0016485]; respiratory electron transport chain [GO:0022904]; response to activity [GO:0014823]; response to alkaloid [GO:0043279]; small molecule metabolic process [GO:0044281]metalloendopeptidase activity [GO:0004222]; ubiquinol-cytochrome-c reductase activity [GO:0008121]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.P22695QCR20Cytochrome b-c1 complex subunit 2, mitochondrial>aerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidative phosphorylation [GO:0006119]; protein processing [GO:0016485]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]Imetalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex.P07919QCR60Cytochrome b-c1 complex subunit 6, mitochondrialzaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidation-reduction process [GO:0055114]; oxidative phosphorylation [GO:0006119]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]6ubiquinol-cytochrome-c reductase activity [GO:0008121]smitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]; mitochondrion [GO:0005739]P14927QCR7!Cytochrome b-c1 complex subunit 7Gaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; oxidation-reduction process [GO:0055114]; oxidative phosphorylation [GO:0006119]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]; mitochondrial respiratory chain complex III [GO:0005750]FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping.O14949QCR8!Cytochrome b-c1 complex subunit 8cellular metabolic process [GO:0044237]; cerebellar Purkinje cell layer development [GO:0021680]; hippocampus development [GO:0021766]; hypothalamus development [GO:0021854]; midbrain development [GO:0030901]; pons development [GO:0021548]; pyramidal neuron development [GO:0021860]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; subthalamus development [GO:0021539]; thalamus development [GO:0021794]emitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; respiratory chain [GO:0070469]FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit, together with cytochrome b, binds to ubiquinone.Q9UDW1QCR9!Cytochrome b-c1 complex subunit 9ASUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.cellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1 (By similarity). {ECO:0000250}.P47985UCRI5Cytochrome b-c1 complex subunit Rieske, mitochondrialComplex III(10)cellular metabolic process [GO:0044237]; respiratory electron transport chain [GO:0022904]; response to antibiotic [GO:0046677]; response to drug [GO:0042493]; response to hormone [GO:0009725]; small molecule metabolic process [GO:0044281]2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]uFUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex < III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.; FUNCTION: The transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex. {ECO:0000250}.P13073COX417Cytochrome c oxidase subunit 4 isoform 1, mitochondrial Complex IVaerobic respiration [GO:0009060]; cellular metabolic process [GO:0044237]; gene expression [GO:0010467]; generation of precursor metabolites and energy [GO:0006091]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; respiratory electron transport chain [GO:0022904]; response to nutrient [GO:0007584]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]*cytochrome-c oxidase activity [GO:0004129]extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.P20674COX5A.Cytochrome c oxidase subunit 5A, mitochondrialhcellular metabolic process [GO:0044237]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]rcytochrome-c oxidase activity [GO:0004129]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex IV [GO:0005751]; myelin sheath [GO:0043209]FUNCTION: This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.P10606COX5B.Cytochrome c oxidase subunit 5B, mitochondrialLcellular metabolic process [GO:0044237]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; respiratory electron transport chain [GO:0022904]; respiratory gaseous exchange [GO:0007585]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]Jcytochrome-c oxidase activity [GO:0004129]; metal ion binding [GO:0046872]iextracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]P12074CX6A1/Cytochrome c oxidase subunit 6A1, mitochondrial+cellular metabolic process [GO:0044237]; gene expression [GO:0010467]; generation of precursor metabolites and energy [GO:0006091]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]bmitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex IV [GO:0005751]P14854CX6B1 Cytochrome c oxidase subunit 6B1FSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}.Lcellular metabolic process [GO:0044237]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]; transcription initiation from RNA polymerase II promoter [GO:0006367]umitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739][FUNCTION: Connects the two COX monomers into the physiological dimeric form. {ECO:0000250}.P09669COX6CCytochrome c oxidase subunit 6Crintegral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]P14406CX7A2/Cytochrome c oxidase subunit 7A2, mitochondrialPextracellular exosome [GO:0070062]; mitochondrial respiratory chain [GO:0005746]P24310CX7A1/Cytochrome c oxidase subunit 7A1, mitochondrialngeneration of precursor metabolites and energy [GO:0006091]; hydrogen ion transmembrane transport [GO:1902600]uintegral component of membrane [GO:0016021]; mitochondrial respiratory chain [GO:0005746]; mitochondrion [GO:0005739]O14548COX7R>Cytochrome c oxidase subunit 7A-related protein, mitochondrial!cellular metabolic process [GO:0044237]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]Wmitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]FUNCTION: Involved in the regulation of oxidative phosphorylation and energy metabolism (By similarity). Necessary for the assembly of mitochondrial respiratory supercomplex (By similarity). {ECO:0000250|UniProtKB:Q61387}.P15954COX7C.Cytochrome c oxidase subunit 7C, mitochondrialP24311COX7B.Cytochrome c oxidase subunit 7B, mitochondrialRcellular metabolic process [GO:0044237]; central nervous system development [GO:0007417]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]FUNCTION: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Plays a role in proper central nervous system (CNS) development in vertebrates. {ECO:0000269|PubMed:23122588}.P10176COX8A.Cytochrome c oxidase subunit 8A, mitochondrialactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cellular metabolic process [GO:0044237]; gene expression [GO:0010467]; generation of precursor metabolites and energy [GO:0006091]; hydrogen ion transmembrane transport [GO:1902600]; positive regulation of defense response to virus by host [GO:0002230]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]Vintegral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]P00403COX2Cytochrome c oxidase subunit 2cellular metabolic process [GO:0044237]; gene expression [GO:0010467]; hydrogen ion transmembrane transport [GO:1902600]; lactation [GO:0007595]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; respiratory electron transport chain [GO:0022904]; response to cold [GO:0009409]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]Kcopper ion binding [GO:0005507]; cytochrome-c oxidase activity [GO:0004129]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277]AFUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.P99999CYC Cytochrome cComplex IV(18)iSUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; ATP synthesis coupled electron transport [GO:0042773]; cellular metabolic process [GO:00442< 37]; cellular respiration [GO:0045333]; dephosphorylation [GO:0016311]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway [GO:0097193]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; programmed cell death [GO:0012501]; respiratory electron transport chain [GO:0022904]; response to reactive oxygen species [GO:0000302]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]; respiratory chain [GO:0070469]FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.P00846ATP6ATP synthase subunit a F0 motor- Aaging [GO:0007568]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; respiratory electron transport chain [GO:0022904]; response to hyperoxia [GO:0055093]; small molecule metabolic process [GO:0044281]mhydrogen ion transmembrane transporter activity [GO:0015078]; transmembrane transporter activity [GO:0022857] extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; proton-transporting ATP synthase complex, coupling factor F(o) [GO:0045263]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.P24539AT5F13ATP synthase F(0) complex subunit B1, mitochondrial F0 motor- BBSUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.,ATP synthesis coupled proton transport [GO:0015986]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.P05496AT5G13ATP synthase F(0) complex subunit C1, mitochondrial F0 motor- CJSUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein.ATP hydrolysis coupled proton transport [GO:0015991]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]{hydrogen ion transmembrane transporter activity [GO:0015078]; lipid binding [GO:0008289]; transporter activity [GO:0005215]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrion [GO:0005739]; proton-transporting ATP synthase complex, coupling factor F(o) [GO:0045263]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.O75947ATP5H%ATP synthase subunit d, mitochondrial F0 motor- Dcellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281];cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]P56385ATP5I%ATP synthase subunit e, mitochondrial F0 motor- Emitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.P56134ATPK%ATP synthase subunit f, mitochondrial F0 motor- F2|SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; proton transport [GO:0015992]; respiratory electron transport chain [GO:0022904]; small molecule metabolic< process [GO:0044281]/transmembrane transporter activity [GO:0022857]0extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; nucleus [GO:0005634]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.P18859ATP5J-ATP synthase-coupling factor 6, mitochondrial F0 motor- F6cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]hydrogen ion transmembrane transporter activity [GO:0015078]; transmembrane transporter activity [GO:0022857]; transporter activity [GO:0005215]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.O75964ATP5L%ATP synthase subunit g, mitochondrial F0 motor- G extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]P03928ATP8ATP synthase protein 8 F0 motor- G8KSUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein.integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}.P48047ATPO%ATP synthase subunit O, mitochondrialF0 motor -O-F1-F0 connector^SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.ATP biosynthetic process [GO:0006754]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; proton transport [GO:0015992]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]drug binding [GO:0008144]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]; transporter activity [GO:0005215]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.P25705ATPA)ATP synthase subunit alpha, mitochondrial F1 motor- A3SUBCELLULAR LOCATION: Mitochondrion inner membrane. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Colocalizes with HRG on the cell surface of T-cells.ATP biosynthetic process [GO:0006754]; ATP hydrolysis coupled proton transport [GO:0015991]; cellular metabolic process [GO:0044237]; embryo development [GO:0009790]; lipid metabolic process [GO:0006629]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; negative regulation of endothelial cell proliferation [GO:0001937]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]+ATP binding [GO:0005524]; MHC class I protein binding [GO:0042288]; poly(A) RNA binding [GO:0044822]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]nextracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). {ECO:0000250}.P06576ATPB(ATP synthase subunit beta, mitochondrial F1 motor-B3dSUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.angiogenesis [GO:0001525]; ATP biosynthetic process [GO:0006754]; ATP hydrolysis coupled proton transport [GO:0015991]; cellular metabolic process [GO:0044237]; generation of p< recursor metabolites and energy [GO:0006091]; lipid metabolic process [GO:0006629]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; mitochondrion organization [GO:0007005]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; organelle organization [GO:0006996]; osteoblast differentiation [GO:0001649]; proton transport [GO:0015992]; regulation of intracellular pH [GO:0051453]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281],ATP binding [GO:0005524]; MHC class I protein binding [GO:0042288]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]; transporter activity [GO:0005215]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase, catalytic core [GO:0005754]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]9FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.P36542ATPG)ATP synthase subunit gamma, mitochondrial F1 motor-C1{SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.ATP biosynthetic process [GO:0006754]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; oxidative phosphorylation [GO:0006119]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]poly(A) RNA binding [GO:0044822]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]^extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) [GO:0000275]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.P30049ATPD)ATP synthase subunit delta, mitochondrial F1 motor-D1uATP biosynthetic process [GO:0006754]; ATP synthesis coupled proton transport [GO:0015986]; cellular metabolic process [GO:0044237]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; oxidative phosphorylation [GO:0006119]; respiratory electron transport chain [GO:0022904]; response to copper ion [GO:0046688]; small molecule metabolic process [GO:0044281]proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]; transporter activity [GO:0005215]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) [GO:0000275]; mitochondrion [GO:0005739]eFUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.P56381ATP5E+ATP synthase subunit epsilon, mitochondrial F1 motor-E1proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; transmembrane transporter activity [GO:0022857]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) [GO:0000275]FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). {ECO:0000250}.Q9UII2ATIF1ATPase inhibitor, mitochondrialIF1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12110673}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; angiogenesis [GO:0001525]; erythrocyte differentiation [GO:0030218]; generation of precursor metabolites and energy [GO:0006091]; heme biosynthetic process [GO:0006783]; mitochondrial depolarization [GO:0051882]; negative regulation of ATPase activity [GO:0032780]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of hydrolase activity [GO:0051346]; negative regulation of nucleotide metabolic process [GO:0045980]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of proteolysis involved in cel< lular protein catabolic process [GO:1903052]; protein homooligomerization [GO:0051260]; protein homotetramerization [GO:0051289]; reactive oxygen species metabolic process [GO:0072593]; regulation of ATP metabolic process [GO:1903578]; regulation of protein targeting to mitochondrion [GO:1903214]angiostatin binding [GO:0043532]; ATPase binding [GO:0051117]; ATPase inhibitor activity [GO:0042030]; calmodulin binding [GO:0005516]; enzyme inhibitor activity [GO:0004857]; protein homodimerization activity [GO:0042803]5cell surface [GO:0009986]; mitochondrion [GO:0005739]FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme. {ECO:0000269|PubMed:12110673, ECO:0000269|PubMed:15528193, ECO:0000269|PubMed:19559621, ECO:0000269|PubMed:23135403}.Q5TC12ATPF17ATP synthase mitochondrial F1 complex assembly factor 1 F1 complex AF1 1%protein complex assembly [GO:0006461]mitochondrion [GO:0005739]hFUNCTION: May play an essential role for the assembly of the mitochondrial F1-F0 complex. {ECO:0000250}.Q8N5M1ATPF27ATP synthase mitochondrial F1 complex assembly factor 2 F1 complex AF 2>proton-transporting ATP synthase complex assembly [GO:0043461]6mitochondrion [GO:0005739]; nuclear speck [GO:0016607]FUNCTION: May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase). {ECO:0000269|PubMed:11410595}.P5637868MP!6.8 kDa mitochondrial proteolipid MLQ ProteinSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.pintegral component of membrane [GO:0016021]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]Q96IX5USMG54Up-regulated during skeletal muscle growth protein 5DAPITgSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]zFUNCTION: Plays a critical role in maintaining the ATP synthase population in mitochondria. {ECO:0000269|PubMed:21345788}.Q15904VAS1V-type proton ATPase subunit S1V1-S1 (optional)aSUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.ATP hydrolysis coupled proton transport [GO:0015991]; cellular iron ion homeostasis [GO:0006879]; establishment of organelle localization [GO:0051656]; insulin receptor signaling pathway [GO:0008286]; ion transmembrane transport [GO:0034220]; pH reduction [GO:0045851]; positive regulation of bone resorption [GO:0045780]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exocytosis [GO:0045921]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoclast development [GO:2001206]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; Rab GTPase binding [GO:0017137]; transporter activity [GO:0005215]endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; proton-transporting two-sector ATPase complex [GO:0016469]; proton-transporting V-type ATPase, V1 domain [GO:0033180]; vacuolar membrane [GO:0005774]FUNCTION: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}.P38606VATA(V-type proton ATPase catalytic subunit AV1-AATP hydrolysis coupled proton transport [GO:0015991]; ATP metabolic process [GO:0046034]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; transport [GO:0006810]`ATP binding [GO:0005524]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; microvillus [GO:0005902]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; proton-transporting two-sector ATPase complex [GO:0016469]; proton-transporting V-type ATPase, V1 domain [GO:0033180]FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.P21281VATB2-V-type proton ATPase subunit B, brain isoformV1-B2SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Melanosome. Note=Endomembrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.ATP hydrolysis coupled proton transport [GO:0015991]; ATP metabolic process [GO:0046034]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; hydrogen ion transmembrane transporter activity [GO:0015078]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]cytosol [GO:0005829]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; proton-transporting V-type ATPase, V1 domain [GO:0033180]; ruffle [GO:0001726]FUNCTION: Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.P21283VATC1 V-type proton ATPase subunit C 1V1-C1kATP hydrolysis coupled proton transport [GO:0015991]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]hydrogen-exporting ATPase activity, phosphorylative mechanism [GO:0008553]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; transporter activity [GO:0005215]2apical part of cell [GO:0045177]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; proton-transporting two-sector ATPase complex [GO:0016469]; proton-transporting V-type ATPase, V1 domain [GO:0033180]9FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.Q9Y5K8VATDV-type proton ATPase subunit DV1-DSUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:21844891}; Peripheral membrane protein {ECO:0000305|PubMed:21844891}; Cytoplasmic side {ECO:0000305|PubMed:< 21844891}. Note=Localizes to centrosome and the base of the cilium.cellular iron ion homeostasis [GO:0006879]; cilium assembly [GO:0042384]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; protein localization to cilium [GO:0061512]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]MATPase activity, coupled to transmembrane movement of substances [GO:0042626]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; proton-transporting V-type ATPase complex [GO:0033176]FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. {ECO:0000250, ECO:0000269|PubMed:21844891}.P36543VATE1 V-type proton ATPase subunit E 1V1-E1ATPase binding [GO:0051117]; hydrogen-exporting ATPase activity, phosphorylative mechanism [GO:0008553]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]Uapical plasma membrane [GO:0016324]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; microvillus [GO:0005902]; mitochondrion [GO:0005739]; proton-transporting two-sector ATPase complex [GO:0016469]; proton-transporting two-sector ATPase complex, catalytic domain [GO:0033178]FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.Q16864VATFV-type proton ATPase subunit FV1-FATPase activity, coupled to transmembrane movement of ions [GO:0042625]; ATPase activity, uncoupled [GO:0042624]; hydrogen ion transmembrane transporter activity [GO:0015078]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; proton-transporting two-sector ATPase complex [GO:0016469]; proton-transporting V-type ATPase, V1 domain [GO:0033180]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]O75348VATG1 V-type proton ATPase subunit G 1V1-G1cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]gATPase binding [GO:0051117]; hydrogen-exporting ATPase activity, phosphorylative mechanism [GO:0008553]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.Q9UI12VATHV-type proton ATPase subunit HV1-HATP hydrolysis coupled proton transport [GO:0015991]; cellular iron ion homeostasis [GO:0006879]; endocytosis [GO:0006897]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; regulation of catalytic activity [GO:0050790]; regulation of defense response to virus by virus [GO:0050690]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035]; viral process [GO:0016032]nenzyme regulator activity [GO:0030234]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase, V1 domain [GO:0000221]FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes. {ECO:0000250}.Q93050VPP10V-type proton ATPase 116 kDa subunit a isoform 1 V0 motor--a1SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane protein. Melanosome. Note=Coated vesicle. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.ATP hydrolysis coupled proton transport [GO:0015991]; ATP synthesis coupled proton transport [GO:0015986]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; toxin transport [GO:1901998]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]cATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; nucleoplasm [GO:0005654]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]FUNCTION: Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity). {ECO:0000250}.Q9Y487VPP20V-type proton ATPase 116 kDa subunit a isoform 2 V0 motor--a2SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome membrane. Note=In kidney proximal tubules, also detected in subapical vesicles. {ECO:0000250}.ATP hydrolysis coupled proton transport [GO:0015991]; ATP synthesis coupled proton transport [GO:0015986]; cellular iron ion homeostasis [GO:0006879]; immune response [GO:0006955]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]FUNCTION: Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. {ECO:0000269|PubMed:16415858, ECO:0000269|PubMed:18157129}.Q13488VPP30V-type proton ATPase 116 kDa subunit a isoform 3 V0 motor--a3XSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.oATP hydrolysis coupled proton transport [GO:0015991]; ATP synthesis coupled proton transport [GO:0015986]; cellular defense response [GO:0006968]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interactio< n with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; positive regulation of cell proliferation [GO:0008284]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]; transporter activity [GO:0005215]apical plasma membrane [GO:0016324]; endosome membrane [GO:0010008]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]FUNCTION: Part of the proton channel of V-ATPases (By similarity). Seems to be directly involved in T-cell activation. {ECO:0000250}.P27449VATL/V-type proton ATPase 16 kDa proteolipid subunit V0 motor--cDSUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.ATP hydrolysis coupled proton transport [GO:0015991]; cellular iron ion homeostasis [GO:0006879]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; phagosome maturation [GO:0090382]; positive regulation of Wnt signaling pathway [GO:0030177]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; viral process [GO:0016032]proton-transporting ATPase activity, rotational mechanism [GO:0046961]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; ubiquitin protein ligase binding [GO:0031625]endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; phagocytic vesicle membrane [GO:0030670]; proton-transporting V-type ATPase, V0 domain [GO:0033179]FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.P61421VA0D1 V-type proton ATPase subunit d 1 V0 motor--d1NATP hydrolysis coupled proton transport [GO:0015991]; brain development [GO:0007420]; cellular iron ion homeostasis [GO:0006879]; cellular protein metabolic process [GO:0044267]; cilium assembly [GO:0042384]; endoplasmic reticulum unfolded protein response [GO:0030968]; insulin receptor signaling pathway [GO:0008286]; interaction with host [GO:0051701]; ion transmembrane transport [GO:0034220]; IRE1-mediated unfolded protein response [GO:0036498]; phagosome maturation [GO:0090382]; proton transport [GO:0015992]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]Jhydrogen-exporting ATPase activity, phosphorylative mechanism [GO:0008553]apical plasma membrane [GO:0016324]; axon terminus [GO:0043679]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670]; proton-transporting V-type ATPase, V0 domain [GO:0033179]; synaptic vesicle [GO:0008021]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]FUNCTION: Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). {ECO:0000250}.P05023AT1A14Sodium/potassium-transporting ATPase subunit alpha-1Na-Kteansporting ATPaseSUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.cardiac muscle contraction [GO:0060048]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular potassium ion homeostasis [GO:0030007]; cellular response to mechanical stimulus [GO:0071260]; cellular response to steroid hormone stimulus [GO:0071383]; cellular sodium ion homeostasis [GO:0006883]; ion transmembrane transport [GO:0034220]; membrane hyperpolarization [GO:0060081]; membrane repolarization [GO:0086009]; membrane repolarization during cardiac muscle cell action potential [GO:0086013]; negative regulation of glucocorticoid biosynthetic process [GO:0031947]; negative regulation of heart contraction [GO:0045822]; positive regulation of heart contraction [GO:0045823]; positive regulation of striated muscle contraction [GO:0045989]; potassium ion import [GO:0010107]; potassium ion import across plasma membrane [GO:1990573]; regulation of blood pressure [GO:0008217]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of sodium ion transport [GO:0002028]; regulation of the force of heart contraction [GO:0002026]; relaxation of cardiac muscle [GO:0055119]; response to drug [GO:0042493]; response to glycoside [GO:1903416]; sodium ion export from cell [GO:0036376]; transmembrane transport [GO:0055085]ADP binding [GO:0043531]; ATP binding [GO:0005524]; chaperone binding [GO:0051087]; phosphatase activity [GO:0016791]; potassium ion binding [GO:0030955]; sodium:potassium-exchanging ATPase activity [GO:0005391]; sodium ion binding [GO:0031402]; steroid hormone binding [GO:1990239]napical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intercalated disc [GO:0014704]; melanosome [GO:0042470]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315]GFUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.P13637AT1A34Sodium/potassium-transporting ATPase subunit alpha-3{SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein {ECO:0000269|PubMed:7711835}.iadult locomotory behavior [GO:0008344]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular potassium ion homeostasis [GO:0030007]; cellular response to steroid hormone stimulus [GO:0071383]; cellular sodium ion homeostasis [GO:0006883]; ionotropic glutamate receptor signaling pathway [GO:0035235]; ion transmembrane transport [GO:0034220]; memory [GO:0007613]; potassium ion import [GO:0010107]; response to drug [GO:0042493]; response to glycoside [GO:1903416]; sodium ion export from cell [GO:0036376]; transmembrane transport [GO:0055085]; visual learning [GO:0008542]ATP binding [GO:0005524]; chaperone binding [GO:0051087]; metal ion binding [GO:0046872]; sodium:potassium-exchanging ATPase activity [GO:0005391]; steroid hormone binding [GO:1990239]axon [GO:0030424]; dendritic spine head [GO:0044327]; dendritic spine neck [GO:0044326]; endoplasmic reticulum [GO:0005783]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sodium:potassium-exchanging ATPase complex [GO:0005890]; synapse [GO:0045202]P05026AT1B13Sodium/potassium-transporting < ATPase subunit beta-1JSUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.!activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; ATP metabolic process [GO:0046034]; blood coagulation [GO:0007596]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular calcium ion homeostasis [GO:0006874]; cellular potassium ion homeostasis [GO:0030007]; cellular sodium ion homeostasis [GO:0006883]; ion transmembrane transport [GO:0034220]; leukocyte migration [GO:0050900]; membrane repolarization [GO:0086009]; membrane repolarization during cardiac muscle cell action potential [GO:0086013]; positive regulation of ATPase activity [GO:0032781]; positive regulation of calcium:sodium antiporter activity [GO:1903281]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of potassium ion import [GO:1903288]; positive regulation of potassium ion transmembrane transporter activity [GO:1901018]; positive regulation of sodium ion export from cell [GO:1903278]; potassium ion import [GO:0010107]; potassium ion import across plasma membrane [GO:1990573]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; protein transport into plasma membrane raft [GO:0044861]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of gene expression [GO:0010468]; relaxation of cardiac muscle [GO:0055119]; response to hypoxia [GO:0001666]; sodium ion export from cell [GO:0036376]; transmembrane transport [GO:0055085]ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; MHC class II protein complex binding [GO:0023026]; sodium:potassium-exchanging ATPase activity [GO:0005391]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; intercalated disc [GO:0014704]; intracellular [GO:0005622]; membrane [GO:0016020]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. {ECO:0000269|PubMed:19694409}.; FUNCTION: Involved in cell adhesion and establishing epithelial cell polarity. {ECO:0000269|PubMed:19694409}.P54709AT1B33Sodium/potassium-transporting ATPase subunit beta-3SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065}; Single-pass type II membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.blood coagulation [GO:0007596]; cellular potassium ion homeostasis [GO:0030007]; cellular sodium ion homeostasis [GO:0006883]; ion transmembrane transport [GO:0034220]; leukocyte migration [GO:0050900]; membrane repolarization [GO:0086009]; positive regulation of ATPase activity [GO:0032781]; positive regulation of potassium ion import [GO:1903288]; positive regulation of potassium ion transmembrane transporter activity [GO:1901018]; positive regulation of sodium ion export from cell [GO:1903278]; potassium ion import [GO:0010107]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; sodium ion export from cell [GO:0036376]; transmembrane transport [GO:0055085]; transport [GO:0006810]}ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; sodium:potassium-exchanging ATPase activity [GO:0005391]caveola [GO:0005901]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; plasma membrane [GO:0005886]; sodium:potassium-exchanging ATPase complex [GO:0005890]FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.Q9BT23LIMD2LIM domain-containing protein 2zinc ion binding [GO:0008270]P40261NNMT Nicotinamide N-methyltransferaseKnown CRC biomarkersMarkersmethylation [GO:0032259]; organ regeneration [GO:0031100]; response to drug [GO:0042493]; response to organonitrogen compound [GO:0010243]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]6nicotinamide N-methyltransferase activity [GO:0008112]cytosol [GO:0005829]FUNCTION: Catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds.P26447S10A4Protein S100-A4zepithelial to mesenchymal transition [GO:0001837]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]fcalcium ion binding [GO:0005509]; poly(A) RNA binding [GO:0044822]; RAGE receptor binding [GO:0050786]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]Q9NY30BTG4 Protein BTG4 Folding, sorting and degradationRNA degradationcell cycle arrest [GO:0007050]; negative regulation of cell proliferation [GO:0008285]; negative regulation of mitotic cell cycle [GO:0045930]; neuron differentiation [GO:0030182]TFUNCTION: Shows marked antiproliferative activity, being able to induce G(1) arrest.Q8TBF8FA81AProtein FAM81AO43556SGCEEpsilon-sarcoglycanECM cytoskeletonSUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Golgi apparatus {ECO:0000250}.Hcell-matrix adhesion [GO:0007160]; muscle organ development [GO:0007517]4cytoskeleton [GO:0005856]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; dystrophin-associated glycoprotein complex [GO:0016010]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; sarcoglycan complex [GO:0016012]; sarcolemma [GO:0042383]FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.Q8N9F0NAT8LN-acetylaspartate synthetaseAminoAcid metbolism+Alanine, aspartate and glutamate metabolismSUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane; Single-pass membrane protein. Rough endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Its enzymatic activity contribution is quantitatively larger in mitochondrial compartment than in extramitochondrial compartment.3aspartate N-acetyltransferase activity [GO:0017188]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; rough endoplasmic reticulum membrane [GO:0030867]FUNCTION: Plays a role in the regulation of lipogenesis by producing N-acetylaspartate acid (NAA), a brain-specific metabolite. NAA occurs in high concentration in brain and its hydrolysis plays a significant part in the maintenance of intact white matter. Promotes dopamine uptake by regulating TNF-alpha expression. Attenuates methamphetamine-induced inhibition of dopamine uptake. {ECO:0000269|PubMed:19524112}.Q08EQ4TMSL1'Putative thymosin beta-4-like protein 1P51397DAP1Death-associated protein 1activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; autophagy [GO:0006914]; cellular response to amino< acid starvation [GO:0034198]; negative regulation of autophagy [GO:0010507]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of transcription, DNA-templated [GO:0045892]!death domain binding [GO:0070513]FUNCTION: Negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death. {ECO:0000269|PubMed:20537536}.Q99952PTN181Tyrosine-protein phosphatase non-receptor type 18ESUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.Xpeptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]Hnon-membrane spanning protein tyrosine phosphatase activity [GO:0004726],cytoplasm [GO:0005737]; nucleus [GO:0005634]FUNCTION: Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.O00625PIRPirin Flavonoid metabolismSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly localized in dot-like subnuclear structures. Cytoplasmic localization of PIR seems to positively correlate with melanoma progression.monocyte differentiation [GO:0030224]; regulation of transcription, DNA-templated [GO:0006355]; transcription from RNA polymerase II promoter [GO:0006366]}metal ion binding [GO:0046872]; quercetin 2,3-dioxygenase activity [GO:0008127]; transcription cofactor activity [GO:0003712]FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro). {ECO:0000269|PubMed:17288615, ECO:0000269|PubMed:20010624, ECO:0000269|PubMed:20711196, ECO:0000269|PubMed:23716661}.P37802TAGL2 Transgelin-2,epithelial cell differentiation [GO:0030855]8extracellular exosome [GO:0070062]; vesicle [GO:0031982]Q9H008LHPPBPhospholysine phosphohistidine inorganic pyrophosphate phosphataseEnergy metabolism Oxidative phosphorylationeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16430861}. Nucleus {ECO:0000269|PubMed:16430861}.dphosphate-containing compound metabolic process [GO:0006796]; protein dephosphorylation [GO:0006470]inorganic diphosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287]; phosphohistidine phosphatase activity [GO:0008969]; protein homodimerization activity [GO:0042803]\cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). {ECO:0000250}.Q13642FHL1%Four and a half LIM domains protein 1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm, cytosol. Note=Predominantly nuclear in myoblasts but is cytosolic in differentiated myotubes.cell differentiation [GO:0030154]; muscle organ development [GO:0007517]; negative regulation of cell growth [GO:0030308]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; organ morphogenesis [GO:0009887]; positive regulation of potassium ion transport [GO:0043268]; regulation of membrane depolarization [GO:0003254]; regulation of potassium ion transmembrane transporter activity [GO:1901016]?ion channel binding [GO:0044325]; zinc ion binding [GO:0008270]}cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]GFUNCTION: May have an involvement in muscle development or hypertrophy.P15121ALDRAldose reductaseCarbohydrate metabolism(Pentose and glucuronate interconversionsIC21-steroid hormone biosynthetic process [GO:0006700]; carbohydrate metabolic process [GO:0005975]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to methylglyoxal [GO:0097238]; cellular response to peptide [GO:1901653]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; fructose biosynthetic process [GO:0046370]; fructose metabolic process [GO:0006000]; inner medullary collecting duct development [GO:0072061]; maternal process involved in female pregnancy [GO:0060135]; naphthalene metabolic process [GO:0018931]; norepinephrine metabolic process [GO:0042415]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of smooth muscle cell proliferation [GO:0048661]; response to stress [GO:0006950]; response to thyroid hormone [GO:0097066]; response to water deprivation [GO:0009414]; small molecule metabolic process [GO:0044281]; sorbitol biosynthetic process [GO:0006061]; steroid metabolic process [GO:0008202]; stress-activated protein kinase signaling cascade [GO:0031098]; tissue homeostasis [GO:0001894]alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; electron carrier activity [GO:0009055]; glyceraldehyde oxidoreductase activity [GO:0043795]scell projection cytoplasm [GO:0032838]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mast cell granule [GO:0042629]; nucleoplasm [GO:0005654]; paranodal junction [GO:0033010]; perinuclear region of cytoplasm [GO:0048471]; Schmidt-Lanterman incisure [GO:0043220]; Schwann cell microvillus [GO:0097454]FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.Q9P1F3ABRALCostars family protein ABRACLQ15555MARE24Microtubule-associated protein RP/EB family member 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10188731}. Note=Associated with the microtubule network. Accumulates at the plus end of microtubules.cell division [GO:0051301]; cell proliferation [GO:0008283]; mitotic nuclear division [GO:0007067]; signal transduction [GO:0007165]`cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]FUNCTION: May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). {ECO:0000250}.O00244ATOX1Copper transport protein ATOX1Digestive_metabolismMineral absorptioncellular copper ion homeostasis [GO:0006878]; copper ion transport [GO:0006825]; intracellular copper ion transport [GO:0015680]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]copper chaperone activity [GO:0016531]; copper-dependent protein binding [GO:0032767]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; metallochaperone activity [GO:0016530]}FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.Q96PM5ZN363;RING finger and CHY zinc finger domain-containing protein 1Ubiquitin mediated proteolysis:SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.DNA repair [GO:0006281]; error-free translesion synthesis [GO:0070987]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; translesion synthesis [GO:0019985]ligase activity [GO:0016874]; p53 binding [GO:0002039]; protein homodimerization activity [GO:0042803]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]"FUNCTION: Mediates E3-dependent ubiquitina< tion and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity. {ECO:0000269|PubMed:16914734, ECO:0000269|PubMed:17721809, ECO:0000269|PubMed:18006823, ECO:0000269|PubMed:19043414, ECO:0000269|PubMed:19483087, ECO:0000269|PubMed:21791603, ECO:0000269|PubMed:21994467}.P07108ACBPAcyl-CoA-binding proteinuSUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus. Note=Golgi localization is dependent on ligand binding.Ebehavioral fear response [GO:0001662]; hair follicle development [GO:0001942]; lateral ventricle development [GO:0021670]; learning or memory [GO:0007611]; long-term synaptic potentiation [GO:0060291]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; transport [GO:0006810]; triglyceride metabolic process [GO:0006641]benzodiazepine receptor binding [GO:0030156]; lipid binding [GO:0008289]; long-chain fatty acyl-CoA binding [GO:0036042]; protein dimerization activity [GO:0046983]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; perinuclear endoplasmic reticulum [GO:0097038]|FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.P07902GALT)Galactose-1-phosphate uridylyltransferase+Amino sugar and nucleotide sugar metabolismcarbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; galactose metabolic process [GO:0006012]; small molecule metabolic process [GO:0044281]; UDP-glucose catabolic process [GO:0006258]gUDP-glucose:hexose-1-phosphate uridylyltransferase activity [GO:0008108]; zinc ion binding [GO:0008270]2cytosol [GO:0005829]; Golgi apparatus [GO:0005794]Q9H2X6HIPK2(Homeodomain-interacting protein kinase 2SUBCELLULAR LOCATION: Nucleus, PML body. Cytoplasm. Note=Concentrated in PML/POD/ND10 nuclear bodies. Small amounts are cytoplasmic.adult walking behavior [GO:0007628]; anterior/posterior pattern specification [GO:0009952]; cellular response to hypoxia [GO:0071456]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; erythrocyte differentiation [GO:0030218]; eye development [GO:0001654]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; iris morphogenesis [GO:0061072]; lens induction in camera-type eye [GO:0060235]; modulation by virus of host morphology or physiology [GO:0019048]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron differentiation [GO:0030182]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; PML body organization [GO:0030578]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA binding [GO:0043388]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein binding [GO:0032092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; protein phosphorylation [GO:0006468]; regulation of cell cycle [GO:0051726]; retina layer formation [GO:0010842]; SMAD protein signal transduction [GO:0060395]; smoothened signaling pathway [GO:0007224]; transforming growth factor beta receptor signaling pathway [GO:0007179]; voluntary musculoskeletal movement [GO:0050882]iATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II transcription coactivator activity [GO:0001105]; SMAD binding [GO:0046332]; transcription corepressor activity [GO:0003714]; virion binding [GO:0046790]cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634]; PML body [GO:0016605]; RNA polymerase II transcription factor complex [GO:0090575] FUNCTION: Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. {ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11925430, ECO:0000269|PubMed:12851404, ECO:0000269|PubMed:12874272, ECO:0000269|PubMed:14678985, ECO:0000269|PubMed:17018294, ECO:0000269|PubMed:17960875, ECO:0000269|PubMed:18695000, ECO:0000269|PubMed:18809579, ECO:0000269|PubMed:19015637, ECO:0000269|PubMed:19046997, ECO:0000269|PubMed:19448668, ECO:0000269|PubMed:20307497, ECO:0000269|PubMed:20573984, ECO:0000269|PubMed:20637728, ECO:0000269|PubMed:20980392, ECO:0000269|PubMed:21192925, ECO:0000269|PubMed:22825850}.P15559NQO1!NAD(P)H dehydrogenase [quinone] 1Saging [GO:0007568]; cellular nitrogen compound metabolic process [GO:0034641]; negative regulation of catalytic activity [GO:0043086]; nitric oxide biosynthetic process [GO:0006809]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of cellular amino acid metabolic process [GO:0006521]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to nutrient [GO:0007584]; response to toxic substance [GO:0009636]; small molecule metabolic process [GO:0044281]; synaptic transmission, cholinergic [GO:0007271]; xenobiotic metabolic process [GO:0006805]cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; identical protein bindin< g [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; poly(A) RNA binding [GO:0044822]; superoxide dismutase activity [GO:0004784]qcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; neuronal cell body [GO:0043025]#FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.Q53GG5PDLI3PDZ and LIM domain protein 3SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10063829}. Note=Localizes to myofiber Z-lines.Hactin filament organization [GO:0007015]; heart development [GO:0007507]Lstructural constituent of muscle [GO:0008307]; zinc ion binding [GO:0008270]Lactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; Z disc [GO:0030018]jFUNCTION: May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.Q9NXJ5PGPIPyroglutamyl-peptidase 1[cysteine-type peptidase activity [GO:0008234]; pyroglutamyl-peptidase activity [GO:0016920]|FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. {ECO:0000269|PubMed:12651114}.Q9NX05F120C5Constitutive coactivator of PPAR-gamma-like protein 2P04080CYTB Cystatin-BeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139332}. Nucleus {ECO:0000269|PubMed:11139332}.adult locomotory behavior [GO:0008344]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of peptidase activity [GO:0010466]; negative regulation of proteolysis [GO:0045861]cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; poly(A) RNA binding [GO:0044822]; protease binding [GO:0002020]tcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleolus [GO:0005730]}FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B.P19532TFE3Transcription factor E3SUBCELLULAR LOCATION: Nucleus.humoral immune response [GO:0006959]; positive regulation of cell adhesion [GO:0045785]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of osteoclast differentiation [GO:0045670]; transcription from RNA polymerase II promoter [GO:0006366]RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region DNA binding [GO:0044212]1FUNCTION: Transcription factor that specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF. In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity. Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer. It also binds very well to a USF/MLTF site.Q9UKY7CDV3Protein CDV3 homologcell proliferation [GO:0008283]Lcytoplasm [GO:0005737]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]P09104ENOG Gamma-enolase Carbohydrate degradationSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]Smagnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; perikaryon [GO:0043204]; phosphopyruvate hydratase complex [GO:0000015]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886]FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). {ECO:0000250}.Q9Y3A5SBDS Ribosome maturation protein SBDSTanslation regulationRibosome biogenesisSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Primarily detected in the cytoplasm, and at low levels in nucleus and nucleolus (PubMed:19602484 and PubMed:17475909). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (PubMed:19759903). {ECO:0000269|PubMed:19759903}.,bone marrow development [GO:0048539]; bone mineralization [GO:0030282]; cell proliferation [GO:0008283]; inner cell mass cell proliferation [GO:0001833]; leukocyte chemotaxis [GO:0030595]; mature ribosome assembly [GO:0042256]; mitotic spindle stabilization [GO:0043148]; rRNA processing [GO:0006364]|microtubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]ycytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFTUD1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. {ECO:0000269|PubMed:17643419, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:19759903, ECO:0000269|PubMed:21536732}.P61296HAND27Heart- and neural crest derivatives-expressed protein 2ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.{adult heart development [GO:0007512]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; apoptotic process involved in heart morphogenesis [GO:0003278]; cardiac neural crest cell development involved in outflow tract morphogenesis [GO:0061309]; cardiac neural crest cell migration involved in outflow tract morphogenesis [GO:0003253]; cardiac right ventricle formation [GO:0003219]; cartilage morphogenesis [GO:0060536]; cell proliferation involved in outflow tract morphogenesis [GO:0061325]; coronary artery morphogenesis [GO:0060982]; embryonic digit morphogenesis [GO:0042733]; heart development [GO:0007507]; heart looping [GO:0001947]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; mesenchymal cell proliferation [GO:0010463]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of DNA binding [GO:0043392]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; neural crest cell development [GO:0014032]; noradrenergic neuron differentiation [GO:0003357]; odontogenesis of dentin-containing tooth [GO:0042475]; palate development [GO:0060021]; peripheral nervous system neuron development [GO:0048935]; positive regulation of semaphorin-plexin signaling pathway involved in outflow tract morphogenesis [GO:2000764]; positive regulation of transcription, DNA-templated [GO:0045893]; positive < regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter involved in norepinephrine biosynthetic process [GO:2000763]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; regulation of secondary heart field cardioblast proliferation [GO:0003266]; regulation of transcription, DNA-templated [GO:0006355]; suckling behavior [GO:0001967]; sympathetic nervous system development [GO:0048485]; thymus development [GO:0048538]; tongue development [GO:0043586]; transcription from RNA polymerase II promoter [GO:0006366]; visceral serous pericardium development [GO:0061032]activating transcription factor binding [GO:0033613]; AT DNA binding [GO:0003680]; E-box binding [GO:0070888]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]gnuclear chromatin [GO:0000790]; protein complex [GO:0043234]; transcription factor complex [GO:0005667]FUNCTION: Essential for cardiac morphogenesis, particularly for the formation of the right ventricle and of the aortic arch arteries. Required for vascular development and regulation of angiogenesis, possibly through a VEGF signaling pathway. Plays also an important role in limb development, particularly in the establishment of anterior-posterior polarization, acting as an upstream regulator of sonic hedgehog (SHH) induction in the limb bud. Is involved in the development of branchial arches, which give rise to unique structures in the head and neck. Binds DNA on E-box consensus sequence 5'-CANNTG-3' (By similarity). {ECO:0000250}.Q6K0P9IFIX)Pyrin and HIN domain-containing protein 1SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleoplasm.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm.; SUBCELLULAR LOCATION: Isoform 5: Nucleus. Nucleus speckle.cell cycle [GO:0007049]nuclear speck [GO:0016607]FUNCTION: Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity of cancer cells. {ECO:0000269|PubMed:16479015, ECO:0000269|PubMed:18247378}.Q99698LYSTLysosomal-trafficking regulatorHblood coagulation [GO:0007596]; defense response to bacterium [GO:0042742]; defense response to protozoan [GO:0042832]; defense response to virus [GO:0051607]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; leukocyte chemotaxis [GO:0030595]; lysosome organization [GO:0007040]; mast cell secretory granule organization [GO:0033364]; melanosome organization [GO:0032438]; microtubule-based process [GO:0007017]; natural killer cell mediated cytotoxicity [GO:0042267]; neutrophil mediated immunity [GO:0002446]; phospholipid homeostasis [GO:0055091]; phospholipid metabolic process [GO:0006644]; pigmentation [GO:0043473]; positive regulation of natural killer cell activation [GO:0032816]; response to drug [GO:0042493]; secretion of lysosomal enzymes [GO:0033299]; T cell mediated immunity [GO:0002456]!phospholipid binding [GO:0005543]cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of membrane [GO:0019898]; microtubule cytoskeleton [GO:0015630]FUNCTION: May be required for sorting endosomal resident proteins into late multivesicular endosomes by a mechanism involving microtubules.Q9Y5Y2NUBP2,Cytosolic Fe-S cluster assembly factor NUBP2SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03039}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03039}. Note=Enriched at the centrosomes during mitosis. {ECO:0000255|HAMAP-Rule:MF_03039}.Xiron-sulfur cluster assembly [GO:0016226]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]Rcytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole centrosome [GO:0031616]QFUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. {ECO:0000255|HAMAP-Rule:MF_03039}.Q7Z6K3PTAR1CProtein prenyltransferase alpha subunit repeat-containing protein 1 protein prenylation [GO:0018342]/protein prenyltransferase activity [GO:0008318]8cytoplasm [GO:0005737]; transferase complex [GO:1990234]Q9BRF8CPPED+Serine/threonine-protein phosphatase CPPED1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23799035}.Pmetal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]:cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]FUNCTION: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes. {ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:23939394}.P54652HSP72#Heat shock-related 70 kDa protein 2Transcriptional RegulationPrp19*male meiosis [GO:0007140]; male meiosis I [GO:0007141]; negative regulation of inclusion body assembly [GO:0090084]; positive regulation of calcium-transporting ATPase activity [GO:1901896]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle [GO:0031662]; protein refolding [GO:0042026]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]; spermatid development [GO:0007286]; synaptonemal complex disassembly [GO:0070194]}ATP binding [GO:0005524]; enzyme binding [GO:0019899]; glycolipid binding [GO:0051861]; unfolded protein binding [GO:0051082]@blood microparticle [GO:0072562]; CatSper complex [GO:0036128]; cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; male germ cell nucleus [GO:0001673]; membrane [GO:0016020]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.Q5TCQ9MAGI3LMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 3TGFTGF-Bindings(8)SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell junction, tight junction. Nucleus {ECO:0000250}. Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity). {ECO:0000250}.apoptotic process [GO:0006915]; intracellular signal transduction [GO:0035556]; nucleotide phosphorylation [GO:0046939]; positive regulation of JUN kinase activity [GO:0043507]; viral process [GO:0016032]@ATP binding [GO:0005524]; guanylate kinase activity [GO:0004385]qbicellular tight junction [GO:0005923]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]kFUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and< tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2. {ECO:0000269|PubMed:10748157}.P07741APT!Adenine phosphoribosyltransferaseNucleotideMetabolismPurine metabolism Purine metabolismyadenine salvage [GO:0006168]; AMP salvage [GO:0044209]; cellular response to insulin stimulus [GO:0032869]; grooming behavior [GO:0007625]; lactation [GO:0007595]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; small molecule metabolic process [GO:0044281]oadenine binding [GO:0002055]; adenine phosphoribosyltransferase activity [GO:0003999]; AMP binding [GO:0016208]jcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.Q15942ZYXZyxin regulatorSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell junction, focal adhesion. Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1.ncell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; regulation of inflammatory response [GO:0050727]; signal transduction [GO:0007165]; stress fiber assembly [GO:0043149]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]?poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]cell-cell adherens junction [GO:0005913]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]WFUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity). {ECO:0000250}.Q9NVE7PANK4Pantothenate kinase 4 Cofactor biosynthesis,coenzyme A biosynthetic process [GO:0015937]CATP binding [GO:0005524]; pantothenate kinase activity [GO:0004594]cytoplasm [GO:0005737]mFUNCTION: Plays a role in the physiological regulation of the intracellular CoA concentration. {ECO:0000250}.Q9Y5Z4HEBP2Heme-binding protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17098234}. Mitochondrion {ECO:0000269|PubMed:17098234}. Note=Mainly localized to the cytoplasm with a much lower abundance in the mitochondrion.negative regulation of mitochondrial membrane potential [GO:0010917]; positive regulation of mitochondrial membrane permeability [GO:0035794]; positive regulation of necrotic cell death [GO:0010940]Vcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]FUNCTION: Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin. {ECO:0000269|PubMed:17098234}.Q5SW96ARH2Low density lipoprotein receptor adapter protein 1 cellProcess Endocytosis>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12451172}.amyloid precursor protein metabolic process [GO:0042982]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of signal transduction [GO:0009967]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; receptor-mediated endocytosis of low-density lipoprotein particle involved in cholesterol transport [GO:0090118]; regulation of establishment of protein localization to plasma membrane [GO:0090003]; regulation of protein binding [GO:0043393]; transport [GO:0006810]AP-2 adaptor complex binding [GO:0035612]; beta-amyloid binding [GO:0001540]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphotyrosine binding [GO:0001784]; receptor signaling complex scaffold activity [GO:0030159]; signaling adaptor activity [GO:0035591]axon [GO:0030424]; basal plasma membrane [GO:0009925]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; early endosome [GO:0005769]; neurofilament [GO:0005883]; recycling endosome [GO:0055037]FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. {ECO:0000269|PubMed:15728179}.Q9Y617SERCPhosphoserine aminotransferase(Glycine, serine and threonine metabolism Amino-acid biosynthesiscellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; L-serine biosynthetic process [GO:0006564]; pyridoxine biosynthetic process [GO:0008615]; small molecule metabolic process [GO:0044281]HO-phospho-L-serine:2-oxoglutarate aminotransferase activity [GO:0004648]Pcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]FUNCTION: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000250|UniProtKB:P10658}.Q9Y2V2CHSP1'Calcium-regulated heat stable protein 11SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21177848}. Cytoplasm, P-body {ECO:0000269|PubMed:21177848}. Cytoplasmic granule {ECO:0000269|PubMed:21177848}. Note=Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded (By similarity). {ECO:0000250}.intracellular signal transduction [GO:0035556]; regulation of mRNA stability [GO:0043488]; regulation of transcription, DNA-templated [GO:0006355]\DNA binding [GO:0003677]; mRNA 3'-UTR binding [GO:0003730]; phosphatase binding [GO:0019902]cytoplasmic exosome (RNase complex) [GO:0000177]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; P granule [GO:0043186]FUNCTION: Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro). {ECO:0000269|PubMed:21078874, ECO:0000269|PubMed:21177848}.P58546MTPN MyotrophinrSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.'catecholamine metabolic process [GO:0006584]; cell growth [GO:0016049]; cellular response to mechanical stimulus [GO:0071260]; cerebellar granule cell differentiation [GO:0021707]; neuron differentiation [GO:0030182]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell growth [GO:0030307]; positive regulation of macromolecule biosynthetic process [GO:0010557]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein metabolic process [GO:0051247]; regulation of barbed-end actin filament capping [GO:2000812]; regulation of striated muscle tissue development [GO:< 0016202]; regulation of translation [GO:0006417]; skeletal muscle tissue regeneration [GO:0043403]; striated muscle cell differentiation [GO:0051146]*sequence-specific DNA binding [GO:0043565]axon [GO:0030424]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; F-actin capping protein complex [GO:0008290]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. {ECO:0000250, ECO:0000269|PubMed:10329199, ECO:0000269|PubMed:16895918, ECO:0000269|PubMed:20625546}.P62256UBE2H!Ubiquitin-conjugating enzyme E2 Hproteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; ubiquitin-dependent protein catabolic process [GO:0006511]ATP binding [GO:0005524]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate histone H2A. {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:8132613}.Q03393PTPS'6-pyruvoyl tetrahydrobiopterin synthase1cellular amino acid metabolic process [GO:0006520]; central nervous system development [GO:0007417]; nitric oxide metabolic process [GO:0046209]; regulation of nitric-oxide synthase activity [GO:0050999]; small molecule metabolic process [GO:0044281]; tetrahydrobiopterin biosynthetic process [GO:0006729]6-pyruvoyltetrahydropterin synthase activity [GO:0003874]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]Hcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. {ECO:0000269|PubMed:1282802}.P30041PRDX6Peroxiredoxin-6Phenylalanine metabolismSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16186110, ECO:0000269|PubMed:19188445}. Lysosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Also found in lung secretory organelles. {ECO:0000250}.hydrogen peroxide catabolic process [GO:0042744]; phospholipid catabolic process [GO:0009395]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]antioxidant activity [GO:0016209]; glutathione peroxidase activity [GO:0004602]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004623]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]FUNCTION: Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.P00558PGK1Phosphoglycerate kinase 1Glycolysis / Gluconeogenesiscanonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; epithelial cell differentiation [GO:0030855]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; phosphorylation [GO:0016310]; small molecule metabolic process [GO:0044281]GATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618]kcytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]FUNCTION: In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).C9JRZ8AK1BF'Aldo-keto reductase family 1 member B15SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:25577493}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol {ECO:0000269|PubMed:25577493}.(oxidation-reduction process [GO:0055114]estradiol 17-beta-dehydrogenase activity [GO:0004303]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]0cytosol [GO:0005829]; mitochondrion [GO:0005739]FUNCTION: Isoform 1: Mainly acts as a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. Has a strong selectivity towards NADP(H) (PubMed:25577493). {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493}.; FUNCTION: Isoform 2: No oxidoreductase activity observed with the tested substrates. {ECO:0000269|PubMed:25577493}.P04632CPNS1Calpain small subunit 1 ApoptosisCalpainSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}.extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; positive regulation of cell proliferation [GO:0008284]; proteolysis [GO:0006508]ecalcium-dependent cysteine-type endopeptidase activity [GO:0004198]; calcium ion binding [GO:0005509]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.O76074PDE5A,cGMP-specific 3',5'-cyclic phosphodiesteraseblood coagulation [GO:0007596]; cGMP catabolic process [GO:0046069]; negative regulation of cardiac muscle contraction [GO:0055118]; negative regulation of T cell proliferation [GO:0042130]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of oocyte development [GO:0060282]; regulation of cGMP metabolic process [GO:0030823]; relaxation of cardiac muscle [GO:0055119]; signal transduction [GO:0007165]3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; cGMP binding [GO:0030553]; metal ion binding [GO:0046872]aFUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:9714779, PubMed:15489334). Specifically regulates nitric-oxide-generated cGMP (PubMed:15489334). {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9714779}.Q9BXP8PAPP2 Pappalysin-2-SUBCELLULAR LOCATION: Secreted {ECO:0000250}.bone morphogenesis [GO:0060349]; cell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; proteolysis [GO:0006508]; regulation of cell growth [GO:0001558]Emetallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]xextracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular [GO:0005622]; membrane [GO:0016020]FUNCTION: Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3. {ECO:0000269|PubMed:11264294}.Q9NT62ATG3&Ubiquitin-like-conjugating enzyme ATG3Regulation of autophagy (38)>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11825910}.^autophagosome assembly [GO:0000045]; cellular protein modification process [GO:0006464]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrion degradation [GO:0000422]; nucleophagy [GO< :0044804]; protein targeting to membrane [GO:0006612]; protein ubiquitination [GO:0016567]; regulation of cilium assembly [GO:1902017]Atg12 transferase activity [GO:0019777]; Atg8 ligase activity [GO:0019776]; enzyme binding [GO:0019899]; ligase activity [GO:0016874]; ubiquitin-like protein transferase activity [GO:0019787]Gcytoplasmic ubiquitin ligase complex [GO:0000153]; cytosol [GO:0005829]FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:20723759}.A8MYN8YO024APutative ankyrin repeat domain-containing protein ENSP00000383090Q96M96FGD4/FYVE, RhoGEF and PH domain-containing protein 4SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Note=Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers (By similarity). {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; apoptotic signaling pathway [GO:0097190]; cytoskeleton organization [GO:0007010]; filopodium assembly [GO:0046847]; lamellipodium assembly [GO:0030032]; microspike assembly [GO:0030035]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; regulation of cell shape [GO:0008360]; regulation of GTPase activity [GO:0043087]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]; small GTPase binding [GO:0031267]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; ruffle [GO:0001726]FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8 (By similarity). {ECO:0000250}.O14950ML12B!Myosin regulatory light chain 12B.Cell motility/Regulation of actin cytoskeleton Myosin H/L(9)axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; muscle contraction [GO:0006936]; regulation of cell shape [GO:0008360]; small GTPase mediated signal transduction [GO:0007264] calcium ion binding [GO:0005509]apical part of cell [GO:0045177]; brush border [GO:0005903]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myosin II complex [GO:0016460]; stress fiber [GO:0001725]; Z disc [GO:0030018]OFUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). {ECO:0000250}.O75508CLD11 Claudin-11Cellular CommunicationTight junction`SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.axon ensheathment [GO:0008366]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; spermatogenesis [GO:0007283]Qidentical protein binding [GO:0042802]; structural molecule activity [GO:0005198]basal part of cell [GO:0045178]; bicellular tight junction [GO:0005923]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}.O43731ERD23%ER lumen protein-retaining receptor 3RSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; protein retention in ER lumen [GO:0006621]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]*ER retention sequence binding [GO:0046923]Xendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity). {ECO:0000250}.O75204TM127Transmembrane protein 127SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}; Multi-pass membrane protein {ECO:0000269|PubMed:20154675}. Cytoplasm {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}. Note=Association of TMEM127 with the cell membrane is enhanced by inhibition of endocytosis. In the cytoplasm, it colocalizes with markers of early endosomal structures, Golgi apparatus and lysosomes. {ECO:0000269|PubMed:20154675, ECO:0000269|PubMed:21156949}.endosome organization [GO:0007032]; negative regulation of cell proliferation [GO:0008285]; negative regulation of TOR signaling [GO:0032007]Rab GTPase binding [GO:0017137]~cytoplasm [GO:0005737]; early endosome [GO:0005769]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Controls cell proliferation acting as a negative regulator of TOR signaling pathway mediated by mTORC1. May act as a tumor suppressor. {ECO:0000269|PubMed:20154675}.Q32NB8PGPS1QCDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondriallipid metabolismGlycerophospholipid metabolism Phospholipid metabolism'cardiolipin biosynthetic process [GO:0032049]; diacylglycerol metabolic process [GO:0046339]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity [GO:0008444]iendoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]yFUNCTION: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin. {ECO:0000250}.Q9NYJ1COA4=Cytochrome c oxidase assembly factor 4 homolog, mitochondrial6FUNCTION: Putative COX assembly factor. {ECO:0000250}.Q96ND0F210AProtein FAM210AvSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000305}.Gintegral component of membrane [GO:0016021]; mitochondrion [GO:0005739]P13611CSPG2Versican core protein Proteoglycans(29)JSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.carbohydrate metabolic process < [GO:0005975]; cell adhesion [GO:0007155]; cell recognition [GO:0008037]; central nervous system development [GO:0007417]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; glycosaminoglycan metabolic process [GO:0030203]; heart development [GO:0007507]; multicellular organismal development [GO:0007275]; osteoblast differentiation [GO:0001649]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; glycosaminoglycan binding [GO:0005539]; hyaluronic acid binding [GO:0005540]extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.Q99538LGMNLegumainLysosome proteases(18)-SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; innate immune response [GO:0045087]; negative regulation of ERBB signaling pathway [GO:1901185]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of neuron apoptotic process [GO:0043524]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; receptor catabolic process [GO:0032801]; renal system process [GO:0003014]; response to acidic pH [GO:0010447]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]; toll-like receptor signaling pathway [GO:0002224]; vitamin D metabolic process [GO:0042359]Rcysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233]apical part of cell [GO:0045177]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. {ECO:0000250, ECO:0000269|PubMed:23776206}.P21741MKMidkineSUBCELLULAR LOCATION: Secreted.adrenal gland development [GO:0030325]; behavioral fear response [GO:0001662]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cerebellar granular layer development [GO:0021681]; cerebral cortex development [GO:0021987]; defecation [GO:0030421]; dentate gyrus development [GO:0021542]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; Notch signaling pathway [GO:0007219]; positive regulation of cell division [GO:0051781]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of behavior [GO:0050795]; response to drug [GO:0042493]; response to glucocorticoid [GO:0051384]; response to wounding [GO:0009611]; short-term memory [GO:0007614]; signal transduction [GO:0007165]Agrowth factor activity [GO:0008083]; heparin binding [GO:0008201]Wcell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]HFUNCTION: Developmentally regulated, secreted growth factor homologous to pleiotrophin (PTN), which has heparin binding activity. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation. Involved in neointima formation after arterial injury, possibly by mediating leukocyte recruitment. Also involved in early fetal adrenal gland development (By similarity). {ECO:0000250}.Q8TDB4HUMMR Protein MGARP|SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:16565373, ECO:0000269|PubMed:21447634}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with RHOT1, RHOT2, TRAK1 and TRAK2 at the mitochondrion. {ECO:0000250}.anterograde axon cargo transport [GO:0008089]; axon transport of mitochondrion [GO:0019896]; cellular response to gonadotropin-releasing hormone [GO:0097211]; cellular response to hypoxia [GO:0071456]; cellular response to steroid hormone stimulus [GO:0071383]; positive regulation of mitochondrion organization [GO:0010822]; protein targeting to mitochondrion [GO:0006626]; regulation of mitochondrion organization [GO:0010821]; retrograde axon cargo transport [GO:0008090][integral component of mitochondrial outer membrane [GO:0031307]; mitochondrion [GO:0005739]FUNCTION: Plays a role in the trafficking of mitochondria along microtubules. Regulates the kinesin-mediated axonal transport of mitochondria to nerve terminals along microtubules during hypoxia. Participates in the translocation of TRAK2/GRIF1 from the cytoplasm to the mitochondrion. Also plays a role in steroidogenesis through maintenance of mitochondrial abundance and morphology (By similarity). {ECO:0000250}.Q6YHK3CD109 CD109 antigen TGF-BindingSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11861284, ECO:0000269|PubMed:16754747}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11861284, ECO:0000269|PubMed:16754747}.hair follicle development [GO:0001942]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of wound healing [GO:0061045]; osteoclast fusion [GO:0072675]; regulation of keratinocyte differentiation [GO:0045616]oserine-type endopeptidase inhibitor activity [GO:0004867]; transforming growth factor beta binding [GO:0050431]anchored component of membrane [GO:0031225]; cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]_FUNCTION: Modulates negatively TGFB1 signaling in keratinocytes. {ECO:0000269|PubMed:16754747}.Q13472TOP3ADNA topoisomerase 3-alphaDNA replication and RepairHomologous recombinationJDNA topological change [GO:0006265]; meiotic nuclear division [GO:0007126]gDNA binding [GO:0003677]; DNA topoisomerase type I activity [GO:0003917]; zinc ion binding [GO:0008270]Dchromosome [GO:0005694]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. {ECO:0000269|PubMed:20445207, EC< O:0000269|PubMed:8622991}.Q9UBV4WNT16Protein Wnt-16WntLigandbone remodeling [GO:0046849]; cardiac epithelial to mesenchymal transition [GO:0060317]; cell fate commitment [GO:0045165]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; negative regulation of cell death [GO:0060548]; neuron differentiation [GO:0030182]; optic cup formation involved in camera-type eye development [GO:0003408]; oxidative stress-induced premature senescence [GO:0090403]; positive regulation of gene expression [GO:0010628]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; replicative senescence [GO:0090399]; Wnt signaling pathway [GO:0016055]frizzled binding [GO:0005109]cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578] FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.P00747PLMN PlasminogenenzymeSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:14699093}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.Vblood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; fibrinolysis [GO:0042730]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of fibrinolysis [GO:0051918]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of fibrinolysis [GO:0051919]; tissue remodeling [GO:0048771]apolipoprotein binding [GO:0034185]; protein domain specific binding [GO:0019904]; receptor binding [GO:0005102]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]3blood microparticle [GO:0072562]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extrinsic component of external side of plasma membrane [GO:0031232]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]8FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. {ECO:0000269|PubMed:14699093}.; FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. {ECO:0000269|PubMed:14699093}.P55058PLTPPhospholipid transfer proteinhigh-density lipoprotein particle remodeling [GO:0034375]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; positive regulation of cholesterol efflux [GO:0010875]; sperm motility [GO:0030317]; vitamin E biosynthetic process [GO:0010189]lipid binding [GO:0008289]Cextracellular region [GO:0005576]; extracellular space [GO:0005615]CFUNCTION: Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine. Essential for the transfer of excess surface lipids from triglyceride-rich lipoproteins to HDL, thereby facilitating the formation of smaller lipoprotein remnants, contributing to the formation of LDL, and assisting in the maturation of HDL particles. PLTP also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion. Two distinct forms of PLTP exist in plasma: an active form that can transfer PC from phospholipid vesicles to high-density lipoproteins (HDL), and an inactive form that lacks this capability.P01033TIMP1Metalloproteinase inhibitor 1 mmp inhibitorSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3010309, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540}.aging [GO:0007568]; blood coagulation [GO:0007596]; cartilage development [GO:0051216]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of metalloenzyme activity [GO:0048553]; negative regulation of trophoblast cell migration [GO:1901164]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of cell proliferation [GO:0008284]; regulation of integrin-mediated signaling pathway [GO:2001044]; response to cytokine [GO:0034097]; response to hormone [GO:0009725]; response to peptide hormone [GO:0043434]cytokine activity [GO:0005125]; metal ion binding [GO:0046872]; metalloendopeptidase inhibitor activity [GO:0008191]; protease binding [GO:0002020]basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. {ECO:0000269|PubMed:1420137, ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:17050530, ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:20545310, ECO:0000269|PubMed:22427646, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540, ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:9065415}.A6NDB9PALM3 Paralemmin-3gSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.negative regulation of cytokine-mediated signaling pathway [GO:0001960]; response to lipopolysaccharide [GO:0032496]; Toll signaling pathway [GO:0008063]ATP binding [GO:0005524]4cytoplasm [GO:0005737]; plasma membrane [GO:0005886]FUNCTION: ATP-binding protein, which may act as a adapter in the Toll-like receptor (TLR) signaling. {ECO:0000269|PubMed:21187075}.P13164IFM1*Interferon-induced transmembrane protein 1INTRAMEMSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19499152, ECO:0000269|PubMed:25105503}; Single-pass membrane protein {ECO:0000269|PubMed:19499152}.cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; intracellular signal transduction [GO:0035556]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negat< ive regulation of viral entry into host cell [GO:0046597]; negative regulation of viral genome replication [GO:0045071]; ossification [GO:0001503]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of immune response [GO:0050776]; response to interferon-alpha [GO:0035455]; response to interferon-beta [GO:0035456]; response to interferon-gamma [GO:0034341]; response to virus [GO:0009615]; type I interferon signaling pathway [GO:0060337]0receptor signaling protein activity [GO:0005057]|integral component of membrane [GO:0016021]; intracellular [GO:0005622]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. {ECO:0000269|PubMed:16847454, ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20838853, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:22634173}.Q8N4N8KIF2BKinesin-like protein KIF2B*SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17538014}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17538014}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17538014}. Note=Association with kinetochore is transient.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cell division [GO:0051301]; microtubule-based movement [GO:0007018]; microtubule depolymerization [GO:0007019]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; regulation of chromosome segregation [GO:0051983]; small GTPase mediated signal transduction [GO:0007264]_ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule motor activity [GO:0003777]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity. {ECO:0000269|PubMed:17538014}.P12259FA5Coagulation factor Vblood circulation [GO:0008015]; blood coagulation [GO:0007596]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]copper ion binding [GO:0005507]extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.P52823STC1Stanniocalcin-1tbone development [GO:0060348]; cellular calcium ion homeostasis [GO:0006874]; cellular response to cAMP [GO:0071320]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hypoxia [GO:0071456]; chondrocyte proliferation [GO:0035988]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; endothelial cell morphogenesis [GO:0001886]; growth plate cartilage axis specification [GO:0003421]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of cell migration [GO:0030336]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of renal phosphate excretion [GO:1903403]; ossification [GO:0001503]; positive regulation of calcium ion import [GO:0090280]; regulation of anion transport [GO:0044070]; regulation of cardiac muscle cell contraction [GO:0086004]; response to vitamin D [GO:0033280]sapical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]]FUNCTION: Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia.Q8N539FBCD1(Fibrinogen C domain-containing protein 1aSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.;chitin binding [GO:0008061]; metal ion binding [GO:0046872]Bintegral component of membrane [GO:0016021]; membrane [GO:0016020]_FUNCTION: Acetyl group-binding receptor which shows a high-affinity and calcium-dependent binding to acetylated structures such as chitin, some N-acetylated carbohydrates, and amino acids, but not to their non-acetylated counterparts. Can facilitate the endocytosis of acetylated components. {ECO:0000269|PubMed:19710473, ECO:0000269|PubMed:19892701}.Q15043S39AEZinc transporter ZIP14%SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, lamellipodium {ECO:0000269|PubMed:12659941, ECO:0000269|PubMed:15642354}. Note=Localized to the plasma membrane and also found colocalized with F-actin concentrated on lamellipodiae.cellular zinc ion homeostasis [GO:0006882]; transmembrane transport [GO:0055085]; zinc II ion transmembrane import [GO:0071578]; zinc II ion transmembrane transport [GO:0071577]vferrous iron transmembrane transporter activity [GO:0015093]; zinc ion transmembrane transporter activity [GO:0005385]endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]FUNCTION: May mediate cellular uptake of nontransferrin-bound iron (By similarity). Broad-scope metal ion transporter with a preference for zinc uptake. {ECO:0000250, ECO:0000269|PubMed:15642354}.Q8N3L3TXLNB Beta-taxilin}FUNCTION: Promotes motor nerve regeneration (By similarity). May be involved in intracellular vesicle traffic. {ECO:0000250}.Q99988GDF15 Growth/differentiation factor 15-SUBCELLULAR LOCATION: Secreted {ECO:0000305}.cell-cell signaling [GO:0007267]; cell development [GO:0048468]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; regulation of apoptotic process [GO:0042981]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]]cytokine activity [GO:0005125]; transforming growth factor beta receptor binding [GO:0005160]gextracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]Q9Y2Y0AR2BP6ADP-ribosylation factor-like protein 2-binding proteinSUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, cilium basal body. Note=The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be < required for cilia basal body localization. {ECO:0000250}.energy reserve metabolic process [GO:0006112]; maintenance of protein location in nucleus [GO:0051457]; positive regulation of tyrosine phosphorylation of Stat3 protein [GO:0042517]; regulation of catalytic activity [GO:0050790]; regulation of insulin secretion [GO:0050796]; regulation of nucleic acid-templated transcription [GO:1903506]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]WGTPase regulator activity [GO:0030695]; transcription coactivator activity [GO:0003713]centrosome [GO:0005813]; cilium [GO:0005929]; cytosol [GO:0005829]; midbody [GO:0030496]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2. {ECO:0000269|PubMed:18234692}.Q96AT9RPERibulose-phosphate 3-epimerasePentose phosphate pathwaycarbohydrate metabolic process [GO:0005975]; cellular carbohydrate metabolic process [GO:0044262]; pentose catabolic process [GO:0019323]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]; small molecule metabolic process [GO:0044281]identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; ribulose-phosphate 3-epimerase activity [GO:0004750]8cytosol [GO:0005829]; extracellular exosome [GO:0070062]FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:20923965}.Q8ND04SMG8 Protein SMG8gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of protein kinase activity [GO:0045859]FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1 kinase activity until the ribosome:SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity. {ECO:0000269|PubMed:19417104}.P13693TCTP(Translationally-controlled tumor protein=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9059837}.;calcium ion transport [GO:0006816]; cellular calcium ion homeostasis [GO:0006874]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; regulation of apoptotic process [GO:0042981]; response to virus [GO:0009615]Bcalcium ion binding [GO:0005509]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; multivesicular body [GO:0005771]; nucleus [GO:0005634]DFUNCTION: Involved in calcium binding and microtubule stabilization.P41236IPP2Protein phosphatase inhibitor 2 generation of precursor metabolites and energy [GO:0006091]; glycogen metabolic process [GO:0005977]; negative regulation of catalytic activity [GO:0043086]; regulation of phosphoprotein phosphatase activity [GO:0043666]; regulation of signal transduction [GO:0009966]Dprotein serine/threonine phosphatase inhibitor activity [GO:0004865]-FUNCTION: Inhibitor of protein-phosphatase 1.P30740ILEULeukocyte elastase inhibitoraSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic granule {ECO:0000269|PubMed:23269243}.:negative regulation of endopeptidase activity [GO:0010951]9serine-type endopeptidase inhibitor activity [GO:0004867]scytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]FUNCTION: Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H. {ECO:0000269|PubMed:11747453}.Q9H0W9CK054Ester hydrolase C11orf54<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16522806}.Uhydrolase activity, acting on ester bonds [GO:0016788]; zinc ion binding [GO:0008270]8extracellular exosome [GO:0070062]; nucleus [GO:0005634]rFUNCTION: Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate. {ECO:0000269|PubMed:16522806}.P49773HINT1,Histidine triad nucleotide-binding protein 1jSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Interaction with CDK7 leads to a more nuclear localization.Dintrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; positive regulation of calcium-mediated signaling [GO:0050850]; purine ribonucleotide catabolic process [GO:0009154]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]ghydrolase activity [GO:0016787]; nucleotide binding [GO:0000166]; protein kinase C binding [GO:0005080]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:9323207}.Q8IVT5KSR1Kinase suppressor of Ras 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20679487}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20679487}. Note=In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery (By similarity). {ECO:0000250}.^positive regulation of MAPK cascade [GO:0043410]; Ras protein signal transduction [GO:0007265]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]; protein kinase activity [GO:0004672]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; protein complex [GO:0043234]FUNCTION: Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity.Q9HBD1RC3H2Roquin-2UbiquitinationE3SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger. {ECO:0000269|PubMed:20412057}."B cell homeostasis [GO:0001782]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; multicellular < organism growth [GO:0035264]; positive regulation of NIK/NF-kappaB signaling [GO:1901224]; post-embryonic development [GO:0009791]; posttranscriptional regulation of gene expression [GO:0010608]; protein polyubiquitination [GO:0000209]; spleen development [GO:0048536]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]; T follicular helper cell differentiation [GO:0061470]DNA binding [GO:0003677]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity). May act as a ubiquitin E3 ligase. Involved in the ubiquitination of MAP3K5 (PubMed:24448648). {ECO:0000250|UniProtKB:P0C090, ECO:0000269|PubMed:24448648}.P07311ACYP1Acylphosphatase-1Pyruvate metabolism<phosphate-containing compound metabolic process [GO:0006796]%acylphosphatase activity [GO:0003998]"extracellular exosome [GO:0070062]2FUNCTION: Its physiological role is not yet clear.P14174MIF&Macrophage migration inhibitory factorTyrosine metabolismSUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens.-carboxylic acid metabolic process [GO:0019752]; cell aging [GO:0007569]; cell proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell aging [GO:0090344]; negative regulation of cell cycle arrest [GO:0071157]; negative regulation of cellular protein metabolic process [GO:0032269]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of gene expression [GO:0010629]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of mature B cell apoptotic process [GO:0002906]; negative regulation of myeloid cell apoptotic process [GO:0033033]; positive chemotaxis [GO:0050918]; positive regulation of arachidonic acid secretion [GO:0090238]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of myeloid leukocyte cytokine production involved in immune response [GO:0061081]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphorylation [GO:0042327]; positive regulation of prostaglandin secretion involved in immune response [GO:0061078]; positive regulation of protein kinase A signaling [GO:0010739]; prostaglandin biosynthetic process [GO:0001516]; protein homotrimerization [GO:0070207]; regulation of macrophage activation [GO:0043030]chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; cytokine receptor binding [GO:0005126]; dopachrome isomerase activity [GO:0004167]; phenylpyruvate tautomerase activity [GO:0050178]; receptor binding [GO:0005102]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; vesicle [GO:0031982]FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. {ECO:0000269|PubMed:15908412, ECO:0000269|PubMed:17443469, ECO:0000269|PubMed:23776208}.O94768ST17B#Serine/threonine-protein kinase 17BSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9786912}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Colocalizes with STK17B at the plasma membrane. {ECO:0000250}.apoptotic process [GO:0006915]; intracellular signal transduction [GO:0035556]; positive regulation of fibroblast apoptotic process [GO:2000271]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]uATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]actin cytoskeleton [GO:0015629]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269|PubMed:9786912}.Q96AB6NTAN1,Protein N-terminal asparagine amidohydrolase;adult locomotory behavior [GO:0008344]; memory [GO:0007613]Bprotein-N-terminal asparagine amidohydrolase activity [GO:0008418]FUNCTION: Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn. {ECO:0000269|PubMed:21375249}.Q9NWV4CA123UPF0587 protein C1orf123Q12965MYO1EUnconventional myosin-IeSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle. Cytoplasmic vesicle, clathrin-coated vesicle. Cell junction {ECO:0000250}. Note=Colocalizes with F-actin (By similarity). In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles. {ECO:0000250}.actin filament-based movement [GO:0030048]; endocytosis [GO:0006897]; glomerular basement membrane development [GO:0032836]; glomerular filtration [GO:0003094]; glomerular visceral epithelial cell development [GO:0072015]; in utero embryonic development [GO:0001701]; nitrogen compound metabolic proc< ess [GO:0006807]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; post-embryonic hemopoiesis [GO:0035166]; vasculogenesis [GO:0001570]actin filament binding [GO:0051015]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; motor activity [GO:0003774]; phosphatidylinositol binding [GO:0035091]actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; brush border [GO:0005903]; cell-cell junction [GO:0005911]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; myosin complex [GO:0016459]FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. {ECO:0000269|PubMed:11940582, ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:20860408}.O00299CLIC1(Chloride intracellular channel protein 1SUBCELLULAR LOCATION: Nucleus. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain.7chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; platelet aggregation [GO:0070527]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of cell cycle [GO:0051726]; regulation of mitochondrial membrane potential [GO:0051881]; signal transduction [GO:0007165]Wchloride channel activity [GO:0005254]; voltage-gated ion channel activity [GO:0005244]blood microparticle [GO:0072562]; brush border [GO:0005903]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle [GO:0031982]FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.P06744G6PIGlucose-6-phosphate isomerasefSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11437381}. Secreted {ECO:0000269|PubMed:11437381}.aldehyde catabolic process [GO:0046185]; angiogenesis [GO:0001525]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gene expression [GO:0010467]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; hemostasis [GO:0007599]; humoral immune response [GO:0006959]; learning or memory [GO:0007611]; methylglyoxal biosynthetic process [GO:0019242]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of neuron apoptotic process [GO:0043524]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]glucose-6-phosphate isomerase activity [GO:0004347]; intramolecular transferase activity [GO:0016866]; monosaccharide binding [GO:0048029]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]AFUNCTION: Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381}.P14550AK1A1Alcohol dehydrogenase [NADP(+)]aldehyde catabolic process [GO:0046185]; cellular aldehyde metabolic process [GO:0006081]; D-glucuronate catabolic process [GO:0042840]; glucose metabolic process [GO:0006006]; L-ascorbic acid biosynthetic process [GO:0019853]alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; electron carrier activity [GO:0009055]; L-glucuronate reductase activity [GO:0047939]apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:11306097, ECO:0000269|PubMed:18276838}.P43005EAA3#Excitatory amino acid transporter 3 Protein digestion and absorptionSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21123949}; Multi-pass membrane protein. Apical cell membrane {ECO:0000269|PubMed:21123949}; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.cysteine transmembrane transport [GO:1903712]; cysteine transport [GO:0042883]; D-aspartate import [GO:0070779]; glutamate secretion [GO:0014047]; ion transport [GO:0006811]; L-glutamate import [GO:0051938]; L-glutamate transmembrane transport [GO:0089711]; neurotransmitter secretion [GO:0007269]; positive regulation of heart rate [GO:0010460]; protein homooligomerization [GO:0051260]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]cysteine transmembrane transporter activity [GO:0033229]; glutamate:sodium symporter activity [GO:0015501]; glutamate binding [GO:0016595]; L-glutamate transmembrane transporter activity [GO:0005313]; sodium:dicarboxylate symporter activity [GO:0017153]apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Transports L-glutamate, L- and D-aspartate and L-cystein (PubMed:21123949). Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium. Negatively regulated by ARL6IP5 (By similarity). {ECO:0000250|UniProtKB:P51906, ECO:0000250|UniProtKB:P51907, ECO:0000269|PubMed:21123949}.Q8TF42UBS3B8Ubiquitin-associated and SH3 domain-containing protein BESUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}.negative regulation of platelet aggregation [GO:0090331]; negative regulation of protein kinase activity [GO:0006469]; regulation of osteoclast differentiation [GO:0045670]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]2protein tyrosine phosphatase activity [GO:0004725]FUNCTION: Interferes with CBL-mediated down-regulation and degradation of receptor-t< ype tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination. {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17880946}.Q8WX93PALLDPalladinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, ruffle. Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere, Z line. Note=Localizes to stress fibers and Z lines.actin cytoskeleton organization [GO:0030036]; cytoskeleton organization [GO:0007010]; epithelial cell morphogenesis [GO:0003382]; keratinocyte development [GO:0003334])muscle alpha-actinin binding [GO:0051371]actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; Z disc [GO:0030018]fFUNCTION: Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci. {ECO:0000269|PubMed:11598191, ECO:0000269|PubMed:15147863, ECO:0000269|PubMed:17537434}.P38935SMBP2DNA-binding protein SMUBP-2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19299493}. Cytoplasm {ECO:0000269|PubMed:19299493}. Cell projection, axon {ECO:0000250}. Note=Colocalizes with the translation initiation factor EIF4G2. {ECO:0000250}.WDNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; protein homooligomerization [GO:0051260]; regulation of transcription, DNA-templated [GO:0006355]; spinal cord motor neuron differentiation [GO:0021522]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]ATP binding [GO:0005524]; ATP-dependent 5'-3' DNA helicase activity [GO:0043141]; ATP-dependent 5'-3' RNA helicase activity [GO:0032575]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; DNA helicase activity [GO:0003678]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; RNA-dependent ATPase activity [GO:0008186]; single-stranded DNA binding [GO:0003697]; transcription factor binding [GO:0008134]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]axon [GO:0030424]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplices in an ATP-dependent reaction. Acts as a transcription regulator. Required for the transcriptional activation of the flounder liver-type antifreeze protein gene. Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. Binds to the insulin II gene RIPE3B enhancer region. May be involved in translation (By similarity). DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. Preferentially binds to the 5'-GGGCT-3' motif. Interacts with tRNA-Tyr. Stimulates the transcription of the human neurotropic virus JCV. {ECO:0000250, ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:19299493}.Q06830PRDX1Peroxiredoxin-1 PeroxisomeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.2cell proliferation [GO:0008283]; erythrocyte homeostasis [GO:0034101]; gene expression [GO:0010467]; hydrogen peroxide catabolic process [GO:0042744]; natural killer cell mediated cytotoxicity [GO:0042267]; regulation of NF-kappaB import into nucleus [GO:0042345]; regulation of stress-activated MAPK cascade [GO:0032872]; removal of superoxide radicals [GO:0019430]; response to reactive oxygen species [GO:0000302]; retina homeostasis [GO:0001895]; skeletal system development [GO:0001501]; transcription initiation from RNA polymerase II promoter [GO:0006367]pperoxidase activity [GO:0004601]; poly(A) RNA binding [GO:0044822]; thioredoxin peroxidase activity [GO:0008379]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]1FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). {ECO:0000250}.P78417GSTO1!Glutathione S-transferase omega-1Glutathione metabolismGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11511179}.^cellular response to arsenic-containing substance [GO:0071243]; glutathione derivative biosynthetic process [GO:1901687]; L-ascorbic acid biosynthetic process [GO:0019853]; L-ascorbic acid metabolic process [GO:0019852]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; positive regulation of ryanodine-sensitive calcium-release channel activity [GO:0060316]; positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014810]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; small molecule metabolic process [GO:0044281]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]glutathione dehydrogenase (ascorbate) activity [GO:0045174]; glutathione transferase activity [GO:0004364]; methylarsonate reductase activity [GO:0050610]; oxidoreductase activity [GO:0016491]axon [GO:0030424]; basement membrane [GO:0005604]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; nuclear membrane [GO:0031965]FUNCTION: Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529}.Q9H299SH3L34SH3 domain-binding glutamic acid-rich-like protein 3cell redox homeostasis [GO:0045454]; positive regulation of GTPase activity [GO:0043547]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of actin filament depolymerization [GO:0030834]; regulation of blood vessel endothelial cell migration [GO:0043535]electron carrier activity [GO:0009055]; GTPase activator activity [GO:0005096]; protein disulfide oxidoreductase activity [GO:0015035]; semaphorin receptor binding [GO:0030215]< lcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; nucleus [GO:0005634]GFUNCTION: Could act as a modulator of glutaredoxin biological activity.P30085KCYUMP-CMP kinasePyrimidine metabolismESUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear.de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside diphosphate phosphorylation [GO:0006165]; nucleoside triphosphate biosynthetic process [GO:0009142]; pyrimidine ribonucleotide biosynthetic process [GO:0009220]; small molecule metabolic process [GO:0044281]; UMP biosynthetic process [GO:0006222]ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; uridine kinase activity [GO:0004849]; uridylate kinase activity [GO:0009041]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132, ECO:0000269|PubMed:23416111}.Q9H0R4HDHD2@Haloacid dehalogenase-like hydrolase domain-containing protein 2;enzyme binding [GO:0019899]; metal ion binding [GO:0046872]Q12765SCRN1 Secernin-1exocytosis [GO:0006887]!dipeptidase activity [GO:0016805]Kcytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]FUNCTION: Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium (By similarity). {ECO:0000250}.Q9NUJ3T11L1#T-complex protein 11-like protein 1microtubule [GO:0005874]Q15181IPYRInorganic pyrophosphatasediphosphate metabolic process [GO:0071344]; gene expression [GO:0010467]; phosphate-containing compound metabolic process [GO:0006796]; tRNA aminoacylation for protein translation [GO:0006418]Qinorganic diphosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287]Q9H3K6BOLA2BolA-like protein 2Q9H4A4AMPBAminopeptidase B'Epithelial-mesenchymal transition (EMT)3Epithelial Cell Surface and Extracellular Moleculesleukotriene biosynthetic process [GO:0019370]; negative regulation of blood pressure [GO:0045776]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; epoxide hydrolase activity [GO:0004301]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]>FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity). {ECO:0000250}.Q99497PARK7 Protein DJ-1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88767}; Lipid-anchor {ECO:0000250|UniProtKB:O88767}. Cytoplasm {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:19229105}. Nucleus {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:15976810}. Membrane raft {ECO:0000250|UniProtKB:O88767}. Mitochondrion {ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105}. Note=Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (PubMed:18711745). Detected in tau inclusions in brains from neurodegenerative disease patients (PubMed:14705119). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation. {ECO:0000269|PubMed:14705119, ECO:0000269|PubMed:18711745}.activation of protein kinase B activity [GO:0032148]; adult locomotory behavior [GO:0008344]; autophagy [GO:0006914]; cellular response to glyoxal [GO:0036471]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to oxidative stress [GO:0034599]; detoxification of copper ion [GO:0010273]; detoxification of mercury ion [GO:0050787]; dopamine uptake involved in synaptic transmission [GO:0051583]; enzyme active site formation via L-cysteine sulfinic acid [GO:0018323]; glycolate biosynthetic process [GO:0046295]; glyoxal catabolic process [GO:1903190]; hydrogen peroxide metabolic process [GO:0042743]; inflammatory response [GO:0006954]; lactate biosynthetic process [GO:0019249]; membrane depolarization [GO:0051899]; membrane hyperpolarization [GO:0060081]; methylglyoxal catabolic process to D-lactate [GO:0019243]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell death [GO:0060548]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268]; negative regulation of death-inducing signaling complex assembly [GO:1903073]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of gene expression [GO:0010629]; negative regulation of hydrogen peroxide-induced cell death [GO:1903206]; negative regulation of hydrogen peroxide-induced neuron death [GO:1903208]; negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway [GO:1903384]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron death [GO:1901215]; negative regulation of oxidative stress-induced cell death [GO:1903202]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein acetylation [GO:1901984]; negative regulation of protein binding [GO:0032091]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of protein K48-linked deubiquitination [GO:1903094]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of TRAIL-activated apoptotic signaling pathway [GO:1903122]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; negative regulation of ubiquitin-specific protease activity [GO:2000157]; positive regulation of androgen receptor activity [GO:2000825]; positive regulation of dopamine biosynthetic process [GO:1903181]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of L-dopa biosynthetic process [GO:1903197]; positive regulation of L-dopa decarboxylase activity [GO:1903200]; positive regulation of mitochondrial electron transport, NADH to ubiquinone [GO:1902958]; positive regulation of mitochondrion degradation [GO:1903599]; positive regulation of oxidative phosphorylation uncoupler activity [GO:2000277]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein homodimerization activity [GO:0090073]; positive re< gulation of protein kinase B signaling [GO:0051897]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of pyrroline-5-carboxylate reductase activity [GO:1903168]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of superoxide dismutase activity [GO:1901671]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; positive regulation of tyrosine 3-monooxygenase activity [GO:1903178]; protein deglycosylation [GO:0006517]; protein stabilization [GO:0050821]; Ras protein signal transduction [GO:0007265]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of fibril organization [GO:1902903]; regulation of inflammatory response [GO:0050727]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of neuron apoptotic process [GO:0043523]; single fertilization [GO:0007338]androgen receptor binding [GO:0050681]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; cytokine binding [GO:0019955]; enzyme binding [GO:0019899]; glyoxalase (glycolic acid-forming) activity [GO:1990422]; glyoxalase III activity [GO:0019172]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-dopa decarboxylase activator activity [GO:0036478]; mercury ion binding [GO:0045340]; mRNA binding [GO:0003729]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; peptidase activity [GO:0008233]; peroxiredoxin activity [GO:0051920]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; repressing transcription factor binding [GO:0070491]; scaffold protein binding [GO:0097110]; small protein activating enzyme binding [GO:0044388]; superoxide dismutase copper chaperone activity [GO:0016532]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; tyrosine 3-monooxygenase activator activity [GO:0036470]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]; ubiquitin-specific protease binding [GO:1990381]axon [GO:0030424]; cell body [GO:0044297]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605] FUNCTION: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) (PubMed:25416785). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745). Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:19229105, PubMed:16632486). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). {ECO:0000250|UniProtKB:Q99LX0, ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12612053, ECO:0000269|PubMed:12855764, ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:14749723, ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:18626009, ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20304780, ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:9070310}.P17655CAN2Calpain-2 catalytic subunitmSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.Xblastocyst development [GO:0001824]; cellular response to amino acid stimulus [GO:0071230]; myoblast fusion [GO:0007520]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of cytoskeleton organization [GO:0051493]; response to hypoxia [GO:0001666]calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; calcium ion binding [GO:0005509]; cysteine-type peptidase activity [GO:0008234]; cytoskeletal protein binding [GO:0008092]chromatin [GO:0000785]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). {ECO:0000269|PubMed:17650508}.P522096PGD16-phosphogluconate dehydrogenase, decarboxylating9carbohydrate metabolic process [GO:0005975]; D-gluconate metabolic process [GO:0019521]; oxidation-reduction process [GO:0055114]; pentose biosynthetic process [GO:0019322]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051]; small molecule metabolic process [GO:0044281]aNADP binding [GO:0050661]; phosphogluconate dehydrogenase (decarboxylating) activity [GO:0004616]Ncytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. {ECO:0000250}.P55957BID$BH3-interacting domain death agonist Pro-apoptosisSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion membrane {ECO:0000250}. Note=When uncleaved, it is predominantly cytoplasmic. {ECO:0000269|PubMed:14583606}.; SUBCELLULAR LOCATION: BH3-interacting domain death agonist p15: Mitochondrion membrane {ECO:0000250}. Note=Translocates to mitochondria as an integral membrane protein. {ECO:0000250}.; SUBCELLULAR LOCATION: BH< 3-interacting domain death agonist p13: Mitochondrion membrane {ECO:0000250}. Note=Associated with the mitochondrial membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion membrane. Note=A significant proportion of isoform 2 localizes to mitochondria, it may be cleaved constitutively._activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; brain development [GO:0007420]; establishment of protein localization to membrane [GO:0090150]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glial cell apoptotic process [GO:0034349]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway [GO:0097193]; mitochondrial outer membrane permeabilization [GO:0097345]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of protein homooligomerization [GO:0032464]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of protein oligomerization [GO:0032461]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; programmed cell death [GO:0012501]; protein homooligomerization [GO:0051260]; protein targeting to mitochondrion [GO:0006626]; regulation of cell proliferation [GO:0042127]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; release of cytochrome c from mitochondria [GO:0001836]; response to estradiol [GO:0032355]; signal transduction in response to DNA damage [GO:0042770]#death receptor binding [GO:0005123]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of mitochondrial membrane [GO:0032592]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739])FUNCTION: The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. {ECO:0000250, ECO:0000269|PubMed:14583606}.Q9NR12PDLI7PDZ and LIM domain protein 7-SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By similarity). {ECO:0000250}. actin cytoskeleton organization [GO:0030036]; cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; ossification [GO:0001503]; positive regulation of osteoblast differentiation [GO:0045669]; receptor-mediated endocytosis [GO:0006898]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; ruffle [GO:0001726]; stress fiber [GO:0001725]4FUNCTION: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity). {ECO:0000250}.P50552VASP%Vasodilator-stimulated phosphoproteinFocal adhesionSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).5actin polymerization or depolymerization [GO:0008154]; axon guidance [GO:0007411]; cell junction assembly [GO:0034329]; neural tube closure [GO:0001843]; positive regulation of actin filament polymerization [GO:0030838]; protein homotetramerization [GO:0051289]; T cell receptor signaling pathway [GO:0050852]profilin binding [GO:0005522]actin cytoskeleton [GO:0015629]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. {ECO:0000269|PubMed:10087267, ECO:0000269|PubMed:10438535, ECO:0000269|PubMed:15939738, ECO:0000269|PubMed:17082196, ECO:0000269|PubMed:18559661}.P68036UB2L3"Ubiquitin-conjugating enzyme E2 L3)SUBCELLULAR LOCATION: Nucleus. Cytoplasm.cell cycle phase transition [GO:0044770]; cell proliferation [GO:0008283]; cellular protein modification process [GO:0006464]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; protein K11-linked ubiquitination [GO:0070979]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; ubiquitin-dependent protein catabolic process [GO:0006511]}ATP binding [GO:0005524]; enzyme binding [GO:0019899]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activator activity [GO:0097027]; ubiquitin-protein transferase activity [GO:0004842]wcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during < the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:15367689, ECO:0000269|PubMed:17003263, ECO:0000269|PubMed:18946090, ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21532592}.O95834EMAL20Echinoderm microtubule-associated protein-like 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11694528}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11694528}. Note=Colocalizes with the microtubule cytoskeleton. Colocalizes with the mitotic spindle.negative regulation of microtubule polymerization [GO:0031115]; regulation of microtubule nucleation [GO:0010968]; sensory perception of sound [GO:0007605]; visual perception [GO:0007601]>microtubule binding [GO:0008017]; tubulin binding [GO:0015631]scytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; spindle [GO:0005819]FUNCTION: Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. {ECO:0000269|PubMed:11694528}.P62942FKB1A*Peptidyl-prolyl cis-trans isomerase FKBP1Ade novo' protein folding [GO:0006458]; amyloid fibril formation [GO:1990000]; calcium ion transmembrane transport [GO:0070588]; chaperone-mediated protein folding [GO:0061077]; extracellular fibril organization [GO:0043206]; heart morphogenesis [GO:0003007]; heart trabecula formation [GO:0060347]; negative regulation of protein phosphatase type 2B activity [GO:0032513]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein binding [GO:0032092]; positive regulation of protein ubiquitination [GO:0031398]; protein folding [GO:0006457]; protein maturation by protein folding [GO:0022417]; protein peptidyl-prolyl isomerization [GO:0000413]; protein refolding [GO:0042026]; regulation of activin receptor signaling pathway [GO:0032925]; regulation of amyloid precursor protein catabolic process [GO:1902991]; regulation of immune response [GO:0050776]; regulation of protein localization [GO:0032880]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; SMAD protein complex assembly [GO:0007183]; T cell activation [GO:0042110]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]~activin binding [GO:0048185]; FK506 binding [GO:0005528]; ion channel binding [GO:0044325]; macrolide binding [GO:0005527]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; signal transducer activity [GO:0004871]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; type I transforming growth factor beta receptor binding [GO:0034713]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; membrane [GO:0016020]; terminal cisterna [GO:0014802]; Z disc [GO:0030018]-FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:9233797}.O75347TBCATubulin-specific chaperone Ade novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; post-chaperonin tubulin folding pathway [GO:0007023]; protein folding [GO:0006457]; tubulin complex assembly [GO:0007021]@chaperone binding [GO:0051087]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]]FUNCTION: Tubulin-folding protein; involved in the early step of the tubulin folding pathway.P06396GELSGelsolinStabilizer(12)eSUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: Isoform 1: Secreted.actin filament capping [GO:0051693]; actin filament polymerization [GO:0030041]; actin filament reorganization [GO:0090527]; actin filament severing [GO:0051014]; actin nucleation [GO:0045010]; aging [GO:0007568]; amyloid fibril formation [GO:1990000]; apoptotic process [GO:0006915]; barbed-end actin filament capping [GO:0051016]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular response to cadmium ion [GO:0071276]; cilium morphogenesis [GO:0060271]; hepatocyte apoptotic process [GO:0097284]; negative regulation of viral entry into host cell [GO:0046597]; oligodendrocyte development [GO:0014003]; phagocytosis, engulfment [GO:0006911]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of actin nucleation [GO:0051127]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of gene expression [GO:0010628]; positive regulation of keratinocyte apoptotic process [GO:1902174]; positive regulation of protein processing in phagocytic vesicle [GO:1903923]; programmed cell death [GO:0012501]; protein destabilization [GO:0031648]; regulation of establishment of T cell polarity [GO:1903903]; regulation of plasma membrane raft polarization [GO:1903906]; regulation of podosome assembly [GO:0071801]; regulation of receptor clustering [GO:1903909]; regulation of wound healing, spreading of epidermal cells [GO:1903689]; renal protein absorption [GO:0097017]; response to ethanol [GO:0045471]; response to folic acid [GO:0051593]; sequestering of actin monomers [GO:0042989]; striated muscle atrophy [GO:0014891]; tissue regeneration [GO:0042246]actin binding [GO:0003779]; calcium ion binding [GO:0005509]; myosin II binding [GO:0045159]; protein domain specific binding [GO:0019904]actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; blood microparticle [GO:0072562]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; myelin sheath [GO:0043209]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; podosome [GO:0002102]; ruffle [GO:0001726]; sarcoplasm [GO:0016528]`FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. {ECO:0000269|PubMed:20393563}.O60664PLIN3 Perilipin-3TSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15545278, ECO:0000269|PubMed:9590177}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000305}. Note=Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails.'vesicle-mediated transport [GO:0016192]cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]; membrane [GO:0016020]FUNCTION: Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network. {ECO:0000269|PubMed:9590177}.P18669PGAM1Phosphoglycerate mutase 1gcanonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; regulation of glycolytic process [GO:0006110]; regulation of pentose-phospha< te shunt [GO:0043456]; respiratory burst [GO:0045730]; small molecule metabolic process [GO:0044281]2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate 2-phosphatase activity [GO:0004083]; bisphosphoglycerate mutase activity [GO:0004082]; phosphoglycerate mutase activity [GO:0004619]; protein kinase binding [GO:0019901]gcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.P11766ADHXAlcohol dehydrogenase class-3ethanol oxidation [GO:0006069]; formaldehyde catabolic process [GO:0046294]; peptidyl-cysteine S-nitrosylation [GO:0018119]; positive regulation of blood pressure [GO:0045777]; respiratory system process [GO:0003016]; response to lipopolysaccharide [GO:0032496]; response to nitrosative stress [GO:0051409]; response to redox state [GO:0051775]; retinoid metabolic process [GO:0001523] alcohol dehydrogenase (NAD) activity [GO:0004022]; electron carrier activity [GO:0009055]; fatty acid binding [GO:0005504]; formaldehyde dehydrogenase activity [GO:0018467]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; zinc ion binding [GO:0008270]>extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.P62937PPIA%Peptidyl-prolyl cis-trans isomerase A5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527992}. Secreted {ECO:0000269|PubMed:16527992}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.blood coagulation [GO:0007596]; entry into host cell [GO:0030260]; establishment of integrated proviral latency [GO:0075713]; leukocyte migration [GO:0050900]; lipid particle organization [GO:0034389]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of protein secretion [GO:0050714]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of viral genome replication [GO:0045069]; RNA-dependent DNA replication [GO:0006278]; uncoating of virus [GO:0019061]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral release from host cell [GO:0019076]; virion assembly [GO:0019068]peptide binding [GO:0042277]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]; unfolded protein binding [GO:0051082]; virion binding [GO:0046790]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.Q7Z4H3HDDC2HD domain-containing protein 2Q08623HDHD1 Pseudouridine-5'-monophosphatase)nucleotide metabolic process [GO:0009117]Rmetal ion binding [GO:0046872]; pseudouridine 5'-phosphatase activity [GO:1990738]FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation. Pseudouridine is then excreted intact in urine. {ECO:0000269|PubMed:20722631}.O75608LYPA1Acyl-protein thioesterase 17fatty acid metabolic process [GO:0006631]; negative regulation of Golgi to plasma membrane protein transport [GO:0042997]; nitric oxide metabolic process [GO:0046209]; protein depalmitoylation [GO:0002084]; regulation of nitric-oxide synthase activity [GO:0050999]; small molecule metabolic process [GO:0044281]zlipase activity [GO:0016298]; lysophospholipase activity [GO:0004622]; palmitoyl-(protein) hydrolase activity [GO:0008474]Tcytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1. Has low lysophospholipase activity. {ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:22399288}.O15037KHNYN Protein KHNYNRNA binding [GO:0003723]O15090ZN536Zinc finger protein 536,SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.negative regulation of neuron differentiation [GO:0045665]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]\metal ion binding [GO:0046872]; retinoic acid-responsive element binding [GO:0044323]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]nucleus [GO:0005634]}FUNCTION: May be involved in transcriptional regulation. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-3'.Q93052LPPLipoma-preferred partnerSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction. Cell membrane. Note=Found in the nucleus, in the cytoplasm and at cell adhesion sites. Shuttles between the cytoplasm and the nucleus. It has been found in sites of cell adhesion such as cell-to-cell contact and focal adhesion which are membrane attachment sites of cells to the extracellular matrix. Mainly nuclear when fused with HMGA2/HMGIC and KMT2A/MLL1.cell adhesion [GO:0007155]gcytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]SFUNCTION: May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. {ECO:0000269|PubMed:10637295, ECO:0000269|Ref.2}.P23528COF1 Cofilin-1#Actin-polymerization regulator (15)SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.actin cytoskeleton organization [GO:0030036]; actin filament depolymerization [GO:0030042]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cytoskeleton organization [GO:0007010]; ephrin receptor signaling pathway [GO:0048013]; establishment of cell polarity [GO:0030010]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; mitotic cytokinesis [GO:0000281]; negative regulation of apoptotic process [GO:0043066]; neural crest cell migration [GO:0001755]; neural fold formation [GO:0001842]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of actin filament depolymerization [GO:0030836]; protein phosphorylation [GO:0006468]; regulati< on of cell morphogenesis [GO:0022604]; regulation of dendritic spine morphogenesis [GO:0061001]; response to amino acid [GO:0043200]; response to virus [GO:0009615]; Rho protein signal transduction [GO:0007266]gcell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; lamellipodium membrane [GO:0031258]; membrane [GO:0016020]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]; vesicle [GO:0031982]FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. {ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:23633677}.O43150ASAP2FArf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Note=Colocalizes with F-actin and ARF6 in phagocytic cups.6positive regulation of catalytic activity [GO:0043085]nenzyme activator activity [GO:0008047]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]BGolgi cisterna membrane [GO:0032580]; plasma membrane [GO:0005886]gFUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration. {ECO:0000269|PubMed:10022920, ECO:0000269|PubMed:10749932, ECO:0000269|PubMed:11304556}.Q8WZA0LZIC Protein LZIC+response to ionizing radiation [GO:0010212]P0CG35TB15BThymosin beta-15B<SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.Uactin filament organization [GO:0007015]; sequestering of actin monomers [GO:0042989]1cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). May be involved in cell migration. {ECO:0000250, ECO:0000269|PubMed:19296525}.P61204ARF3ADP-ribosylation factor 3SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17555535}.phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; protein transport [GO:0015031]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; vesicle-mediated transport [GO:0016192]6GTPase activity [GO:0003924]; GTP binding [GO:0005525]mextracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.P06703S10A6Protein S100-A6pSUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.yaxonogenesis [GO:0007409]; positive regulation of fibroblast proliferation [GO:0048146]; signal transduction [GO:0007165]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; ion transmembrane transporter activity [GO:0015075]; protein homodimerization activity [GO:0042803]; S100 protein binding [GO:0044548]; tropomyosin binding [GO:0005523]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]FUNCTION: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. {ECO:0000269|PubMed:22399290}.Q9NZD2GLTPGlycolipid transfer protein>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980653}.glycolipid transport [GO:0046836]; glycosphingolipid metabolic process [GO:0006687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]iglycolipid binding [GO:0051861]; glycolipid transporter activity [GO:0017089]; lipid binding [GO:0008289]Ocytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. {ECO:0000269|PubMed:15329726, ECO:0000269|PubMed:15504043, ECO:0000269|PubMed:17980653, ECO:0000269|PubMed:18261224}.Q9Y303NAGA4Putative N-acetylglucosamine-6-phosphate deacetylase Amino-sugar metabolismcarbohydrate metabolic process [GO:0005975]; N-acetylglucosamine metabolic process [GO:0006044]; N-acetylneuraminate catabolic process [GO:0019262]ametal ion binding [GO:0046872]; N-acetylglucosamine-6-phosphate deacetylase activity [GO:0008448]HFUNCTION: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. {ECO:0000269|PubMed:22692205}.Q9NR19ACSA)Acetyl-coenzyme A synthetase, cytoplasmic5acetate biosynthetic process [GO:0019413]; acetyl-CoA biosynthetic process from acetate [GO:0019427]; ethanol oxidation [GO:0006069]; lipid biosynthetic process [GO:0008610]; propionate biosynthetic process [GO:0019542]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]\acetate-CoA ligase activity [GO:0003987]; AMP binding [GO:0016208]; ATP binding [GO:0005524]}cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]`FUNCTION: Activates acetate so that it can be used for lipid synthesis or for energy generation.P07195LDHBL-lactate dehydrogenase B chain Fermentationcarbohydrate metabolic process [GO:0005975]; cellular metabolic process [GO:0044237]; lactate metabolic process [GO:0006089]; NAD metabolic process [GO:0019674]; pyruvate metabolic process [GO:0006090]; small molecule metabolic process [GO:0044281]GL-lactate dehydrogenase activity [GO:0004459]; NAD binding [GO:0051287]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]O95361TRI16&Tripartite motif-containing protein 16histone H3 acetylation [GO:0043966]; histone H4 acetylation [GO:0043967]; positive regulation of interleukin-1 beta secretion [GO:0050718]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of retinoic acid receptor signaling pathway [GO:0048386]; positive regulation of transcription, DNA-templated [GO:0045893]; response to growth hormone [GO:0060416]; response to organophosphorus [GO:0046683]; response to retinoic acid [GO:0032526]~DNA binding [GO:0003677]; interleukin-1 binding [GO:0019966]; NACHT domain binding [GO:0032089]; zinc ion binding [GO:0008270]-cytoplasm [GO:0005737]; PML body [GO< :0016605]LFUNCTION: May play a role in the regulation of keratinocyte differentiation.P07737PROF1 Profilin-1actin cytoskeleton organization [GO:0030036]; blood coagulation [GO:0007596]; negative regulation of actin filament bundle assembly [GO:0032232]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of stress fiber assembly [GO:0051497]; neural tube closure [GO:0001843]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of ATPase activity [GO:0032781]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of ruffle assembly [GO:1900029]; protein stabilization [GO:0050821]; regulation of transcription from RNA polymerase II promoter [GO:0006357]actin binding [GO:0003779]; actin monomer binding [GO:0003785]; adenyl-nucleotide exchange factor activity [GO:0000774]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; poly(A) RNA binding [GO:0044822]; proline-rich region binding [GO:0070064]blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. {ECO:0000269|PubMed:18573880}.P48507GSH0-Glutamate--cysteine ligase regulatory subunit Sulfur metabolism^apoptotic mitochondrial changes [GO:0008637]; cellular nitrogen compound metabolic process [GO:0034641]; cysteine metabolic process [GO:0006534]; glutamate metabolic process [GO:0006536]; glutathione biosynthetic process [GO:0006750]; glutathione derivative biosynthetic process [GO:1901687]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of glutamate-cysteine ligase activity [GO:0035229]; regulation of blood vessel size [GO:0050880]; regulation of mitochondrial depolarization [GO:0051900]; response to drug [GO:0042493]; response to nitrosative stress [GO:0051409]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; xenobiotic metabolic process [GO:0006805]enzyme regulator activity [GO:0030234]; glutamate-cysteine ligase activity [GO:0004357]; glutamate-cysteine ligase catalytic subunit binding [GO:0035226]Dcytosol [GO:0005829]; glutamate-cysteine ligase complex [GO:0017109]Q7L9L4MOB1BMOB kinase activator 1BHIPPO YAP inhibitoreSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15067004}. Nucleus {ECO:0000269|PubMed:15067004}.{hippo signaling [GO:0035329]; positive regulation of phosphorylation [GO:0042327]; protein autophosphorylation [GO:0046777]ckinase activator activity [GO:0019209]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]fcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L. {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}.Q9NYJ8TAB28TGF-beta-activated kinase 1 and MAP3K7-binding protein 2SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10882101}; Peripheral membrane protein {ECO:0000269|PubMed:10882101}. Cytoplasm, cytosol {ECO:0000269|PubMed:10882101}. Note=Following IL1 stimulation, translocation occurs from the membrane to cytosol.activation of MAPK activity [GO:0000187]; Fc-epsilon receptor signaling pathway [GO:0038095]; heart development [GO:0007507]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein kinase activity [GO:0045860]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]LK63-linked polyubiquitin binding [GO:0070530]; zinc ion binding [GO:0008270]Rcytosol [GO:0005829]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886]RFUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'-linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187'. Involved in heart development. {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:20493459}.Q9H479FN3KFructosamine-3-kinaseepithelial cell differentiation [GO:0030855]; fructosamine metabolic process [GO:0030389]; fructoselysine metabolic process [GO:0030393]; phosphorylation [GO:0016310]+fructosamine-3-kinase activity [GO:0030387]FUNCTION: May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme.P32455GBP1.Interferon-induced guanylate-binding protein 1YSUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Secreted. Note=Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of interferon-gamma induction. Golgi membrane localization requires isoprenylation and the presence of another IFN-gamma-induced factor.jcytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-2 secretion [GO:1900041]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; negative regulation of T cell receptor signaling pathway [GO:0050860]; regulation of calcium-mediated signaling [GO:0050848]; regulation of protein localization to plasma membrane [GO:1903076]actin binding [GO:0003779]; cytokine binding [GO:0019955]; enzyme binding [GO:0019899]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; Hsp90 protein binding [GO:0051879];< identical protein binding [GO:0042802]; spectrin binding [GO:0030507]Tcytosol [GO:0005829]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]2FUNCTION: Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes. {ECO:0000269|PubMed:22106366}.P68371TBB4BTubulin beta-4B chain Phagosomede novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; movement of cell or subcellular component [GO:0006928]; natural killer cell mediated cytotoxicity [GO:0042267]; organelle organization [GO:0006996]; protein folding [GO:0006457]; protein polymerization [GO:0051258]double-stranded RNA binding [GO:0003725]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; MHC class I protein binding [GO:0042288]; structural constituent of cytoskeleton [GO:0005200]; unfolded protein binding [GO:0051082]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; nucleus [GO:0005634]FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.Q7Z406MYH14 Myosin-14actin filament-based movement [GO:0030048]; actomyosin structure organization [GO:0031032]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; mitochondrion morphogenesis [GO:0070584]; neuronal action potential [GO:0019228]; regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605]; skeletal muscle contraction [GO:0003009]; skeletal muscle tissue development [GO:0007519]; small GTPase mediated signal transduction [GO:0007264]; vocalization behavior [GO:0071625]qactin-dependent ATPase activity [GO:0030898]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146](actomyosin [GO:0042641]; axon [GO:0030424]; brush border [GO:0005903]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; membrane [GO:0016020]; myelin sheath [GO:0043209]; myosin II complex [GO:0016460]; myosin II filament [GO:0097513]; stress fiber [GO:0001725]FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. {ECO:0000250}.O95825QORL1%Quinone oxidoreductase-like protein 1&quinone metabolic process [GO:1901661]gNADP binding [GO:0050661]; NADPH:quinone reductase activity [GO:0003960]; zinc ion binding [GO:0008270]P36405ARL3&ADP-ribosylation factor-like protein 3SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cell projection, cilium. Note=Detected predominantly in the photoreceptor connecting cilium. Present on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules.cilium morphogenesis [GO:0060271]; cytokinesis [GO:0000910]; intraciliary transport [GO:0042073]; kidney development [GO:0001822]; organelle organization [GO:0006996]; photoreceptor cell development [GO:0042461]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; small GTPase mediated signal transduction [GO:0007264]; smoothened signaling pathway [GO:0007224]GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]5centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; midbody [GO:0030496]; nucleus [GO:0005634]; photoreceptor connecting cilium [GO:0032391]; primary cilium [GO:0072372]; spindle microtubule [GO:0005876]FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit. {ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18588884, ECO:0000269|PubMed:22085962}.Q13630FCLGDP-L-fucose synthaseFructose and mannose metabolism Nucleotide-sugar biosynthesisde novo' GDP-L-fucose biosynthetic process [GO:0042351]; cytolysis [GO:0019835]; GDP-mannose metabolic process [GO:0019673]; leukocyte cell-cell adhesion [GO:0007159]coenzyme binding [GO:0050662]; electron carrier activity [GO:0009055]; GDP-4-dehydro-D-rhamnose reductase activity [GO:0042356]; GDP-L-fucose synthase activity [GO:0050577]; isomerase activity [GO:0016853]FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. {ECO:0000269|PubMed:8910301}.Q06210GFPT1@Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1cellular protein metabolic process [GO:0044267]; circadian regulation of gene expression [GO:0032922]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; endoplasmic reticulum unfolded protein response [GO:0030968]; energy reserve metabolic process [GO:0006112]; fructose 6-phosphate metabolic process [GO:0006002]; glutamine metabolic process [GO:0006541]; IRE1-mediated unfolded protein response [GO:0036498]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047]rcarbohydrate binding [GO:0030246]; glutamine-fructose-6-phosphate transaminase (isomerizing) activity [GO:0004360]FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1.P16152CBR1Carbonyl reductase [NADPH] 1Arachidonic acid metabolism*arachidonic acid metabolic process [GO:0019369]; cyclooxygenase pathway [GO:0019371]; drug metabolic process [GO:0017144]; epithelial cell differentiation [GO:0030855]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; vitamin K metabolic process [GO:0042373] 15-hydroxyprostaglandin dehydrogenase (NADP+) activity [GO:0047021]; carbonyl reductase (NADPH) activity [GO:0004090]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; prostaglandin-E2 9-reductase activity [GO:0050221]\cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. {ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:184< 49627, ECO:0000269|PubMed:18826943}.P52565GDIR1 Rho GDP-dissociation inhibitor 1Excretory metabolism(Vasopressin-regulated water reabsorption>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23434736}.rcellular response to mechanical stimulus [GO:0071260]; cellular response to organic cyclic compound [GO:0071407]; cellular response to redox state [GO:0071461]; movement of cell or subcellular component [GO:0006928]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell migration [GO:0030336]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of axonogenesis [GO:0050772]; regulation of axonogenesis [GO:0050770]; regulation of cell shape [GO:0008360]; regulation of protein localization [GO:0032880]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; semaphorin-plexin signaling pathway [GO:0071526]; small GTPase mediated signal transduction [GO:0007264]}fatty acid binding [GO:0005504]; GTPase activator activity [GO:0005096]; Rho GDP-dissociation inhibitor activity [GO:0005094]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; immunological synapse [GO:0001772]; nucleus [GO:0005634]NFUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1. {ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:23434736}.P61923COPZ1Coatomer subunit zeta-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.COPI coating of Golgi vesicle [GO:0048205]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane organization [GO:0061024]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; toxin transport [GO:1901998]4COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.Q15435PP1R7*Protein phosphatase 1 regulatory subunit 7,SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.chromosome segregation [GO:0007059]; positive regulation of protein dephosphorylation [GO:0035307]; regulation of catalytic activity [GO:0050790]benzyme regulator activity [GO:0030234]; protein phosphatase type 1 regulator activity [GO:0008599]ichromosome [GO:0005694]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]EFUNCTION: Regulatory subunit of protein phosphatase 1. {ECO:0000250}.P46734MP2K3:Dual specificity mitogen-activated protein kinase kinase 3MAPKMAPKK1activation of MAPK activity [GO:0000187]; cardiac muscle contraction [GO:0060048]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of apoptotic process [GO:0042981]; regulation of cytokine biosynthetic process [GO:0042035]; regulation of mitotic cell cycle [GO:0007346]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated MAPK cascade [GO:0051403]; stress-activated protein kinase signaling cascade [GO:0031098]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38.A8MXQ7YH010HPutative IQ motif and ankyrin repeat domain-containing protein LOC642574P32119PRDX2Peroxiredoxin-2cellular response to oxidative stress [GO:0034599]; gene expression [GO:0010467]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of apoptotic process [GO:0043066]; regulation of apoptotic process [GO:0042981]; removal of superoxide radicals [GO:0019430]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; transcription initiation from RNA polymerase II promoter [GO:0006367]Oantioxidant activity [GO:0016209]; thioredoxin peroxidase activity [GO:0008379]FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).P30626SORCNSorcinSUBCELLULAR LOCATION: Cytoplasm. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels.Gaction potential [GO:0001508]; calcium ion transport [GO:0006816]; cytoplasmic sequestering of transcription factor [GO:0042994]; heart development [GO:0007507]; intracellular sequestering of iron ion [GO:0006880]; muscle organ development [GO:0007517]; negative regulation of heart rate [GO:0010459]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; negative regulation of< transcription regulatory region DNA binding [GO:2000678]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; proteolysis [GO:0006508]; regulation of calcium ion transport [GO:0051924]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of cell communication by electrical coupling [GO:0010649]; regulation of cell communication by electrical coupling involved in cardiac conduction [GO:1901844]; regulation of heart contraction [GO:0008016]; regulation of high voltage-gated calcium channel activity [GO:1901841]; regulation of relaxation of muscle [GO:1901077]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of striated muscle contraction [GO:0006942]; signal transduction [GO:0007165]; transport [GO:0006810]Pcalcium channel regulator activity [GO:0005246]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; ion channel binding [GO:0044325]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; receptor binding [GO:0005102]axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine neck [GO:0044326]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; T-tubule [GO:0030315]; Z disc [GO:0030018]FUNCTION: Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels. {ECO:0000269|PubMed:17699613}.Q9NYL2MLTK2Mitogen-activated protein kinase kinase kinase MLTSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15684425}. Nucleus {ECO:0000269|PubMed:15684425}. Note=Translocates to the nucleus upon ultraviolet B irradiation.activation of JUN kinase activity [GO:0007257]; activation of MAPKK activity [GO:0000186]; cell cycle arrest [GO:0007050]; cell cycle checkpoint [GO:0000075]; cell death [GO:0008219]; cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; cytoskeleton organization [GO:0007010]; DNA damage checkpoint [GO:0000077]; intracellular signal transduction [GO:0035556]; positive regulation of apoptotic process [GO:0043065]; protein phosphorylation [GO:0006468]; response to radiation [GO:0009314]; response to stress [GO:0006950]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; poly(A) RNA binding [GO:0044822]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, causes cell shrinkage and disruption of actin stress fibers. Isoform 1 may have role in neoplastic cell transformation and cancer development. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'. {ECO:0000269|PubMed:10924358, ECO:0000269|PubMed:11042189, ECO:0000269|PubMed:11836244, ECO:0000269|PubMed:15172994, ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:15684425}.P61457PHS(Pterin-4-alpha-carbinolamine dehydrataseJSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic and/or nuclear.cellular nitrogen compound metabolic process [GO:0034641]; L-phenylalanine catabolic process [GO:0006559]; positive regulation of transcription, DNA-templated [GO:0045893]; protein heterooligomerization [GO:0051291]; protein homotetramerization [GO:0051289]; regulation of protein homodimerization activity [GO:0043496]; small molecule metabolic process [GO:0044281]; tetrahydrobiopterin biosynthetic process [GO:0006729]; transcription, DNA-templated [GO:0006351]4-alpha-hydroxytetrahydrobiopterin dehydratase activity [GO:0008124]; identical protein binding [GO:0042802]; phenylalanine 4-monooxygenase activity [GO:0004505]; transcription coactivator activity [GO:0003713])FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.Q04446GLGB!1,4-alpha-glucan-branching enzymeStarch and sucrose metabolism Glycan biosynthesiscarbohydrate metabolic process [GO:0005975]; generation of precursor metabolites and energy [GO:0006091]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; small molecule metabolic process [GO:0044281]1,4-alpha-glucan branching enzyme activity [GO:0003844]; cation binding [GO:0043169]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]FUNCTION: Required for sufficient glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule and, consequently, in reducing the osmotic pressure within cells.O95359TACC24Transforming acidic coiled-coil-containing protein 2mSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.)astral microtubule organization [GO:0030953]; cell proliferation [GO:0008283]; cerebral cortex development [GO:0021987]; interkinetic nuclear migration [GO:0022027]; microtubule cytoskeleton organization [GO:0000226]; neurogenesis [GO:0022008]; regulation of microtubule-based process [GO:0032886]-nuclear hormone receptor binding [GO:0035257]cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. {ECO:0000250, ECO:0000269|PubMed:10749935}.Q86YD1PTOV1+Prostate tumor-overexpressed gene 1 proteinSUBCELLULAR LOCATION: Cell membrane. Cytoplasm, perinuclear region. Nucleus. Note=Translocates from the cytoplasm to the nucleus at the onset of S-phase. Also localizes to lipid rafts.bregulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: May activate transcription. Required for nuclear translocation of FLOT1. Promotes cell proliferation. {ECO:0000269|PubMed:12598323, ECO:0000269|PubMed:15713644, ECO:0000269|PubMed:17641689}.Q9NVZ3NECP2-Adaptin ear-binding coat-associated protein 2SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with AP-2 at the plasma membrane. {ECO:0000250}.8endocytosis [GO:0006897]; protein transport [GO:0015031]uclathrin vesicle coat [GO:0030125]; coated pit [GO:0005905]; intracellular [GO:0005622]; plasma membrane [GO:0005886]1FUNCTION: Involved in endocytosis. {ECO:0000250}.O00764PDXKPyridoxal kinase;cell proliferation [GO:0008283]; pyridoxal 5'-phosphate salvage [GO:0009443]; pyridoxal phosphate biosynthetic process [GO:0042823]; small molecule metabolic process [GO:0044281]; vitamin B6 metabolic process [GO:0042816]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]DATP binding [GO:0005524]; lithium ion binding [GO:0031403]; magnesium ion bindi< ng [GO:0000287]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803]; pyridoxal kinase activity [GO:0008478]; pyridoxal phosphate binding [GO:0030170]; sodium ion binding [GO:0031402]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]JFUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6.Q7LG56RIR2B1Ribonucleoside-diphosphate reductase subunit M2 B!Modulation of nucleotide pools(3) Genetic information processingpSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates from cytoplasm to nucleus in response to DNA damage.deoxyribonucleoside diphosphate metabolic process [GO:0009186]; deoxyribonucleoside triphosphate metabolic process [GO:0009200]; deoxyribonucleotide biosynthetic process [GO:0009263]; DNA repair [GO:0006281]; gene expression [GO:0010467]; kidney development [GO:0001822]; mitochondrial DNA replication [GO:0006264]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; renal system process [GO:0003014]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]}metal ion binding [GO:0046872]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; ribonucleoside-diphosphate reductase complex [GO:0005971]FUNCTION: Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage. {ECO:0000269|PubMed:10716435, ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:11719458}.O953366PGL6-phosphogluconolactonasecarbohydrate metabolic process [GO:0005975]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051]; small molecule metabolic process [GO:0044281]T6-phosphogluconolactonase activity [GO:0017057]; monosaccharide binding [GO:0048029]FFUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.Q14019COTL1Coactosin-like proteinkSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus membrane; Peripheral membrane protein.Vdefense response to fungus [GO:0050832]; leukotriene biosynthetic process [GO:0019370]7actin binding [GO:0003779]; enzyme binding [GO:0019899]tcytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965]FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis. {ECO:0000269|PubMed:11583571, ECO:0000269|PubMed:19807693}.Q9H993CF211UPF0364 protein C6orf211cellular response to DNA damage stimulus [GO:0006974]; methylation [GO:0032259]; protein methylation [GO:0006479]; regulation of response to DNA damage stimulus [GO:2001020]enzyme binding [GO:0019899]; protein carboxyl O-methyltransferase activity [GO:0051998]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]FUNCTION: O-methyltransferase that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues. Methylates PCNA, suggesting it is involved in the DNA damage response. {ECO:0000269|PubMed:25732820}.Q9GZT9EGLN1Egl nine homolog 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}. Nucleus {ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). Nuclear export requires functional XPO1. {ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}.cardiac muscle tissue morphogenesis [GO:0055008]; cellular response to hypoxia [GO:0071456]; heart trabecula formation [GO:0060347]; labyrinthine layer development [GO:0060711]; negative regulation of cAMP catabolic process [GO:0030821]; negative regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051344]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; oxygen homeostasis [GO:0032364]; peptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]; regulation of angiogenesis [GO:0045765]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; response to hypoxia [GO:0001666]; response to nitric oxide [GO:0071731]; ventricular septum morphogenesis [GO:0060412]enzyme binding [GO:0019899]; iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]; peptidyl-proline 4-dioxygenase activity [GO:0031545]; peptidyl-proline dioxygenase activity [GO:0031543]Bcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:21792862, ECO:0000269|PubMed:25129147}.Q9NQ88TIGAR!Fructose-2,6-bisphosphatase TIGARSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:25928429}. Nucleus {ECO:0000269|PubMed:25928429}. Mitochondrion {ECO:0000269|PubMed:23185017}. Note=Translocated to the mitochondria during hypoxia in a HIF1A-dependent manner (PubMed:23185017). Colocalizes with HK2 in the mitochondria during hypoxia (PubMed:23185017). Translocated to the nucleus during hypoxia and/or genome stress-induced DNA damage responses in cancer cells (PubMed:25928429). Translocation to the mitochondria is enhanced in ischemic cortex after reperfusion and/or during oxygen and glucose deprivation (OGD)/reoxygenation insult in primary neurons (By similarity). {ECO:0000250|UniProtKB:Q8BZA9, ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:25928429}.cellular response to cobalt ion [GO:0071279]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to hypoxia [GO:0071456]; dephosphorylation [GO:0016311]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; gene expression [GO:0010467]; intestinal epithelial cell development [GO:0060576]; negative regulation of glucose catabolic process to lactate via pyruvate [GO:1904024]; negative regulation of gly< colytic process [GO:0045820]; negative regulation of macromitophagy [GO:1901525]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of DNA repair [GO:0045739]; positive regulation of hexokinase activity [GO:1903301]; regulation of pentose-phosphate shunt [GO:0043456]; regulation of response to DNA damage checkpoint signaling [GO:1902153]; response to gamma radiation [GO:0010332]; response to ischemia [GO:0002931]; response to xenobiotic stimulus [GO:0009410]; transcription initiation from RNA polymerase II promoter [GO:0006367]bisphosphoglycerate 2-phosphatase activity [GO:0004083]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]; phosphatase activity [GO:0016791]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular [GO:0005622]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]FUNCTION: Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate (PubMed:19015259). Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production (PubMed:16839880, PubMed:22887998). Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death (PubMed:16839880, PubMed:19713938, PubMed:23726973, PubMed:22887998, PubMed:23817040). Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity (PubMed:23185017). In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage (By similarity). Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation (PubMed:23726973). Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions (By similarity). Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner (PubMed:22887998). Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses (PubMed:25928429). Involved in intestinal tumor progression (PubMed:23726973). {ECO:0000250|UniProtKB:Q8BZA9, ECO:0000269|PubMed:16839880, ECO:0000269|PubMed:19015259, ECO:0000269|PubMed:19713938, ECO:0000269|PubMed:22887998, ECO:0000269|PubMed:23185017, ECO:0000269|PubMed:23726973, ECO:0000269|PubMed:23817040, ECO:0000269|PubMed:25928429}.O75832PSD10/26S proteasome non-ATPase regulatory subunit 1026SeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18040287}. Nucleus {ECO:0000269|PubMed:18040287}.T anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome regulatory particle assembly [GO:0070682]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032])transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; FUNCTION: Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.P61960UFM1Ubiquitin-fold modifier 1eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15071506}. Cytoplasm {ECO:0000269|PubMed:15071506}.protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; response to endoplasmic reticulum stress [GO:0034976]Pcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]:FUNCTION: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847). This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellula< r processes. TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (PubMed:25219498). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress (By similarity). {ECO:0000250|UniProtKB:P61961, ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:25219498}.O60869EDF1,Endothelial differentiation-related factor 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin.kendothelial cell differentiation [GO:0045446]; multicellular organismal development [GO:0007275]; positive regulation of DNA binding [GO:0043388]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of lipid metabolic process [GO:0019216]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]}poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism. {ECO:0000269|PubMed:10567391, ECO:0000269|PubMed:12040021, ECO:0000269|PubMed:15112053, ECO:0000269|PubMed:9813014}.Q14157UBP2L#Ubiquitin-associated protein 2-likeabinding of sperm to zona pellucida [GO:0007339]; hematopoietic stem cell homeostasis [GO:0061484] PcG protein complex [GO:0031519]O96033MOC2A-Molybdopterin synthase sulfur carrier subunithSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:15073332}.molybdopterin cofactor biosynthetic process [GO:0032324]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]Mmolybdopterin synthase activity [GO:0030366]; nucleotide binding [GO:0000166]ecytosol [GO:0005829]; extracellular exosome [GO:0070062]; molybdopterin synthase complex [GO:0019008]&FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. {ECO:0000255|HAMAP-Rule:MF_03051, ECO:0000269|PubMed:12732628}.P55211CASP9 Caspase-9CaspasesDactivation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; aging [GO:0007568]; apoptotic process [GO:0006915]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to UV [GO:0034644]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glial cell apoptotic process [GO:0034349]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet formation [GO:0030220]; positive regulation of neuron apoptotic process [GO:0043525]; programmed cell death [GO:0012501]; regulation of response to DNA damage stimulus [GO:2001020]; response to antibiotic [GO:0046677]; response to cobalt ion [GO:0032025]; response to estradiol [GO:0032355]; response to lipopolysaccharide [GO:0032496]; signal transduction in response to DNA damage [GO:0042770]cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; enzyme activator activity [GO:0008047]; peptidase activity [GO:0008233]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]wapoptosome [GO:0043293]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).; FUNCTION: Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.Q9NTK5OLA1Obg-like ATPase 1JSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167, ECO:0000269|PubMed:20053727}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03167, ECO:0000269|PubMed:20053727}. Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03167, ECO:0000269|PubMed:20053727}. Note=Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm."ATP metabolic process [GO:0046034]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022]centrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]gFUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.Q8WUP2FBLI1Filamin-binding LIM protein 1sSUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Note=Associated with actin stress fiber at cell-ECM focal adhesion sites. Isoform 1 and isoform 3 are recruited and localized at actin stress fibers and clustered at cell-EMC adhesion sites through interaction with FERMT2. Isoform 2 is localized at actin stress fibers.cell junction assembly [GO:0034329]; regulation of cell shape [GO:0008360]; regulation of integrin activation [GO:0033623]; single organismal cell-cell adhesion [GO:0016337];filamin binding [GO:0031005]; zinc ion binding [GO:0008270]fcell cortex [GO:0005938]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; stress fiber [GO:0001725]|FUNCTION: Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion. {ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455, ECO:0000269|PubMed:19074766}.Q9BUF5TBB6Tubulin beta-6 chainde novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; microtubule-based process [GO:0007017]; protein folding [GO:0006457]; protein polymerization [GO:0051258]kGTPase activity [GO:0003924]; GTP binding [GO:0005525]; structural constituent of cytoskeleton [GO:0005200]jcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; nucleus [GO:0005634]FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity< ). {ECO:0000250}.Q9UHV9PFD2Prefoldin subunit 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17936702}. Cytoplasm {ECO:0000269|PubMed:17936702}. Mitochondrion {ECO:0000269|PubMed:17936702}.de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; positive regulation of cytoskeleton organization [GO:0051495]; protein folding [GO:0006457]_protein binding involved in protein folding [GO:0044183]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; prefoldin complex [GO:0016272] FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}.P78318IGBP1 Immunoglobulin-binding protein 1B cell activation [GO:0042113]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of dephosphorylation [GO:0035306]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of microtubule-based movement [GO:0060632]; regulation of protein phosphatase type 2A activity [GO:0034047]; response to interleukin-1 [GO:0070555]; response to tumor necrosis factor [GO:0034612]; signal transduction [GO:0007165]hprotein phosphatase 2A binding [GO:0051721]; protein phosphatase type 2A regulator activity [GO:0008601]Fcytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]sFUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits. {ECO:0000269|PubMed:19818709, ECO:0000269|PubMed:23591866}.P00338LDHAL-lactate dehydrogenase A chaincellular metabolic process [GO:0044237]; cellular response to extracellular stimulus [GO:0031668]; glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089]; NAD metabolic process [GO:0019674]; positive regulation of apoptotic process [GO:0043065]; post-embryonic organ development [GO:0048569]; pyruvate metabolic process [GO:0006090]; response to cAMP [GO:0051591]; response to drug [GO:0042493]; response to estrogen [GO:0043627]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]P28482MK01"Mitogen-activated protein kinase 1Regulators(57)SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Note=Associated with the spindle during prometaphase and metaphase (By similarity). PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser- 246 and Ser-248 as well as autophosphorylation at Thr-190 promote nuclear localization. {ECO:0000250}.activation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; B cell receptor signaling pathway [GO:0050853]; blood coagulation [GO:0007596]; caveolin-mediated endocytosis [GO:0072584]; cell cycle [GO:0007049]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to heat [GO:0034605]; chemotaxis [GO:0006935]; cytosine metabolic process [GO:0019858]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB signaling pathway [GO:0038127]; ERK1 and ERK2 cascade [GO:0070371]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; labyrinthine layer blood vessel development [GO:0060716]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; long-term synaptic potentiation [GO:0060291]; lung morphogenesis [GO:0060425]; mammary gland epithelial cell proliferation [GO:0033598]; MAPK cascade [GO:0000165]; MAPK import into nucleus [GO:0000189]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of cell differentiation [GO:0045596]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; platelet activation [GO:0030168]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of translation [GO:0045727]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of cellular response to heat [GO:1900034]; regulation of cytoskeleton organization [GO:0051493]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of Golgi inheritance [GO:0090170]; regulation of protein stability [GO:0031647]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of stress-activated MAPK cascade [GO:0032872]; response to epidermal growth factor [GO:0070849]; response to estrogen [GO:0043627]; response to exogenous dsRNA [GO:0043330]; response to stress [GO:0006950]; response to toxic substance [GO:0009636]; sensory perception of pain [GO:0019233]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; stress-activated MAPK cascade [GO:0051403]; synaptic transmission [GO:0007268]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; trachea formation [GO:0060440]; transcription, DNA-templated [GO:0006351]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]ATP binding [GO:0005524]; DNA binding [GO:0003677]; MAP kinase activity [GO:0004707]; phosphatase binding [GO:0019902]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]8axon [GO:0030424]; caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; nucleoplas< m [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein complex [GO:0043234]; pseudopodium [GO:0031143]j FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.; FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.Q9UJU6DBNLDrebrin-like proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell projection {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Detected in neuron cell body and cell projections, such as neurites. Colocalizes with cytosolic dynamin in hippocampus neurons (By similarity). Cortical actin cytoskeleton. Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes (By similarity). {ECO:0000250}.activation of JUN kinase activity [GO:0007257]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; immune system process [GO:0002376]; neuron projection morphogenesis [GO:0048812]; podosome assembly [GO:0071800]; programmed cell death [GO:0012501]; Rac protein signal transduction [GO:0016601]; receptor-mediated endocytosis [GO:0006898]; ruffle assembly [GO:0097178]; synapse assembly [GO:0007416]gactin binding [GO:0003779]; actin filament binding [GO:0051015]; enzyme activator activity [GO:0008047]rcell cortex [GO:0005938]; cell junction [GO:0030054]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; podosome [GO:0002102]; postsynaptic density [GO:0014069]; ruffle [GO:0001726]FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. {ECO:0000250, ECO:0000269|PubMed:14729663}.Q15813TBCETubulin-specific chaperone EUSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.de novo' posttranslational protein folding [GO:0051084]; adult locomotory behavior [GO:0008344]; cellular protein metabolic process [GO:0044267]; developmental growth [GO:0048589]; microtubule cytoskeleton organization [GO:0000226]; muscle atrophy [GO:0014889]; peripheral nervous system neuron axonogenesis [GO:0048936]; post-chaperonin tubulin folding pathway [GO:0007023]; post-embryonic development [GO:0009791]; protein folding [GO:0006457]chaperone binding [GO:0051087]0cytoplasm [GO:0005737]; microtubule [GO:0005874]FUNCTION: Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation. {ECO:0000269|PubMed:11847227}.Q16775GLO2/Hydroxyacylglutathione hydrolase, mitochondrial Secondary metabolite metabolismcSUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.Zcarbohydrate metabolic process [GO:0005975]; glutathione biosynthetic process [GO:0006750]Uhydroxyacylglutathione hydrolase activity [GO:0004416]; zinc ion binding [GO:0008270]]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]wFUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.Q9Y2S6TMA7*Translation machinery-associated protein 7P54577SYYC"Tyrosine--tRNA ligase, cytoplasmicAminoacyl-tRNA biosynthesis>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16429158}.apoptotic process [GO:0006915]; gene expression [GO:0010467]; signal transduction [GO:0007165]; tRNA aminoacylation for protein translation [GO:0006418]; tyrosyl-tRNA aminoacylation [GO:0006437]ATP binding [GO:0005524]; interleukin-8 receptor binding [GO:0005153]; poly(A) RNA binding [GO:0044822]; signal transducer activity [GO:0004871]; tRNA binding [GO:0000049]; tyrosine-tRNA ligase activity [GO:0004831]dcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.Q9UIC8LCMT1$Leucine carboxyl methyltransferase 1ncellular protein modification process [GO:0006464]; C-terminal protein methylation [GO:0006481]; negative regulation of protein complex assembly [GO:0031333]< ; protein methylation [GO:0006479]; regulation of apoptotic process [GO:0042981]; regulation of glucose metabolic process [GO:0010906]; regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090266]protein C-terminal carboxyl O-methyltransferase activity [GO:0003880]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]FUNCTION: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. {ECO:0000269|PubMed:10600115}.Q99426TBCBTubulin-folding cofactor B SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15831477}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15831477}. Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone.de novo' posttranslational protein folding [GO:0051084]; cell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; nervous system development [GO:0007399]qcytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]1FUNCTION: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.Q9NQW7XPP1Xaa-Pro aminopeptidase 1Cbradykinin catabolic process [GO:0010815]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; protein homodimerization activity [GO:0042803]FUNCTION: Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.Q9NVD7PARVA Alpha-parvinSUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Constituent of focal adhesions. Associates with the actin cytoskeleton.actin cytoskeleton reorganization [GO:0031532]; actin-mediated cell contraction [GO:0070252]; cell junction assembly [GO:0034329]; cilium morphogenesis [GO:0060271]; establishment or maintenance of cell polarity [GO:0007163]; heterotypic cell-cell adhesion [GO:0034113]; outflow tract septum morphogenesis [GO:0003148]; regulation of cell shape [GO:0008360]; smooth muscle cell chemotaxis [GO:0071670]; sprouting angiogenesis [GO:0002040]; substrate adhesion-dependent cell spreading [GO:0034446]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; Z disc [GO:0030018]FUNCTION: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. {ECO:0000250, ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563}.Q495T6MMEL1%Membrane metallo-endopeptidase-like 1SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Secreted. Note=A secreted form produced by proteollytic cleavage also exists. {ECO:0000250}.endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]FUNCTION: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond (By similarity). {ECO:0000250}.Q96MW1CCD43(Coiled-coil domain-containing protein 43Q9Y2H0DLGP4 Disks large-associated protein 4XSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.signaling [GO:0023052]+membrane [GO:0016020]; synapse [GO:0045202]FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.Q99614TTC1"Tetratricopeptide repeat protein 1protein folding [GO:0006457]9cytoplasm [GO:0005737]; peroxisomal membrane [GO:0005778]Q2TAA2IAH1.Isoamyl acetate-hydrolyzing esterase 1 homolog$lipid catabolic process [GO:0016042]6hydrolase activity, acting on ester bonds [GO:0016788])FUNCTION: Probable lipase. {ECO:0000250}.Q8NC51PAIRB5Plasminogen activator inhibitor 1 RNA-binding proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12505151}. Nucleus {ECO:0000269|PubMed:12505151}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12505151}. Note=Also found in perinuclear regions.Wregulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488]BmRNA 3'-UTR binding [GO:0003730]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay.Q9H1H9KI13AKinesin-like protein KIF13ASUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody. Endosome membrane. Golgi apparatus membrane {ECO:0000250}. Note=Recruited to the midbody during cytokinesis.hcargo loading into vesicle [GO:0035459]; cytokinesis [GO:0000910]; endosome to lysosome transport [GO:0008333]; Golgi to plasma membrane protein transport [GO:0043001]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; microtubule-based movement [GO:0007018]; plus-end-directed vesicle transport along microtubule [GO:0072383]centrosome [GO:0005813]; endosome membrane [GO:0010008]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; trans-Golgi network membrane [GO:0032588].FUNCTION: Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. {ECO:0000269|PubMed:19841138, ECO:0000269|PubMed:20208530}.P53004BIEABiliverdin reductase A) Porphyrin-containing compound metabolismheme catabolic process [GO:0042167]; oxidation-reduction process [GO:0055114]; porphyrin-containing compound metabolic process [GO:0006778]; small molecule metabolic process [GO:0044281]Ibiliverdin reductase activity [GO:0004074]; zinc ion binding [GO:0008270]FUNCTION: Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.< Q9NR09BIRC6+Baculoviral IAP repeat-containing protein 6anti-apoptosis*SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18329369}. Midbody {ECO:0000269|PubMed:18329369}. Endosome {ECO:0000269|PubMed:18329369}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18329369}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18329369}. Note=Concentrates in a pericentriolar compartment in interphase, moves partially to spindle poles in metaphase, and finally localizes to the spindle midzone and the midbody in telophase and during cytokinesis.Yapoptotic process [GO:0006915]; cell division [GO:0051301]; labyrinthine layer development [GO:0060711]; mitotic nuclear division [GO:0007067]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; positive regulation of cell proliferation [GO:0008284]; protein phosphorylation [GO:0006468]; protein ubiquitination [GO:0016567]; regulation of cell proliferation [GO:0042127]; regulation of cytokinesis [GO:0032465]; spongiotrophoblast layer development [GO:0060712]cysteine-type endopeptidase inhibitor activity [GO:0004869]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; endosome [GO:0005768]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; spindle pole [GO:0000922]; trans-Golgi network [GO:0005802]FUNCTION: Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369}.Q99961SH3G1 Endophilin-A2 SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, podosome {ECO:0000269|PubMed:23285027}. Note=Associated with postsynaptic endosomes in hippocampal neurons. {ECO:0000250}.kcentral nervous system development [GO:0007417]; endocytosis [GO:0006897]; signal transduction [GO:0007165]Bidentical protein binding [GO:0042802]; lipid binding [GO:0008289]cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; podosome [GO:0002102]FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity). {ECO:0000250}.Q01432AMPD3AMP deaminase 3ADP metabolic process [GO:0046031]; AMP catabolic process [GO:0006196]; ATP metabolic process [GO:0046034]; energy homeostasis [GO:0097009]; erythrocyte homeostasis [GO:0034101]; GTP metabolic process [GO:0046039]; IMP salvage [GO:0032264]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; small molecule metabolic process [GO:0044281]CAMP deaminase activity [GO:0003876]; metal ion binding [GO:0046872]CFUNCTION: AMP deaminase plays a critical role in energy metabolism.P36507MP2K2:Dual specificity mitogen-activated protein kinase kinase 2activation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; axon guidance [GO:0007411]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation involved in lung morphogenesis [GO:0060502]; ERK1 and ERK2 cascade [GO:0070371]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; MAPK cascade [GO:0000165]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine autophosphorylation [GO:0036289]; positive regulation of axonogenesis [GO:0050772]; positive regulation of cell motility [GO:2000147]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; Ras protein signal transduction [GO:0007265]; regulation of axon regeneration [GO:0048679]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of Golgi inheritance [GO:0090170]; regulation of stress-activated MAPK cascade [GO:0032872]; small GTPase mediated signal transduction [GO:0007264]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; trachea formation [GO:0060440]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]pATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; PDZ domain binding [GO:0030165]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; scaffold protein binding [GO:0097110] cell-cell junction [GO:0005911]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; late endosome [GO:0005770]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases (By similarity). {ECO:0000250}.Q8TF74WIPF2,WAS/WASL-interacting protein family member 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}. Note=Localized to stress fibers and bundles of actin filaments.actin cortical patch assembly [GO:0000147]; actin cortical patch localization [GO:0051666]; actin filament-based movement [GO:0030048]; endocytosis [GO:0006897]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; positive regulation of actin nucleation [GO:0051127]; regulation of cell shape [GO:0008360]; small GTPase mediated signal transduction [GO:0007264]#actin filament binding [GO:0051015]Tactin cortical patch [GO:0030479]; actin filament [GO:0005884]; cytosol [GO:0005829]nFUNCTION: Plays an active role in the formation of cell surface protrusions downstream of activated PDGFB receptors. Plays an important role in actin-microspike formation through cooperation with WASL. May cooperate with WASP and WASL to induce mobilization and reorganization of the actin filament system. {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}.P27816MAP4 Microtubule-associated protein 4cell division [GO:0051301]; establishment of spindle orientation [GO:0051294];< microtubule sliding [GO:0051012]; mitotic spindle organization [GO:0007052]Kpoly(A) RNA binding [GO:0044822]; structural molecule activity [GO:0005198]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; plasma membrane [GO:0005886]tFUNCTION: Non-neuronal microtubule-associated protein. Promotes microtubule assembly. {ECO:0000269|PubMed:10791892}.P62714PP2ABFSerine/threonine-protein phosphatase 2A catalytic subunit beta isoformCatenin-destruction-complex^SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16541025}. Nucleus {ECO:0000269|PubMed:16541025}. Chromosome, centromere {ECO:0000269|PubMed:16541025}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16541025}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles.apoptotic mitochondrial changes [GO:0008637]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of Ras protein signal transduction [GO:0046580]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein dephosphorylation [GO:0006470]; regulation of gene expression [GO:0010468]; response to antibiotic [GO:0046677]; response to endoplasmic reticulum stress [GO:0034976]; response to hydrogen peroxide [GO:0042542]Zmetal ion binding [GO:0046872]; protein serine/threonine phosphatase activity [GO:0004722]chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]; spindle pole [GO:0000922]FUNCTION: PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. {ECO:0000269|PubMed:2555176}.O14562UBFD1)Ubiquitin domain-containing protein UBFD1QFUNCTION: May play a role as NF-kappa-B regulator. {ECO:0000269|PubMed:19285159}.Q96CN7ISOC1+Isochorismatase domain-containing protein 1catalytic activity [GO:0003824];extracellular exosome [GO:0070062]; peroxisome [GO:0005777]P10746HEM4Uroporphyrinogen-III synthasecellular response to amine stimulus [GO:0071418]; cellular response to arsenic-containing substance [GO:0071243]; heme biosynthetic process [GO:0006783]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to antibiotic [GO:0046677]; small molecule metabolic process [GO:0044281]; uroporphyrinogen III biosynthetic process [GO:0006780]Rcofactor binding [GO:0048037]; uroporphyrinogen-III synthase activity [GO:0004852]FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).P22392NDKBNucleoside diphosphate kinase BSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell projection, lamellipodium. Cell projection, ruffle. Note=Isoform 2 is mainly cytoplasmic and isoform 1 and isoform 2 are excluded from the nucleolus. Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cell adhesion [GO:0007155]; cellular response to drug [GO:0035690]; cellular response to fatty acid [GO:0071398]; cellular response to glucose stimulus [GO:0071333]; CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; hippocampus development [GO:0021766]; integrin-mediated signaling pathway [GO:0007229]; lactation [GO:0007595]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; negative regulation of myeloid leukocyte differentiation [GO:0002762]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside triphosphate biosynthetic process [GO:0009142]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of neuron projection development [GO:0010976]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; purine nucleotide metabolic process [GO:0006163]; pyrimidine nucleotide metabolic process [GO:0006220]; regulation of epidermis development [GO:0045682]; regulation of transcription, DNA-templated [GO:0006355]; response to amine [GO:0014075]; response to cAMP [GO:0051591]; response to testosterone [GO:0033574]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; UTP biosynthetic process [GO:0006228]aATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]; protein histidine kinase activity [GO:0004673]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]cell periphery [GO:0071944]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; intracellular [GO:0005622]; lamellipodium [GO:0030027]; mitochondrial outer membrane [GO:0005741]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]yFUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity. {ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:8392752}.P18085ARF4ADP-ribosylation factor 4&SUBCELLULAR LOCATION: Golgi apparatus.Iactivation of phospholipase D activity [GO:0031584]; apical protein localization [GO:0045176]; brain development [GO:0007420]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; epidermal growth factor receptor signaling pathway [GO:0007173]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; negative regulation of apoptotic process [GO:0043066]; organelle organization [GO:0006996]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein ADP-ribosylation [GO:0006471]; protein localization to cilium [GO:0061512]; protein transport [GO:0015031]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to axon injury [GO:0048678]; small GTPase mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192]mepidermal growth factor receptor binding [GO:0005154]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; ruffle membrane [GO:0032587]P51812KS6A3#Ribosomal protein S6 kinase alpha-3ERK kinase target axon guidance [GO:0007411]; cell cycle [GO:0007049]; central nervous system development [GO:0007417]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell growth [GO:0030307]; positiv< e regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of DNA-templated transcription in response to stress [GO:0043620]; regulation of translation in response to stress [GO:0043555]; response to lipopolysaccharide [GO:0032496]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; stress-activated MAPK cascade [GO:0051403]; synaptic transmission [GO:0007268]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]'ATP binding [GO:0005524]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; magnesium ion binding [GO:0000287]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; ribosomal protein S6 kinase activity [GO:0004711]Fcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] FUNCTION: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1. {ECO:0000269|PubMed:10436156, ECO:0000269|PubMed:16213824, ECO:0000269|PubMed:16223362, ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18722121, ECO:0000269|PubMed:8250835, ECO:0000269|PubMed:9770464}.Q96KP4CNDP2"Cytosolic non-specific dipeptidaseArginine and proline metabolism[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:17121880}..cellular nitrogen compound metabolic process [GO:0034641]; glutathione biosynthetic process [GO:0006750]; glutathione derivative biosynthetic process [GO:1901687]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; xenobiotic metabolic process [GO:0006805]carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; tripeptidase activity [GO:0034701]FUNCTION: Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. {ECO:0000269|PubMed:17121880, ECO:0000269|PubMed:19346245}.Q9Y696CLIC4(Chloride intracellular channel protein 49SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic vesicle membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus matrix. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion. Cell junction. Note=Colocalized with AKAP9 at the centrosome and midbody. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Present in an intracellular vesicular compartment that likely represent trans-Golgi network vesicles.angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; branching morphogenesis of an epithelial tube [GO:0048754]; cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; chloride transport [GO:0006821]; endothelial cell morphogenesis [GO:0001886]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; fertilization [GO:0009566]; keratinocyte differentiation [GO:0030216]; multicellular organism growth [GO:0035264]; negative regulation of cell migration [GO:0030336]; regulation of cytoskeleton organization [GO:0051493]; retina vasculature morphogenesis in camera-type eye [GO:0061299]; vacuolar acidification [GO:0007035] actin cytoskeleton [GO:0015629]; apical part of cell [GO:0045177]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; centrosome [GO:0005813]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; microvillus [GO:0005902]; midbody [GO:0030496]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). {ECO:0000269|PubMed:12163372, ECO:0000269|PubMed:14569596, ECO:0000269|PubMed:16176272, ECO:0000269|PubMed:16239224, ECO:0000269|PubMed:18302930, ECO:0000269|PubMed:19247789}.Q6GYQ0RGPA1-Ral GTPase-activating protein subunit alpha-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocated to the nucleus, when associated with TCF3/E12. {ECO:0000250}.activation of GTPase activity [GO:0090630]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of transcription, DNA-templated [GO:0006355]XGTPase activator activity [GO:0005096]; protein heterodimerization activity [GO:0046982]FUNCTION: Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.P09960LKHA4Leukotriene A-4 hydrolase Lipid metabolismarachidonic acid metabolic process [GO:0019369]; inflammatory response [GO:0006954]; leukotriene biosynthetic process [GO:0019370]; leukotriene metab< olic process [GO:0006691]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; response to peptide hormone [GO:0043434]; response to zinc ion [GO:0010043]; small molecule metabolic process [GO:0044281]; Type I pneumocyte differentiation [GO:0060509]*aminopeptidase activity [GO:0004177]; epoxide hydrolase activity [GO:0004301]; leukotriene-A4 hydrolase activity [GO:0004463]; metalloaminopeptidase activity [GO:0070006]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]iFUNCTION: Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity. {ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:1975494, ECO:0000269|PubMed:2244921}.Q04760LGULLactoylglutathione lyase/carbohydrate metabolic process [GO:0005975]; glutathione metabolic process [GO:0006749]; methylglyoxal metabolic process [GO:0009438]; negative regulation of apoptotic process [GO:0043066]; osteoclast differentiation [GO:0030316]; regulation of transcription from RNA polymerase II promoter [GO:0006357]Mlactoylglutathione lyase activity [GO:0004462]; zinc ion binding [GO:0008270]JFUNCTION: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis. {ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}.Q15404RSU1Ras suppressor protein 1.cell junction assembly [GO:0034329]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neural precursor cell proliferation [GO:2000179]; Ras protein signal transduction [GO:0007265]; signal transduction [GO:0007165]Ucytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]FUNCTION: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.Q9H446RWDD1RWD domain-containing protein 1DFUNCTION: Protects DRG2 from proteolytic degradation. {ECO:0000250}.P04075ALDOA Fructose-bisphosphate aldolase ASUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). {ECO:0000250}.actin filament organization [GO:0007015]; ATP biosynthetic process [GO:0006754]; blood coagulation [GO:0007596]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; muscle cell cellular homeostasis [GO:0046716]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; protein homotetramerization [GO:0051289]; regulation of cell shape [GO:0008360]; small molecule metabolic process [GO:0044281]; striated muscle contraction [GO:0006941]actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; tubulin binding [GO:0015631] actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; I band [GO:0031674]; M band [GO:0031430]; membrane [GO:0016020]; nucleus [GO:0005634]; platelet alpha granule lumen [GO:0031093]FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). {ECO:0000250}.P18206VINCVinculin{SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18439753}. Cell junction, adherens junction {ECO:0000269|PubMed:18439753}. Cell membrane {ECO:0000269|PubMed:18439753}; Peripheral membrane protein {ECO:0000269|PubMed:18439753}; Cytoplasmic side {ECO:0000269|PubMed:18439753}. Cell junction, focal adhesion {ECO:0000269|PubMed:18439753}. Note=Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions (By similarity). Colocalizes with LIMD1 in the focal adhesions. {ECO:0000250}.radherens junction assembly [GO:0034333]; apical junction assembly [GO:0043297]; axon extension [GO:0048675]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; epithelial cell-cell adhesion [GO:0090136]; lamellipodium assembly [GO:0030032]; morphogenesis of an epithelium [GO:0002009]; movement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]; negative regulation of cell migration [GO:0030336]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; protein localization to cell surface [GO:0034394]actin binding [GO:0003779]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; dystroglycan binding [GO:0002162]; structural molecule activity [GO:0005198]; ubiquitin protein ligase binding [GO:0031625]actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; brush border [GO:0005903]; cell [GO:0005623]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cell-substrate junction [GO:0030055]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; inner dense plaque of desmosome [GO:0090637]; membrane raft [GO:0045121]; outer dense plaque of desmosome [GO:0090636]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; terminal web [GO:1990357]; zonula adherens [GO:0005915]2FUNCTION: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}.P26639SYTC#Threonine--tRNA ligase, cytoplasmicgene expression [GO:0010467]; threonyl-tRNA aminoacylation [GO:0006435]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]uATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; threonine-tRNA ligase activity [GO:0004829]qactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]P16930FAAAFumarylacetoacetase Amino-acid degradationarginine catabolic process [GO:0006527]; cellular nitrogen compound metabolic process [GO:0034641]; L-phenylalanine catabolic process [GO:0006559]; small molecule metabolic process [GO:0044281]; tyrosine catabolic process [GO:0006572]Ifumarylacetoacetase activity [GO:0004334]; metal ion binding [GO:0046872]Q9BQI5SGIP18SH3-containing GRB2-like protein 3-interacting protein 1SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000305|PubMed:20946875}; Peripheral membrane protein {ECO:0000305|PubMed:20946875}; Cytoplasmic side {ECO:0000305|PubMed:20946875}.endocytosis [GO:0006897]; membrane tubulation [GO:0097320]; positive regulation of energy homeostasis [GO:2000507]; positive regulation of feeding behavior [GO:2000253]; positive regulation of receptor-mediated endocytosis [GO:0048260]; response to dietary excess [GO:0002021]dmicrotubule binding [GO:0008017]; phospholipid binding [GO:0005543]; SH3 domain binding [GO:0017124]AP-2 adaptor complex [GO:0030122]; clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005< 905]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]FUNCTION: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity). {ECO:0000250}.Q9UIL1SCOCShort coiled-coil proteinSUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network. Cytoplasm, cytosol.2positive regulation of macroautophagy [GO:0016239]1cytosol [GO:0005829]; Golgi membrane [GO:0000139]gFUNCTION: Positive regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:22354037}.Q9UHD1CHRD17Cysteine and histidine-rich domain-containing protein 1chaperone-mediated protein folding [GO:0061077]; negative regulation of Rho-dependent protein serine/threonine kinase activity [GO:2000299]; regulation of cellular response to heat [GO:1900034]; regulation of centrosome duplication [GO:0010824]AHsp90 protein binding [GO:0051879]; zinc ion binding [GO:0008270]FUNCTION: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis. {ECO:0000269|PubMed:20230755}.Q15057ACAP2GArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2aSUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.mcellular response to nerve growth factor stimulus [GO:1990090]; protein localization to endosome [GO:0036010]FGTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]5endosome membrane [GO:0010008]; membrane [GO:0016020]nFUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6). {ECO:0000269|PubMed:11062263}.Q99733NP1L4$Nucleosome assembly protein 1-like 4Gpoly(A) RNA binding [GO:0044822]; unfolded protein binding [GO:0051082]dcytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]Q9H1Z4WDR13WD repeat-containing protein 13<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12659815}.0cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]Q9UPP1PHF8Histone lysine demethylase PHF8Chromatin modificationK-demethylasesSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis.Cbrain development [GO:0007420]; chromatin organization [GO:0006325]; G1/S transition of mitotic cell cycle [GO:0000082]; histone H3-K27 demethylation [GO:0071557]; histone H3-K36 demethylation [GO:0070544]; histone H3-K9 demethylation [GO:0033169]; histone H4-K20 demethylation [GO:0035574]; mitotic cell cycle [GO:0000278]; negative regulation of chromatin silencing at rDNA [GO:0061188]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase I promoter [GO:0045943]; transcription, DNA-templated [GO:0006351]schromatin binding [GO:0003682]; histone demethylase activity [GO:0032452]; histone demethylase activity (H3-K27 specific) [GO:0071558]; histone demethylase activity (H3-K36 specific) [GO:0051864]; histone demethylase activity (H3-K9 specific) [GO:0032454]; histone demethylase activity (H4-K20 specific) [GO:0035575]; iron ion binding [GO:0005506]; methylated histone binding [GO:0035064]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]; zinc ion binding [GO:0008270]enuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. {ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419, ECO:0000269|PubMed:20531378, ECO:0000269|PubMed:20548336, ECO:0000269|PubMed:20622853, ECO:0000269|PubMed:20622854}.O14641DVL22Segment polarity protein dishevelled homolog DVL-2DSHxSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity). {ECO:0000250}. canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in regulation of cell proliferation [GO:0044340]; cellular protein localization [GO:0034613]; cochlea morphogenesis [GO:0090103]; convergent extension involved in neural plate elongation [GO:0022007]; heart development [GO:0007507]; hippo signaling [GO:0035329]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; neural tube closure [GO:0001843]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; segment specification [GO:0007379]; small GTPase mediated signal transduction [GO:0007264]; transcription from RNA polymerase II promoter [GO:0006366]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]Efrizzled binding [GO:0005109]; identical protein binding [GO:0042802]apical part of cell [GO:0045177]; clathrin-coated endocytic vesicle [GO:0045334]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple < Wnt genes (By similarity). {ECO:0000250}.Q15633TRBP2#RISC-loading complex subunit TARBP2HSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus.5gene expression [GO:0010467]; miRNA loading onto RISC involved in gene silencing by miRNA [GO:0035280]; multicellular organism growth [GO:0035264]; negative regulation of defense response to virus by host [GO:0050689]; negative regulation of protein kinase activity [GO:0006469]; positive regulation of translation [GO:0045727]; positive regulation of viral genome replication [GO:0045070]; pre-miRNA processing [GO:0031054]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; production of siRNA involved in RNA interference [GO:0030422]; regulation of viral transcription [GO:0046782]; single fertilization [GO:0007338]; siRNA loading onto RISC involved in RNA interference [GO:0035087]; spermatid development [GO:0007286]; targeting of mRNA for destruction involved in RNA interference [GO:0030423]double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; miRNA binding [GO:0035198]; pre-miRNA binding [GO:0070883]; protein homodimerization activity [GO:0042803]; protein N-terminus binding [GO:0047485]; siRNA binding [GO:0035197]cytoplasm [GO:0005737]; cytosol [GO:0005829]; micro-ribonucleoprotein complex [GO:0035068]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]FUNCTION: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs. This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR. {ECO:0000269|PubMed:12475984, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:19219043}.Q16851UGPA,UTP--glucose-1-phosphate uridylyltransferase=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8354390}.carbohydrate metabolic process [GO:0005975]; cellular glucuronidation [GO:0052695]; glucose 1-phosphate metabolic process [GO:0019255]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; small molecule metabolic process [GO:0044281]; UDP-glucose metabolic process [GO:0006011]; UDP-glucuronate biosynthetic process [GO:0006065]; xenobiotic metabolic process [GO:0006805]glucose binding [GO:0005536]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; pyrimidine ribonucleotide binding [GO:0032557]; UTP:glucose-1-phosphate uridylyltransferase activity [GO:0003983]RFUNCTION: Plays a central role as a glucosyl donor in cellular metabolic pathways.P49441INPP$Inositol polyphosphate 1-phosphataseInositol phosphate metabolism Signal transductiondephosphorylation [GO:0016311]; inositol phosphate metabolic process [GO:0043647]; phosphate-containing compound metabolic process [GO:0006796]; phosphatidylinositol phosphorylation [GO:0046854]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]inositol-1,3,4-trisphosphate 1-phosphatase activity [GO:0052829]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; metal ion binding [GO:0046872]P20810ICAL Calpastatinanti-apoptosis(17)Zaging [GO:0007568]; brain development [GO:0007420]; egg activation [GO:0007343]; liver development [GO:0001889]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520]; negative regulation of cell cycle arrest [GO:0071157]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; organ regeneration [GO:0031100]calcium-dependent cysteine-type endopeptidase inhibitor activity [GO:0010859]; endopeptidase inhibitor activity [GO:0004866]; poly(A) RNA binding [GO:0044822]Ycytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.Q13371PHLPPhosducin-like proteinNheterotrimeric G-protein complex assembly [GO:1902605]; intracellular signal transduction [GO:0035556]; negative regulation of protein refolding [GO:0061084]; protein folding [GO:0006457]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; signal transduction [GO:0007165]; visual perception [GO:0007601]XFUNCTION: Isoform 1: Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.; FUNCTION: Isoform 2: Acts as a negative regulator of heterotrimeric G proteins assembly by trapping the preloaded G beta subunits inside the CCT chaperonin.Q96HC4PDLI5PDZ and LIM domain protein 5SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Detected both at presynaptic and postsynaptic sites. {ECO:0000250}.eregulation of dendritic spine morphogenesis [GO:0061001]; regulation of synapse assembly [GO:0051963]~actin binding [GO:0003779]; actinin binding [GO:0042805]; protein kinase C binding [GO:0005080]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cytosol [GO:0005829]; membrane [GO:0016020]; neuron projection [GO:0043005]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Z disc [GO:0030018]FUNCTION: May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity). {ECO:0000250}.P50395GDIB#Rab GDP dissociation inhibitor betaqSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.protein transport [GO:0015031]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192]~GTPase activator activity [GO:0005096]; poly(A) RNA binding [GO:0044822]; Rab GDP-dissociation inhibitor activity [GO:0005093]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; myelin sheath [GO:0043209]; vesicle [GO:0031982]FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.Q13177PAK2%Serine/threonine-protein kinase PAK 2PAKs(6)SUBCELLULAR LOCATION: Serine/threonine-protein kinase PAK 2: Cytoplasm. Note=MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane.; SUBCELLULAR LOCATION: PAK-2p34: Nucleus. Cytoplasm, perinuclear region. Membrane; Lipid-anchor. Note=Interaction with ARHGAP10 probably changes PAK-2p34 location to< cytoplasmic perinuclear region. Myristoylation changes PAK-2p34 location to the membrane.actin cytoskeleton organization [GO:0030036]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:2001271]; negative regulation of protein kinase activity [GO:0006469]; peptidyl-serine phosphorylation [GO:0018105]; phosphorylation [GO:0016310]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein tyrosine kinase activity [GO:0061098]; programmed cell death [GO:0012501]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of defense response to virus by virus [GO:0050690]; regulation of growth [GO:0040008]; regulation of MAPK cascade [GO:0043408]; regulation of mitotic cell cycle [GO:0007346]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; small GTPase mediated signal transduction [GO:0007264]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated protein kinase signaling cascade [GO:0031098]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activator activity [GO:0030296]; Rac GTPase binding [GO:0048365]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation. {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:9171063}.P51570GALK1 Galactokinasecarbohydrate metabolic process [GO:0005975]; galactitol metabolic process [GO:0019402]; galactose catabolic process [GO:0019388]; galactose metabolic process [GO:0006012]; small molecule metabolic process [GO:0044281]]ATP binding [GO:0005524]; galactokinase activity [GO:0004335]; galactose binding [GO:0005534]0FUNCTION: Major enzyme for galactose metabolism.P61088UBE2N!Ubiquitin-conjugating enzyme E2 N#Ubiquitination and modification(11)eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19340006}. Cytoplasm {ECO:0000269|PubMed:19340006}.cellular protein modification process [GO:0006464]; cytokine-mediated signaling pathway [GO:0019221]; DNA double-strand break processing [GO:0000729]; double-strand break repair via homologous recombination [GO:0000724]; Fc-epsilon receptor signaling pathway [GO:0038095]; histone ubiquitination [GO:0016574]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of DNA repair [GO:0045739]; positive regulation of histone modification [GO:0031058]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; postreplication repair [GO:0006301]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; proteolysis [GO:0006508]; regulation of DNA repair [GO:0006282]; regulation of histone ubiquitination [GO:0033182]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; ubiquitin-dependent protein catabolic process [GO:0006511]@ATP binding [GO:0005524]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein complex [GO:0043234]; UBC13-MMS2 complex [GO:0031372]; UBC13-UEV1A complex [GO:0035370]; ubiquitin ligase complex [GO:0000151]FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity). {ECO:0000250}.Q9NQ48LZTL12Leucine zipper transcription factor-like protein 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22072986}.negative regulation of protein localization to ciliary membrane [GO:1903568]; negative regulation of protein< localization to cilium [GO:1903565]; organelle organization [GO:0006996]Lidentical protein binding [GO:0042802]; protein complex binding [GO:0032403]eFUNCTION: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. {ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22510444}.P14618KPYMPyruvate kinase PKMSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.DATP biosynthetic process [GO:0006754]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; glucose metabolic process [GO:0006006]; liver development [GO:0001889]; organ regeneration [GO:0031100]; programmed cell death [GO:0012501]; pyruvate biosynthetic process [GO:0042866]; response to gravity [GO:0009629]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; response to muscle inactivity [GO:0014870]; response to nutrient [GO:0007584]; skeletal muscle tissue regeneration [GO:0043403]; small molecule metabolic process [GO:0044281]ADP binding [GO:0043531]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MHC class II protein complex binding [GO:0023026]; poly(A) RNA binding [GO:0044822]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743].cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular vesicle [GO:1903561]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982]FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. {ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:21620138}.P34949MPIMannose-6-phosphate isomerasecellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose biosynthetic process [GO:0009298]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]Rmannose-6-phosphate isomerase activity [GO:0004476]; zinc ion binding [GO:0008270]FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.P60983GMFBGlia maturation factor beta|learning [GO:0007612]; locomotory behavior [GO:0007626]; negative regulation of Arp2/3 complex-mediated actin nucleation [GO:0034316]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; nervous system development [GO:0007399]; positive regulation of catalytic activity [GO:0043085]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]enzyme activator activity [GO:0008047]; protein kinase inhibitor activity [GO:0004860]; signal transducer activity [GO:0004871]intracellular [GO:0005622]FUNCTION: This protein causes differentiation of brain cells, stimulation of neural regeneration, and inhibition of proliferation of tumor cells.O43583DENRDensity-regulated proteinformation of translation preinitiation complex [GO:0001731]; IRES-dependent translational initiation [GO:0002192]; ribosome disassembly [GO:0032790]3translation initiation factor activity [GO:0003743]FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:20713520}.Q13526PIN16Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1|SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16476580}. Nucleus speckle {ECO:0000269|PubMed:21497122}. Cytoplasm {ECO:0000269|PubMed:21497122}. Note=Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122). {ECO:0000269|PubMed:16476580}.1cell cycle [GO:0007049]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; negative regulation of cell motility [GO:2000146]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of type I interferon production [GO:0032480]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of cytokinesis [GO:0032465]; regulation of mitotic nuclear division [GO:0007088]; regulation of pathway-restricted SMAD protein phosphorylation [GO:0060393]GTPase activating protein binding [GO:0032794]; mitogen-activated protein kinase kinase binding [GO:0031434]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; phosphoserine binding [GO:0050815]; phosphothreonine binding [GO:0050816]cytosol [GO:0005829]; midbody [GO:0030496]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). {ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920, ECO:0000269|PubMed:22608923}.P52306GDS1)Rap1 GTPase-GDP dissociation stimulator 1negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; positive regu< lation of GTPase activity [GO:0043547]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]xcytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]FUNCTION: Stimulates GDP/GTP exchange reaction of a group of small GTP-binding proteins (G proteins) including Rap1a/Rap1b, RhoA, RhoB and KRas, by stimulating the dissociation of GDP from and the subsequent binding of GTP to each small G protein.O14745NHRF1/Na(+)/H(+) exchange regulatory cofactor NHE-RF1FSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Apical cell membrane {ECO:0000250}. Endomembrane system; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Note=Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent manner. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast. Found in microvilli, ruffling membrane and filopodia of HeLa cells. Present in lipid rafts of T-cells. {ECO:0000250}."actin cytoskeleton organization [GO:0030036]; adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; auditory receptor cell stereocilium organization [GO:0060088]; bile acid secretion [GO:0032782]; cellular phosphate ion homeostasis [GO:0030643]; establishment of epithelial cell apical/basal polarity [GO:0045198]; establishment of Golgi localization [GO:0051683]; establishment of nucleus localization [GO:0040023]; establishment of protein localization to plasma membrane [GO:0090002]; gland morphogenesis [GO:0022612]; glutathione transport [GO:0034635]; microvillus assembly [GO:0030033]; negative regulation of catenin import into nucleus [GO:0035414]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of sodium:proton antiporter activity [GO:0032416]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; protein complex assembly [GO:0006461]; regulation of cell shape [GO:0008360]; regulation of cell size [GO:0008361]; regulation of excretion [GO:0044062]; regulation of protein kinase activity [GO:0045859]; regulation of sodium:proton antiporter activity [GO:0032415]; renal absorption [GO:0070293]; renal phosphate ion absorption [GO:0097291]; renal sodium ion transport [GO:0003096]; sensory perception of sound [GO:0007605]; Wnt signaling pathway [GO:0016055]:beta-2 adrenergic receptor binding [GO:0031698]; beta-catenin binding [GO:0008013]; chloride channel regulator activity [GO:0017081]; growth factor receptor binding [GO:0070851]; PDZ domain binding [GO:0030165]; phosphatase binding [GO:0019902]; protein self-association [GO:0043621]; receptor binding [GO:0005102]actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cell periphery [GO:0071944]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; membrane raft [GO:0045121]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; sperm midpiece [GO:0097225]; stereocilium [GO:0032420]; stereocilium bundle tip [GO:0032426]; vesicle [GO:0031982]]FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269|PubMed:10499588, ECO:0000269|PubMed:18784102, ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9430655}.A6NHX0GATL2GATS-like protein 2P60660MYL6Myosin light polypeptide 6axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; skeletal muscle tissue development [GO:0007519]; small GTPase mediated signal transduction [GO:0007264]actin-dependent ATPase activity [GO:0030898]; calcium ion binding [GO:0005509]; motor activity [GO:0003774]; structural constituent of muscle [GO:0008307]brush border [GO:0005903]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; myosin complex [GO:0016459]; unconventional myosin complex [GO:0016461]; vesicle [GO:0031982]BFUNCTION: Regulatory light chain of myosin. Does not bind calcium.Q5TFE4NT5D1+5'-nucleotidase domain-containing protein 1dephosphorylation [GO:0016311]E5'-nucleotidase activity [GO:0008253]; metal ion binding [GO:0046872]Q8N6H7ARFG23ADP-ribosylation factor GTPase-activating protein 2VSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17760859}. Golgi apparatus membrane {ECO:0000269|PubMed:17760859}; Peripheral membrane protein {ECO:0000269|PubMed:17760859}; Cytoplasmic side {ECO:0000269|PubMed:17760859}. Note=Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment.Gprotein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]_FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269|PubMed:17760859}.Q9UNF1MAGD2Melanoma-associated antigen D2membrane [GO:0016020]P12955PEPDXaa-Pro dipeptidaseucellular amino acid metabolic process [GO:0006520]; collagen catabolic process [GO:0030574]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; dipeptidase activity [GO:0016805]; manganese ion binding [GO:0030145]; metallocarboxypeptidase activity [GO:0004181]FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.P41226UBA7+Ubiquitin-like modifier-activating enzyme 7cellular protein modification process [GO:0006464]; cytokine-mediated signaling pathway [GO:0019221]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; ISG15-protein conjugation [GO:0032020]; modification-dependent protein catabolic process [GO:0019941]; negative regulation of type I interferon production [GO:0032480]; protein ubiquitination [GO:0016567]; translesion synthesis [GO:0019985]ATP binding [GO:0005524]; ISG15 activating enzyme activity [GO:0019782]; ubiquitin activating enzyme activity [GO:0004839]; ubiquitin-protein transferase activity [GO:0004842]Dcytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]TFUNCTION: Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquit< in-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000269|PubMed:16254333, ECO:0000269|PubMed:20133869}.Q6UX71PXDC2"Plexin domain-containing protein 2`SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.Oextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]OFUNCTION: May play a role in tumor angiogenesis. {ECO:0000269|PubMed:11559528}.P49589SYCC"Cysteine--tRNA ligase, cytoplasmiccysteinyl-tRNA aminoacylation [GO:0006423]; gene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; cysteine-tRNA ligase activity [GO:0004817]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049],cytoplasm [GO:0005737]; cytosol [GO:0005829]P68366TBA4ATubulin alpha-4A chainde novo' posttranslational protein folding [GO:0051084]; blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; protein folding [GO:0006457]; protein polymerization [GO:0051258]ucytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; microtubule [GO:0005874]O14907TX1B3Tax1-binding protein 3SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the cell membrane by interaction with membrane proteins.qactivation of GTPase activity [GO:0090630]; negative regulation of cell proliferation [GO:0008285]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of Wnt signaling pathway [GO:0030178]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; Wnt signaling pathway [GO:0016055]'protein C-terminus binding [GO:0008022]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:21139582}.O75083WDR1WD repeat-containing protein 1uSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, podosome {ECO:0000269|PubMed:22721921}.blood coagulation [GO:0007596]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of actin filament depolymerization [GO:0030836]; regulation of oligodendrocyte differentiation [GO:0048713]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; sarcomere organization [GO:0045214]; sensory perception of sound [GO:0007605]actin filament [GO:0005884]; cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; myelin sheath [GO:0043209]; podosome [GO:0002102]pFUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. {ECO:0000250}.Q7Z6B0CCD91(Coiled-coil domain-containing protein 91SSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12808037}; Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12808037}; Peripheral membrane protein {ECO:0000269|PubMed:12808037}. Note=Colocalizes with GGA1 and GGA2. May be recruited to the TGN by GGA1 and GGA2.protein transport [GO:0015031]MGolgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654]_FUNCTION: Involved in the regulation of membrane traffic through the trans-Golgi network (TGN).Q15257PTPA1Serine/threonine-protein phosphatase 2A activatoreSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17333320}. Nucleus {ECO:0000269|PubMed:17333320}.0mitotic spindle organization in nucleus [GO:0030472]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; negative regulation of protein dephosphorylation [GO:0035308]; positive regulation of apoptotic process [GO:0043065]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of protein dephosphorylation [GO:0035307]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of phosphoprotein phosphatase activity [GO:0043666]; regulation of protein phosphatase type 2A activity [GO:0034047]|ATP binding [GO:0005524]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase type 2A regulator activity [GO:0008601]; protein tyrosine phosphatase activator activity [GO:0008160]; receptor binding [GO:0005102]calcium channel complex [GO:0034704]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A. {ECO:0000250, ECO:0000269|PubMed:16916641, ECO:0000269|PubMed:17333320}.P68104EF1A1Elongation factor 1-alpha 1RNA TransporterSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens.6cellular protein metabolic process [GO:0044267]; cellular response to epidermal growth factor stimulus [GO:0071364]; gene expression [GO:0010467]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; translational elongation [GO:0006414]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049]\cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation elongation factor 1 complex [GO:0005853]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. {ECO:0000269|PubMed:17177976}.P60174TPISTriosephosphate isomerase Carbohydrate biosynthesiscanonical gl< ycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; multicellular organismal development [GO:0007275]; pentose-phosphate shunt [GO:0006098]; small molecule metabolic process [GO:0044281]_triose-phosphate isomerase activity [GO:0004807]; ubiquitin protein ligase binding [GO:0031625]pcytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634]Q7L1Q6BZW17Basic leucine zipper and W2 domain-containing protein 1-cytoplasm [GO:0005737]; membrane [GO:0016020]wFUNCTION: Enhances histone H4 gene transcription but does not seem to bind DNA directly. {ECO:0000269|PubMed:11524015}.Q15628TRADDETumor necrosis factor receptor type 1-associated DEATH domain proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11684708}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250}.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; death-inducing signaling complex assembly [GO:0071550]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; necroptotic process [GO:0070266]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of apoptotic process [GO:0043065]; positive regulation of hair follicle development [GO:0051798]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein heterooligomerization [GO:0051291]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of necrotic cell death [GO:0010939]; signal transduction [GO:0007165]; tumor necrosis factor-mediated signaling pathway [GO:0033209]binding, bridging [GO:0060090]; death domain binding [GO:0070513]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; membrane raft [GO:0045121]; nucleus [GO:0005634]; receptor complex [GO:0043235]%FUNCTION: The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B. {ECO:0000250}.Q5JVS0HABP4*Intracellular hyaluronan-binding protein 4pSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Transported into the nuclear compartment in activated leukocytes.1blood coagulation [GO:0007596]; cellular response to mechanical stimulus [GO:0071260]; negative regulation of DNA binding [GO:0043392]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sarcomere [GO:0030017]FUNCTION: May be involved in nuclear functions such as the remodeling of chromatin and the regulation of transcription. {ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:16455055}.Q9NRV9HEBP1Heme-binding protein 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12413491}.circadian rhythm [GO:0007623]heme binding [GO:0020037]]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]HFUNCTION: May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities. {ECO:0000269|PubMed:12413491}.P499025NTC Cytosolic purine 5'-nucleotidasegadenosine metabolic process [GO:0046085]; drug metabolic process [GO:0017144]; IMP metabolic process [GO:0046040]; nucleobase-containing small molecule metabolic process [GO:0055086]; phosphorylation [GO:0016310]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide catabolic process [GO:0006195]; small molecule metabolic process [GO:0044281]5'-nucleotidase activity [GO:0008253]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; nucleotide binding [GO:0000166]FUNCTION: May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.Q9Y5B8NDK7Nucleoside diphosphate kinase 7brain development [GO:0007420]; ciliary receptor clustering involved in smoothened signaling pathway [GO:0060830]; CTP biosynthetic process [GO:0006241]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement [GO:0003351]; GTP biosynthetic process [GO:0006183]; intraciliary transport [GO:0042073]; left/right pattern formation [GO:0060972]; UTP biosynthetic process [GO:0006228]mATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]Tcentrosome [GO:0005813]; ciliary basal body [GO:0036064]; intracellular [GO:0005622]FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.Q9BT73PSMG3Proteasome assembly chaperone 3FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes. {ECO:0000269|PubMed:17189198}.Q9UEW8STK396STE20/SPS1-related proline-alanine-rich protein kinasewSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Nucleus when caspase-cleaved. {ECO:0000305}.Aactivation of protein kinase activity [GO:0032147]; cellular hypotonic response [GO:0071476]; intracellular signal transduction [GO:0035556]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of rubidium ion transmembrane transporter activity [GO:2000687]; negative regulation of rubidium ion transport [GO:2000681]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of potassium ion transport [GO:0043268]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of blood pressure [GO:0008217]; regulation of inflammatory response [GO:0050727]; regulation of ion homeostasis [GO:2000021]; regulation of mitotic cell cycle [GO:0007346]; response to stress [GO:0006950]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; receptor signaling protein serine/threonine kinase activity [GO:0004702]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]FUNCTION: May act as a mediator of stress-activated signal< s. Mediates the inhibiton of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. {ECO:0000250|UniProtKB:Q9Z1W9}.Q9P2T1GMPR2GMP reductase 2GMP metabolic process [GO:0046037]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; small molecule metabolic process [GO:0044281]CGMP reductase activity [GO:0003920]; metal ion binding [GO:0046872]8cytosol [GO:0005829]; GMP reductase complex [GO:1902560]FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation. {ECO:0000269|PubMed:12009299, ECO:0000269|PubMed:12669231, ECO:0000269|PubMed:16359702, ECO:0000269|PubMed:22037469}.O00233PSMD9.26S proteasome non-ATPase regulatory subunit 9\anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of insulin secretion [GO:0046676]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of insulin secretion [GO:0032024]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome regulatory particle assembly [GO:0070682]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]_bHLH transcription factor binding [GO:0043425]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome regulatory particle [GO:0005838]rFUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process. {ECO:0000269|PubMed:19490896}.P35579MYH9Myosin-9SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. {ECO:0000269|PubMed:20052411}.actin cytoskeleton reorganization [GO:0031532]; actin filament-based movement [GO:0030048]; actomyosin structure organization [GO:0031032]; angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood vessel endothelial cell migration [GO:0043534]; cytokinesis [GO:0000910]; ephrin receptor signaling pathway [GO:0048013]; establishment of meiotic spindle localization [GO:0051295]; establishment of T cell polarity [GO:0001768]; integrin-mediated signaling pathway [GO:0007229]; in utero embryonic development [GO:0001701]; leukocyte migration [GO:0050900]; meiotic spindle organization [GO:0000212]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte differentiation [GO:0030224]; myoblast fusion [GO:0007520]; negative regulation of actin filament severing [GO:1903919]; phagocytosis, engulfment [GO:0006911]; platelet aggregation [GO:0070527]; platelet formation [GO:0030220]; positive regulation of protein processing in phagocytic vesicle [GO:1903923]; protein transport [GO:0015031]; regulation of cell shape [GO:0008360]; small GTPase mediated signal transduction [GO:0007264]; termination of G-protein coupled receptor signaling pathway [GO:0038032]; uropod organization [GO:0032796]actin binding [GO:0003779]; actin-dependent ATPase activity [GO:0030898]; actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]; motor activity [GO:0003774]; poly(A) RNA binding [GO:0044822]; protein anchor [GO:0043495]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]~actin cytoskeleton [GO:0015629]; actomyosin [GO:0042641]; actomyosin contractile ring [GO:0005826]; brush border [GO:0005903]; cell-cell adherens junction [GO:0005913]; cell leading edge [GO:0031252]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; myosin II complex [GO:0016460]; myosin II filament [GO:0097513]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; ruffle [GO:0001726]; spindle [GO:0005819]; stress fiber [GO:0001725]; uropod [GO:0001931]FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10. {ECO:0000269|PubMed:20052411}.Q02750MP2K1:Dual specificity mitogen-activated protein kinase kinase 1-SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm. Nucleus. Note=Localizes at centrosomes during prometaphase, midzone during anaphase and midbody during telophase/cytokinesis.\ activation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; axon guidance [GO:0007411]; cell cycle arrest [GO:0007050]; cell motility [GO:0048870]; cellular senescence [GO:0090398]; chemotaxis [GO:0006935]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation involved in lung morphogenesis [GO:0060502]; ERK1 and ERK2 cascade [GO:0070371]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; Golgi inheritance [GO:0048313]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; keratinocyte differentiation [GO:0030216]; labyrinthine layer development [GO:0060711]; MAPK cascade [GO:0000165]; melanosome transport [GO:0032402]; mitotic nuclear division [GO:0007067]; movement of cell or subcellular component [GO:0006928]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of cell proliferation [GO:0008285]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; neuron differentiation [GO:0030182]; neurotrophin TRK receptor signaling pathway [GO:< 0048011]; placenta blood vessel development [GO:0060674]; positive regulation of axonogenesis [GO:0050772]; positive regulation of cell migration [GO:0030335]; positive regulation of gene expression [GO:0010628]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; protein heterooligomerization [GO:0051291]; Ras protein signal transduction [GO:0007265]; regulation of axon regeneration [GO:0048679]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of Golgi inheritance [GO:0090170]; regulation of stress-activated MAPK cascade [GO:0032872]; regulation of vascular smooth muscle contraction [GO:0003056]; response to axon injury [GO:0048678]; response to glucocorticoid [GO:0051384]; response to oxidative stress [GO:0006979]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; trachea formation [GO:0060440]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vesicle transport along microtubule [GO:0047496]ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein C-terminus binding [GO:0008022]; protein kinase activity [GO:0004672]; protein N-terminus binding [GO:0047485]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; receptor signaling protein tyrosine phosphatase activity [GO:0004728]/axon [GO:0030424]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; late endosome [GO:0005770]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis. {ECO:0000269|PubMed:14737111, ECO:0000269|PubMed:17101779}.O95352ATG7.Ubiquitin-like modifier-activating enzyme ATG7Regulation of autophagySUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}.adult walking behavior [GO:0007628]; cardiac muscle cell development [GO:0055013]; cellular amino acid metabolic process [GO:0006520]; cellular protein modification process [GO:0006464]; cellular response to hyperoxia [GO:0071455]; cellular response to nitrogen starvation [GO:0006995]; cellular response to starvation [GO:0009267]; central nervous system neuron axonogenesis [GO:0021955]; cerebellar Purkinje cell layer development [GO:0021680]; cerebral cortex development [GO:0021987]; C-terminal protein lipidation [GO:0006501]; defense response to virus [GO:0051607]; late nucleophagy [GO:0044805]; liver development [GO:0001889]; macroautophagy [GO:0016236]; membrane fusion [GO:0061025]; mitochondrion degradation [GO:0000422]; negative regulation of apoptotic process [GO:0043066]; negative regulation of histone H4-K16 acetylation [GO:2000619]; negative stranded viral RNA replication [GO:0039689]; neurological system process [GO:0050877]; piecemeal microautophagy of nucleus [GO:0034727]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mucus secretion [GO:0070257]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein modification process [GO:0031401]; post-embryonic development [GO:0009791]; protein catabolic process [GO:0030163]; protein lipidation [GO:0006497]; protein modification by small protein conjugation [GO:0032446]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567]; pyramidal neuron development [GO:0021860]; regulation of mitochondrion degradation [GO:1903146]; regulation of protein ubiquitination [GO:0031396]; suppression by virus of host autophagy [GO:0039521]Atg12 activating enzyme activity [GO:0019778]; Atg8 activating enzyme activity [GO:0019779]; protein homodimerization activity [GO:0042803]; transcription factor binding [GO:0008134]; ubiquitin activating enzyme activity [GO:0004839]maxoneme [GO:0005930]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; pre-autophagosomal structure [GO:0000407]FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. {ECO:0000269|PubMed:11096062, ECO:0000269|PubMed:16303767, ECO:0000269|PubMed:22170151}.P61077UB2D3"Ubiquitin-conjugating enzyme E2 D3+Protein processing in endoplasmic reticulumSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18508924}; Peripheral membrane protein {ECO:0000269|PubMed:18508924}. Endosome membrane {ECO:0000269|PubMed:18508924}; Peripheral membran< e protein {ECO:0000269|PubMed:18508924}.apoptotic process [GO:0006915]; BMP signaling pathway [GO:0030509]; cellular protein modification process [GO:0006464]; cellular response to hypoxia [GO:0071456]; DNA repair [GO:0006281]; gene expression [GO:0010467]; innate immune response [GO:0045087]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of type I interferon production [GO:0032480]; positive regulation of protein targeting to mitochondrion [GO:1903955]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; ubiquitin-dependent protein catabolic process [GO:0006511]ATP binding [GO:0005524]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]cytosol [GO:0005829]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (By similarity). {ECO:0000250}.Q53HC0CCD92(Coiled-coil domain-containing protein 92SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22863007}.centriole [GO:0005814]P67775PP2AAGSerine/threonine-protein phosphatase 2A catalytic subunit alpha isoformSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16541025}. Nucleus {ECO:0000269|PubMed:16541025}. Chromosome, centromere {ECO:0000269|PubMed:16541025}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16541025}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 (By similarity). {ECO:0000250}.apoptotic process [GO:0006915]; ceramide metabolic process [GO:0006672]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; inactivation of MAPK activity [GO:0000188]; meiotic cell cycle [GO:0051321]; mesoderm development [GO:0007498]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope reassembly [GO:0007084]; negative regulation of cell growth [GO:0030308]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of tyrosine phosphorylation of Stat3 protein [GO:0042518]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; protein dephosphorylation [GO:0006470]; regulation of cell adhesion [GO:0030155]; regulation of cell differentiation [GO:0045595]; regulation of DNA replication [GO:0006275]; regulation of growth [GO:0040008]; regulation of transcription, DNA-templated [GO:0006355]; regulation of Wnt signaling pathway [GO:0030111]; response to organic substance [GO:0010033]; RNA splicing [GO:0008380]; second-messenger-mediated signaling [GO:0019932]@chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase type 2A complex [GO:0000159]; spindle pole [GO:0000922]-FUNCTION: PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. {ECO:0000250, ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:22613722, ECO:0000269|PubMed:9920888}.P04083ANXA1 Annexin A1[SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Note=Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium. Found in the cytoplasm of type II pneumocytes and alveolar macrophages. {ECO:0000250}.2alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen peroxide [GO:0070301]; DNA duplex unwinding [GO:0032508]; DNA rewinding [GO:0036292]; endocrine pancreas development [GO:0031018]; estrous cycle [GO:0044849]; gliogenesis [GO:0042063]; hepatocyte differentiation [GO:0070365]; inflammatory response [GO:0006954]; insulin secretion [GO:0030073]; keratinocyte differentiation [GO:0030216]; movement of cell or subcellular component [GO:0006928]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of apoptotic process [GO:0043066]; negative regulation of interleukin-8 secretion [GO:2000483]; negative regulation of phospholipase A2 activity [GO:1900138]; neutrophil clearance [GO:0097350]; neutrophil homeostasis [GO:0001780]; peptide cross-linking [GO:0018149]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of neutrophil apoptotic process [GO:0033031]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of vesicle fusion [GO:0031340]; prolactin secretion [GO:0070459]; prostate gland development [GO:0030850]; regulation of cell proliferation [GO:0042127]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to interleukin-1 [GO:0070555]; response to peptide hormone [GO:0043434]; response to X-ray [< GO:0010165]; signal transduction [GO:0007165]&annealing helicase activity [GO:0036310]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; double-stranded DNA-dependent ATPase activity [GO:0033676]; helicase activity [GO:0004386]; phospholipase A2 inhibitor activity [GO:0019834]; phospholipid binding [GO:0005543]; protein binding, bridging [GO:0030674]; receptor binding [GO:0005102]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; structural molecule activity [GO:0005198]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cilium [GO:0005929]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; mast cell granule [GO:0042629]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; sarcolemma [GO:0042383]; vesicle [GO:0031982]FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.Q9Y6K9NEMONF-kappa-B essential modulatorRasPI3K/AKTSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14651848}. Nucleus {ECO:0000269|PubMed:14651848}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress.activation of MAPK activity [GO:0000187]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; B cell homeostasis [GO:0001782]; cellular response to DNA damage stimulus [GO:0006974]; establishment of vesicle localization [GO:0051650]; Fc-epsilon receptor signaling pathway [GO:0038095]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of neuron death [GO:1901215]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; response to virus [GO:0009615]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; viral process [GO:0016032]1linear polyubiquitin binding [GO:1990450]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; signal transducer activity [GO:0004871]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; intracellular [GO:0005622]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; spindle pole [GO:0000922]; ubiquitin ligase complex [GO:0000151]FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination. {ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660}.Q9BZV1UBXN6UBX domain-containing protein 6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18656546}. Nucleus {ECO:0000269|PubMed:18656546}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18656546}. Note=Localizes at the centrosome both in interphase and during mitosis.cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Acts in a complex with VCP and cooperates with USP7 in promoting MDM2 deubiquitination and stabilization. MDM2 stabilization leads to MDM2-dependent TP53 degradation. {ECO:0000269|PubMed:18768758}.P50453SPB9 Serpin B9_apoptotic process [GO:0006915]; cellular response to estrogen stimulus [GO:0071391]; immune response [GO:0006955]; mast cell mediated immunity [GO:0002448]; negative regulation by symbiont of host apoptotic process [GO:0033668]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of endopeptidase activity [GO:0010951]; positive regulation of gene expression [GO:0010628]; protection from natural killer cell mediated cytotoxicity [GO:0042270]; response to bacterium [GO:0009617]cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Granzyme B inhibitor.P631041433Z14-3-3 protein zeta/deltaPI3Kinhibitor/FOXOSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Located to stage I to stage IV melanosomes.apoptotic process [GO:0006915]; blood coagulation [GO:0007596]; establishment of Golgi localization [GO:0051683]; gene expression [GO:0010467]; Golgi reassembly [GO:0090168]; intrinsic apoptotic signaling pathway [GO:0097193]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; platelet activation [GO:0030168]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; protein targeting [GO:0006605]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; transcription initiation from RNA polymerase II promoter [GO:0006367]identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]Ablood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]< FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:9360956}.Q9UH65SWP70Switch-associated protein 70SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Nucleus. Cell projection, lamellipodium. Note=In resting B-cells it is localized mainly in the cytoplasm and upon cell activation it is recruited to the plasma membrane and then translocates to the nucleus. In activated, class-switching B-cells it is associated with membrane IgG but not IgM. Localized to loose actin filament arrays located behind actively extending lamellipodia.actin filament bundle assembly [GO:0051017]; isotype switching [GO:0045190]; negative regulation of actin filament depolymerization [GO:0030835]; negative regulation of cell-cell adhesion mediated by integrin [GO:0033633]; negative regulation of peptidyl-serine dephosphorylation [GO:1902309]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of mast cell chemotaxis [GO:0060754]; regulation of protein localization [GO:0032880]TATP binding [GO:0005524]; calcium ion binding [GO:0005509]; DNA binding [GO:0003677]dcytosol [GO:0005829]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. It also mediates signaling of membrane ruffling. Regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion (By similarity). {ECO:0000250}.Q96FW1OTUB1Ubiquitin thioesterase OTUB1`cellular response to DNA damage stimulus [GO:0006974]; cellular response to interleukin-1 [GO:0071347]; DNA repair [GO:0006281]; immune system process [GO:0002376]; negative regulation of double-strand break repair [GO:2000780]; negative regulation of histone H2A K63-linked ubiquitination [GO:1901315]; protein K48-linked deubiquitination [GO:0071108]NEDD8-specific protease activity [GO:0019784]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.; FUNCTION: Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain.O94760DDAH13N(G),N(G)-dimethylarginine dimethylaminohydrolase 1@arginine catabolic process [GO:0006527]; citrulline metabolic process [GO:0000052]; nitric oxide mediated signal transduction [GO:0007263]; positive regulation of angiogenesis [GO:0045766]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; regulation of systemic arterial blood pressure [GO:0003073]amino acid binding [GO:0016597]; catalytic activity [GO:0003824]; dimethylargininase activity [GO:0016403]; metal ion binding [GO:0046872]FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.P35080PROF2 Profilin-2{actin cytoskeleton organization [GO:0030036]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of ruffle assembly [GO:1900028]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of ATPase activity [GO:0032781]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of stress fiber assembly [GO:0051496]; protein stabilization [GO:0050821]; regulation of synaptic vesicle exocytosis [GO:2000300]actin monomer binding [GO:0003785]; adenyl-nucleotide exchange factor activity [GO:0000774]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]scytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; terminal bouton [GO:0043195]FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.P63172DYLT1Dynein light chain Tctex-type 1SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to mitotic spindles. {ECO:0000250}.Zcell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; intracellular transport of viral protein in host cell [GO:0019060]; microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; mitotic nuclear division [GO:0007067]; negative regulation of neurogenesis [GO:0050768]; neuron projection morphogenesis [GO:0048812]; regulation of cytoskeleton organization [GO:0051493]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; regulation of GTPase activity [GO:0043087]; viral entry into host cell [GO:0046718]Cidentical protein binding [GO:0042802]; motor activity [GO:0003774]cytoplasmic dynein complex [GO:0005868]; Golgi apparatus [GO:0005794]; host cell [GO:0043657]; microtubule [GO:0005874]; spindle [GO:0005819]OFUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein. {ECO:0000269|PubMed:18647839}.; FUNCTION: Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cy< toskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Involved in the regulation of mitotic spindle orientation (By similarity). {ECO:0000250}.P11413G6PD#Glucose-6-phosphate 1-dehydrogenaseVcarbohydrate metabolic process [GO:0005975]; cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; cytokine production [GO:0001816]; erythrocyte maturation [GO:0043249]; gene expression [GO:0010467]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glutathione metabolic process [GO:0006749]; lipid metabolic process [GO:0006629]; NADPH regeneration [GO:0006740]; NADP metabolic process [GO:0006739]; negative regulation of protein glutathionylation [GO:0010734]; oxidation-reduction process [GO:0055114]; pentose biosynthetic process [GO:0019322]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051]; regulation of neuron apoptotic process [GO:0043523]; response to ethanol [GO:0045471]; response to food [GO:0032094]; response to organic cyclic compound [GO:0014070]; ribose phosphate biosynthetic process [GO:0046390]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]; transcription initiation from RNA polymerase II promoter [GO:0006367]glucose-6-phosphate dehydrogenase activity [GO:0004345]; glucose binding [GO:0005536]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]+centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]nFUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394}.Q15056IF4H+Eukaryotic translation initiation factor 4HBSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.$cellular protein metabolic process [GO:0044267]; developmental growth [GO:0048589]; gene expression [GO:0010467]; regulation of translational initiation [GO:0006446]; sexual reproduction [GO:0019953]; translation [GO:0006412]; translational initiation [GO:0006413]; viral process [GO:0016032]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA. {ECO:0000269|PubMed:10585411, ECO:0000269|PubMed:11418588}.Q15843NEDD8PSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9353319}. Note=Mainly nuclear.anatomical structure morphogenesis [GO:0009653]; cellular protein modification process [GO:0006464]; protein localization [GO:0008104]; protein neddylation [GO:0045116]; proteolysis [GO:0006508]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to organic cyclic compound [GO:0014070]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ubiquitin-dependent protein catabolic process [GO:0006511]-ubiquitin protein ligase binding [GO:0031625]FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. Attachment of NEDD8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. {ECO:0000269|PubMed:10318914, ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:11953428}.P52594AGFG11Arf-GAP domain and FG repeat-containing protein 13SUBCELLULAR LOCATION: Nucleus. Cytoplasmic vesicle.acrosome assembly [GO:0001675]; intermediate filament organization [GO:0045109]; mRNA export from nucleus [GO:0006406]; multicellular organismal development [GO:0007275]; spermatid nucleus differentiation [GO:0007289]zDNA binding [GO:0003677]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]cell projection [GO:0042995]; cytoplasmic membrane-bounded vesicle [GO:0016023]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; nuclear pore [GO:0005643]FUNCTION: Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. {ECO:0000250, ECO:0000269|PubMed:10613896, ECO:0000269|PubMed:14701878, ECO:0000269|PubMed:15749819}.P31150GDIA$Rab GDP dissociation inhibitor alphaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19570034}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19570034}.negative regulation of axonogenesis [GO:0050771]; negative regulation of protein targeting to membrane [GO:0090315]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of small GTPase mediated signal transduction [GO:0051056]; response to calcium ion [GO:0051592]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]GDP-dissociation inhibitor activity [GO:0005092]; GTPase activator activity [GO:0005096]; Rab GDP-dissociation inhibitor activity [GO:0005093]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; midbody [GO:0030496]; myelin sheath [GO:0043209]; neuron projection [GO:0043005]; protein complex [GO:0043234]qFUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. {ECO:0000269|PubMed:23815289}.Q9UBB4ATX10 Ataxin-10RSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16498633}.{nervous system development [GO:0007399]; neuron projection development [GO:0031175]; protein homotrimerization [GO:0070207]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. {ECO:0000250}.Q9NQP4PFD4Prefoldin subunit 4de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]~cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; prefoldin complex [GO:0016272]P12814ACTN1Alpha-actinin-1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24069336, ECO< :0000269|PubMed:7750553}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:7750553}. Cell membrane {ECO:0000250}. Cell junction {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures (By similarity). {ECO:0000250}.actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; actin filament network formation [GO:0051639]; actin filament organization [GO:0007015]; blood coagulation [GO:0007596]; cell junction assembly [GO:0034329]; extracellular matrix organization [GO:0030198]; focal adhesion assembly [GO:0048041]; negative regulation of cellular component movement [GO:0051271]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; platelet formation [GO:0030220]; platelet morphogenesis [GO:0036344]; regulation of apoptotic process [GO:0042981]; regulation of nucleic acid-templated transcription [GO:1903506]Ractin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; double-stranded RNA binding [GO:0003725]; integrin binding [GO:0005178]; ion channel binding [GO:0044325]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; protein homodimerization activity [GO:0042803]; vinculin binding [GO:0017166]brush border [GO:0005903]; cell-cell junction [GO:0005911]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; pseudopodium [GO:0031143]; ruffle [GO:0001726]; stress fiber [GO:0001725]; Z disc [GO:0030018]FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.Q9UHY1NRBP Nuclear receptor-binding proteinSUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:11956649}. Endomembrane system {ECO:0000269|PubMed:11956649}. Cell projection, lamellipodium {ECO:0000269|PubMed:11956649}. Note=Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia.ER to Golgi vesicle-mediated transport [GO:0006888]; gene expression [GO:0010467]; transcription initiation from RNA polymerase II promoter [GO:0006367]nATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]cell cortex [GO:0005938]; endomembrane system [GO:0012505]; lamellipodium [GO:0030027]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication. {ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397, ECO:0000303|PubMed:11956649}.Q96QG7MTMR9Myotubularin-related protein 9>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16787938}.&enzyme regulator activity [GO:0030234]FUNCTION: Probable pseudophosphatase. Contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}.Q15018F175BBRISC complex subunit Abro1*cellular response to freezing [GO:0071497]"polyubiquitin binding [GO:0031593]2BRISC complex [GO:0070552]; cytoplasm [GO:0005737]FUNCTION: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. May act as a central scaffold protein that assembles the various components of the BRISC complex.Q01518CAP1%Adenylyl cyclase-associated protein 1]SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; activation of adenylate cyclase activity [GO:0007190]; ameboidal-type cell migration [GO:0001667]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; establishment or maintenance of cell polarity [GO:0007163]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165]cortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]FUNCTION: Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity.Q96G28CFA36)Cilia- and flagella-associated protein 36SUBCELLULAR LOCATION: Nucleus {ECO:0000303|PubMed:19680650}. Cytoplasm {ECO:0000303|PubMed:19680650}. Cell projection, cilium, flagellum {ECO:0000305}.Jcell projection [GO:0042995]; cytoplasm [GO:0005737]; nucleus [GO:0005634]*FUNCTION: May act as an effector for ARL3.P80217IN35!Interferon-induced 35 kDa proteinDSUBCELLULAR LOCATION: Nucleus. Note=Nuclear following IFN treatment.bcytokine-mediated signaling pathway [GO:0019221]; type I interferon signaling pathway [GO:0060337]*cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Not yet known.Q15691MARE14Microtubule-associated protein RP/EB family member 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Associated with the microtubule network at the growing distal tip of microtubules. Also enriched at the centrosome.cell division [GO:0051301]; cell proliferation [GO:0008283]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of microtubule polymerization [GO:0031115]; organelle organization [GO:0006996]; positive regulation of microtubule plus-end binding [GO:1903033]; protein localization to microtubule [GO:0035372]; small GTPase mediated signal transduction [GO:0007264]tmicrotubule plus-end binding [GO:0051010]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]cell projection membrane [GO:0031253]; centrosome [GO:0005813]; cortical microtubule cytoskeleton [GO:0030981]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule plus-end [GO:0035371]FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. {ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404}.Q9P0J7KCMF1!E3 ubiquitin-protein ligase KCMF1;ligase activity [GO:0016874]; zinc ion binding [GO:0008270]pFUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination. {ECO:0000269|PubMed:15581609}.Q9ULD2MTUS1)Microtubule-associated tumor suppressor 1'SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10697957, ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=In neurons, translocates into the nucleus after treatment with angiotensin-II. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Localizes with the mitotic spindle during mitosis and with the intercellular bridge during cytokinesis.extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle [GO:0005< 819]FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth. {ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}.Q9Y490TLN1Talin-1SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell surface {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Colocalizes with LAYN at the membrane ruffles. Localized preferentially in focal adhesions than fibrillar adhesions (By similarity). {ECO:0000250}.axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell-cell junction assembly [GO:0007043]; cell-substrate junction assembly [GO:0007044]; cellular protein metabolic process [GO:0044267]; cortical actin cytoskeleton organization [GO:0030866]; cytoskeletal anchoring at plasma membrane [GO:0007016]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; movement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; viral process [GO:0016032]integrin binding [GO:0005178]; LIM domain binding [GO:0030274]; structural constituent of cytoskeleton [GO:0005200]; vinculin binding [GO:0017166]Icell-cell junction [GO:0005911]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587] FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity). {ECO:0000250}.Q9UBI1COMD3 COMM domain-containing protein 3eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.regulation of transcription, DNA-templated [GO:0006355]; sodium ion transport [GO:0006814]; transcription, DNA-templated [GO:0006351]FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (PubMed:23637203). {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:23637203, ECO:0000305|PubMed:21778237}.O75351VPS4B.Vacuolar protein sorting-associated protein 4B+SUBCELLULAR LOCATION: Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells.cell separation after cytokinesis [GO:0000920]; cholesterol transport [GO:0030301]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; endosome to lysosome transport via multivesicular body sorting pathway [GO:0032510]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; negative regulation of cell death [GO:0060548]; negative regulation of exosomal secretion [GO:1903542]; nucleus organization [GO:0006997]; positive regulation of centriole elongation [GO:1903724]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of viral life cycle [GO:1903902]; positive regulation of viral process [GO:0048524]; positive regulation of viral release from host cell [GO:1902188]; potassium ion transport [GO:0006813]; protein depolymerization [GO:0051261]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; regulation of viral process [GO:0050792]; response to lipid [GO:0033993]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; vacuole organization [GO:0007033]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral release from host cell [GO:0019076]ATPase activity [GO:0016887]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Flemming body [GO:0090543]; late endosome membrane [GO:0031902]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:18687924}.Q9P0R6GSKIPGSK3-beta interaction protein>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16981698}.Q9UJF2NGAP"Ras GTPase-activating protein nGAP Classical negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]gcytoplasm [GO:0005737]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]=FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.O95394AGM1Phosphoacetylglucosamine mutasecellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; glucosamine metabolic process [GO:0006041]; glucose 1-phosphate metabolic process [GO:0019255]; hemopoiesis [GO:0030097]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; protein O-linked glycosylation [GO:0006493]; spermatogenesis [GO:0007283]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]magnesium ion binding [GO:0000287]; phosphoacetylglucosamine mutase activity [GO:0004610]; phosphoglucomutase activity [GO:0004614]:FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation. {ECO:0000303|PubMed:24589341, ECO:0000303|PubMed:24698316, ECO:0000303|PubMed:24931394}.Q9UPY3DICEREndoribonuclease Dicer>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16424907}.A angiogenesis [GO:0001525]; apoptotic DNA fragmentation [GO:0006309]; branching morphogenesis of an epithelial tube [GO:0048754]; cardiac muscle cell development [GO:0055013]; cardiac neural crest cell development involved in outflow tract morphogenesis [GO:0061309]; cartilage development [GO:0051216]; cerebral c< ortex development [GO:0021987]; conversion of ds siRNA to ss siRNA [GO:0036404]; conversion of ds siRNA to ss siRNA involved in RNA interference [GO:0033168]; defense response to virus [GO:0051607]; embryonic hindlimb morphogenesis [GO:0035116]; ganglion development [GO:0061548]; gene expression [GO:0010467]; hair follicle cell proliferation [GO:0071335]; hair follicle morphogenesis [GO:0031069]; inner ear receptor cell development [GO:0060119]; intestinal epithelial cell development [GO:0060576]; lung development [GO:0030324]; miRNA loading onto RISC involved in gene silencing by miRNA [GO:0035280]; mRNA stabilization [GO:0048255]; multicellular organism growth [GO:0035264]; myoblast differentiation involved in skeletal muscle regeneration [GO:0014835]; negative regulation of Schwann cell proliferation [GO:0010626]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nerve development [GO:0021675]; neuron projection morphogenesis [GO:0048812]; olfactory bulb interneuron differentiation [GO:0021889]; peripheral nervous system myelin formation [GO:0032290]; positive regulation of gene expression [GO:0010628]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of myelination [GO:0031643]; positive regulation of Schwann cell differentiation [GO:0014040]; post-embryonic development [GO:0009791]; pre-miRNA processing [GO:0031054]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; production of siRNA involved in RNA interference [GO:0030422]; regulation of cell cycle [GO:0051726]; regulation of enamel mineralization [GO:0070173]; regulation of muscle cell apoptotic process [GO:0010660]; regulation of neuron differentiation [GO:0045664]; regulation of oligodendrocyte differentiation [GO:0048713]; regulation of viral genome replication [GO:0045069]; reproductive structure development [GO:0048608]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; siRNA loading onto RISC involved in RNA interference [GO:0035087]; spinal cord motor neuron differentiation [GO:0021522]; spindle assembly [GO:0051225]; spleen development [GO:0048536]; stem cell maintenance [GO:0019827]; targeting of mRNA for destruction involved in RNA interference [GO:0030423]; zygote asymmetric cell division [GO:0010070]ATP binding [GO:0005524]; deoxyribonuclease I activity [GO:0004530]; double-stranded RNA binding [GO:0003725]; endoribonuclease activity [GO:0004521]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; pre-miRNA binding [GO:0070883]; protein domain specific binding [GO:0019904]; ribonuclease III activity [GO:0004525]; siRNA binding [GO:0035197]4ARC complex [GO:0033167]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; growth cone [GO:0030426]; micro-ribonucleoprotein complex [GO:0035068]; nucleus [GO:0005634]; RISC-loading complex [GO:0070578]FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes. {ECO:0000269|PubMed:15242644, ECO:0000269|PubMed:15973356, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:19219043}.P06733ENOA Alpha-enolase{SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10802057}. Cell membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.; SUBCELLULAR LOCATION: Isoform MBP-1: Nucleus.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; negative regulation of cell growth [GO:0030308]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; response to virus [GO:0009615]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]'DNA binding [GO:0003677]; GTPase binding [GO:0051020]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; M band [GO:0031430]; membrane [GO:0016020]; nucleus [GO:0005634]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]FUNCTION: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.; FUNCTION: MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.P30711GSTT1!Glutathione S-transferase theta-1glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805][glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]nFUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide. {ECO:0000269|PubMed:16298388, ECO:0000269|PubMed:20097269}.P17931LEG3 Galectin-3SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. Note=Secreted by a non-classical secretory pathway and associates with the cell surface.eosinophil chemotaxis [GO:0048245]; epithelial cell differentiation [GO:0030855]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; macrophage chemotaxis [GO:0048246]; monocyte chemotaxis [GO:0002548]; mononuclear cell migration [GO:0071674]; mRNA processing [GO:0006397]; negative regulation of endocytosis [GO:0045806]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of immunological synapse formation [GO:2000521]; negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:2001189]; negative regulation of T cell receptor signaling pathway [GO:0050860]; neutrophil chemotaxis [GO:0030593]; positive chemotaxis [GO:0050918]; positive regulation of calcium ion import [GO:0090280]; positive regulation of mononuclear cell migration [GO:0071677]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of T cell apoptotic process [GO:0070232]; regulation of T cell proliferation [GO:0042129]; RNA splicing [GO:0008380< ]; skeletal system development [GO:0001501]carbohydrate binding [GO:0030246]; chemoattractant activity [GO:0042056]; IgE binding [GO:0019863]; laminin binding [GO:0043236]; poly(A) RNA binding [GO:0044822]ycytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; immunological synapse [GO:0001772]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]; spliceosomal complex [GO:0005681]FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. {ECO:0000250, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:19594635, ECO:0000269|PubMed:19616076}.P53618COPBCoatomer subunit betaKSUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity). Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity). Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity). Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity). Very little found in plasma membrane fraction (By similarity). {ECO:0000250}.COPI coating of Golgi vesicle [GO:0048205]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane organization [GO:0061024]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; viral process [GO:0016032])structural molecule activity [GO:0005198]]COPI vesicle coat [GO:0030126]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]$FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. {ECO:0000250, ECO:0000269|PubMed:18385291, ECO:0000269|PubMed:18725938, ECO:0000269|PubMed:19364919, ECO:0000269|PubMed:20056612}.A6NDU8CE051UPF0600 protein C5orf51Q9NRN7ADPPTIL-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12815048}.pantothenate metabolic process [GO:0015939]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]^holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:0000287]TFUNCTION: Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN. {ECO:0000269|PubMed:11286508, ECO:0000269|PubMed:12815048, ECO:0000269|PubMed:18022563}.Q01433AMPD2AMP deaminase 2AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; cyclic purine nucleotide metabolic process [GO:0052652]; energy homeostasis [GO:0097009]; GTP metabolic process [GO:0046039]; IMP biosynthetic process [GO:0006188]; IMP salvage [GO:0032264]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; small molecule metabolic process [GO:0044281]FUNCTION: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. {ECO:0000269|PubMed:23911318}.P40855PEX19 Peroxisomal biogenesis factor 19SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Lipid-anchor; Cytoplasmic side. Note=Mainly cytoplasmic. Some fraction membrane-associated to the outer surface of peroxisomes.chaperone-mediated protein folding [GO:0061077]; chaperone-mediated protein transport [GO:0072321]; establishment of protein localization to peroxisome [GO:0072663]; negative regulation of lipid binding [GO:1900131]; peroxisome fission [GO:0016559]; peroxisome membrane biogenesis [GO:0016557]; peroxisome organization [GO:0007031]; protein import into peroxisome membrane [GO:0045046]; protein stabilization [GO:0050821]; protein targeting to peroxisome [GO:0006625]; transmembrane transport [GO:0055085]ATPase binding [GO:0051117]; peroxisome membrane class-1 targeting sequence binding [GO:0036105]; protein N-terminus binding [GO:0047485]>brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein complex [GO:0043234]FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the< integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53. {ECO:0000269|PubMed:10051604, ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:11259404, ECO:0000269|PubMed:11883941, ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:15007061}.O43399TPD54Tumor protein D54-regulation of cell proliferation [GO:0042127]poly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]Dcytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]P13489RINIRibonuclease inhibitormRNA catabolic process [GO:0006402]; negative regulation of catalytic activity [GO:0043086]; regulation of angiogenesis [GO:0045765],ribonuclease inhibitor activity [GO:0008428]_angiogenin-PRI complex [GO:0032311]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:14515218, ECO:0000269|PubMed:17292889}.P09972ALDOC Fructose-bisphosphate aldolase CTcanonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; epithelial cell differentiation [GO:0030855]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]_cytoskeletal protein binding [GO:0008092]; fructose-bisphosphate aldolase activity [GO:0004332]ocytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]P31939PUR9-Bifunctional purine biosynthesis protein PURHde novo' IMP biosynthetic process [GO:0006189]; brainstem development [GO:0003360]; cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; dihydrofolate metabolic process [GO:0046452]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside metabolic process [GO:0009116]; organ regeneration [GO:0031100]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to inorganic substance [GO:0010035]; small molecule metabolic process [GO:0044281]; tetrahydrofolate biosynthetic process [GO:0046654]IMP cyclohydrolase activity [GO:0003937]; phosphoribosylaminoimidazolecarboxamide formyltransferase activity [GO:0004643]; protein homodimerization activity [GO:0042803]kcytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]kFUNCTION: Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. {ECO:0000269|PubMed:14966129}.P30520PURA2%Adenylosuccinate synthetase isozyme 2VSUBCELLULAR LOCATION: Cytoplasm. Note=Partially associated with particulate fractions.Gde novo' AMP biosynthetic process [GO:0044208]; AMP biosynthetic process [GO:0006167]; aspartate metabolic process [GO:0006531]; cellular response to electrical stimulus [GO:0071257]; immune system process [GO:0002376]; IMP metabolic process [GO:0046040]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to ammonium ion [GO:0060359]; response to purine-containing compound [GO:0014074]; small molecule metabolic process [GO:0044281]adenylosuccinate synthase activity [GO:0004019]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; phosphate ion binding [GO:0042301]ncytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.Q15819UB2V2)Ubiquitin-conjugating enzyme E2 variant 2Ubiquitination and modificationcell proliferation [GO:0008283]; DNA double-strand break processing [GO:0000729]; error-free postreplication DNA repair [GO:0042275]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of DNA repair [GO:0045739]; positive regulation of neuron projection development [GO:0010976]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of synapse assembly [GO:0051965]; postreplication repair [GO:0006301]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of DNA repair [GO:0006282]ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]qcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; UBC13-MMS2 complex [GO:0031372]xFUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. {ECO:0000269|PubMed:10089880, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:9705497}.Q5JSZ5PRC2BProtein PRRC2BQ9UBQ7GRHPR.Glyoxylate reductase/hydroxypyruvate reductaseMcellular nitrogen compound metabolic process [GO:0034641]; dicarboxylic acid metabolic process [GO:0043648]; excretion [GO:0007588]; glyoxylate metabolic process [GO:0046487]; metabolic process [GO:0008152]; oxidation-reduction process [GO:0055114]; protein oligomerization [GO:0051259]; small molecule metabolic process [GO:0044281]carboxylic acid binding [GO:0031406]; glycerate dehydrogenase activity [GO:0008465]; glyoxylate reductase (NADP) activity [GO:0030267]; hydroxypyruvate reductase activity [GO:0016618]; NAD binding [GO:0051287]; NADPH binding [GO:0070402]; protein homodimerization activity [GO:0042803]qcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; peroxisomal matrix [GO:0005782]FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.P62495ERF11Eukaryotic peptide chain release factor subunit 1mRNA surveillance pathway9cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; protein methylation [GO:0006479]; regulation of translational termination [GO:0006449]; translation [GO:0006412]; translational termination [GO:0006415]poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation release factor activity [GO:0003747]; translation release factor activity, codon specific [GO:0016149]; translation termination factor activity [GO:0008079]]cytoplasm [GO:0005737]; cytosol [GO:0005829]; translation release factor complex [GO:0018444]NFUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. {ECO:0000269|PubMed:7990965}.Q9NWT6HIF1N*Hypoxia-inducible factor 1-alpha inhibitorSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.< cellular response to hypoxia [GO:0071456]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061428]; oxidation-reduction process [GO:0055114]; peptidyl-asparagine hydroxylation [GO:0042265]; peptidyl-aspartic acid hydroxylation [GO:0042264]; peptidyl-histidine hydroxylation [GO:0036138]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of vasculogenesis [GO:2001214]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; transcription, DNA-templated [GO:0006351]vankyrin repeat binding [GO:0071532]; carboxylic acid binding [GO:0031406]; cofactor binding [GO:0048037]; iron ion binding [GO:0005506]; NF-kappaB binding [GO:0051059]; Notch binding [GO:0005112]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]; oxygen sensor activity [GO:0019826]; peptidyl-asparagine 3-dioxygenase activity [GO:0036140]; peptidyl-histidine dioxygenase activity [GO:0036139]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]tcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000269|PubMed:12042299, ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:17003112, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:21251231}.Q9UNH7SNX6Sorting nexin-6ySUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:11485546, ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774}. Early endosome membrane {ECO:0000269|PubMed:19935774, ECO:0000303|PubMed:11485546}; Peripheral membrane protein {ECO:0000269|PubMed:11485546}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000269|PubMed:20354142}. Cytoplasm {ECO:0000269|PubMed:20830743}. Nucleus {ECO:0000269|PubMed:11591366, ECO:0000269|PubMed:20830743}. Note=Interaction with SNX1 or SNX2 promotes location at endosome membranes (PubMed:19935774). Only a minor proportion is seen in the nucleus. {ECO:0000269|PubMed:19935774}.endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle organization [GO:0016050]xdynactin binding [GO:0034452]; phosphatidylinositol binding [GO:0035091]; protein homodimerization activity [GO:0042803]$cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extrinsic component of membrane [GO:0019898]; intracellular [GO:0005622]; nucleus [GO:0005634]; retromer complex [GO:0030904]; tubular endosome [GO:0097422]FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:19935774). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R (PubMed:17148574). May function as link between transport vesicles and dynactin (Probable). Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network (PubMed:20354142). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B (By similarity). May contribute to transcription regulation (Probable). {ECO:0000250|UniProtKB:Q6P8X1, ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:20354142, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:24610942, ECO:0000303|PubMed:19935774, ECO:0000303|PubMed:20830743, ECO:0000305}.Q5SNT6FA21BWASH complex subunit FAM21BO60749SNX2Sorting nexin-2SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}; Peripheral membrane protein {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}; Cytoplasmic side {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}. Cell projection, lamellipodium {ECO:0000269|PubMed:20604901}. Note=Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles (PubMed:18088323). Colocalized with F-actin at the leading edge of lamellipodia in cells in a KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}.early endosome to Golgi transport [GO:0034498]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; lamellipodium morphogenesis [GO:0072673]; protein oligomerization [GO:0051259]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle organization [GO:0016050]epidermal growth factor receptor binding [GO:0005154]; insulin receptor binding [GO:0005158]; leptin receptor binding [GO:1990460]; phosphatidylinositol binding [GO:0035091]; transferrin receptor binding [GO:1990459]lcytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane [GO:0016020]; protein complex [GO:0043234]; retromer complex [GO:0030904]FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:16179610). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:17101778). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). {ECO:00002< 69|PubMed:16179610, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:20138391, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:23085988, ECO:0000303|PubMed:16179610}.P48444COPDCoatomer subunit delta8adult locomotory behavior [GO:0008344]; cerebellar Purkinje cell layer maturation [GO:0021691]; COPI coating of Golgi vesicle [GO:0048205]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; pigmentation [GO:0043473]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]clathrin adaptor complex [GO:0030131]; COPI vesicle coat [GO:0030126]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.P51452DUS3&Dual specificity protein phosphatase 3phasphotase inhibit ERK<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10224087}.inactivation of MAPK activity [GO:0000188]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of JNK cascade [GO:0046329]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell receptor signaling pathway [GO:0050860]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of mitotic cell cycle [GO:0045931]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]MAP kinase phosphatase activity [GO:0033549]; protein kinase binding [GO:0019901]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2. {ECO:0000269|PubMed:10224087, ECO:0000269|PubMed:11863439}.P53611PGTB2.Geranylgeranyl transferase type-2 subunit beta|cellular protein modification process [GO:0006464]; protein geranylgeranylation [GO:0018344]; visual perception [GO:0007601]sRab geranylgeranyltransferase activity [GO:0004663]; Rab GTPase binding [GO:0017137]; zinc ion binding [GO:0008270]:Rab-protein geranylgeranyltransferase complex [GO:0005968]FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.O43768ENSAAlpha-endosulfinecell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of catalytic activity [GO:0043086]; regulation of insulin secretion [GO:0050796]; regulation of protein phosphatase type 2A activity [GO:0034047]; response to glucose [GO:0009749]; response to nutrient [GO:0007584]; transport [GO:0006810]Iion channel inhibitor activity [GO:0008200]; phosphatase inhibitor activity [GO:0019212]; potassium channel inhibitor activity [GO:0019870]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase inhibitor activity [GO:0004864]; protein phosphatase type 2A regulator activity [GO:0008601]; receptor binding [GO:0005102]WFUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents. {ECO:0000250, ECO:0000269|PubMed:9653196}.Q9BTE6AASD1"Alanyl-tRNA editing protein Aarsd1'alanyl-tRNA aminoacylation [GO:0006419]alanine-tRNA ligase activity [GO:0004813]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]mFUNCTION: Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala). {ECO:0000250}.P55209NP1L1$Nucleosome assembly protein 1-like 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.cellular response to peptide hormone stimulus [GO:0071375]; DNA replication [GO:0006260]; nucleosome assembly [GO:0006334]; positive regulation of cell proliferation [GO:0008284]; Schwann cell proliferation [GO:0014010]dmelanosome [GO:0042470]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleus [GO:0005634]oFUNCTION: May be involved in modulating chromatin formation and contribute to regulation of cell proliferation.Q15631TSNTranslineSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11801738}. Nucleus {ECO:0000269|PubMed:11801738}.~DNA recombination [GO:0006310]; gene expression [GO:0010467]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]DNA binding [GO:0003677]; endoribonuclease activity [GO:0004521]; mRNA binding [GO:0003729]; sequence-specific DNA binding [GO:0043565]; single-stranded DNA binding [GO:0003697]FUNCTION: DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.; FUNCTION: Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.Q9H0A8COMD4 COMM domain-containing protein 4FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF-kappa-B. {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.Q9BR76COR1B Coronin-1BSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16027158}. Note=Localized to the leading edge in fibroblasts, as well as weakly along actin stress fibers.actin cytoskeleton organization [GO:0030036]; actin filament branching [GO:0090135]; actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cellular response to platelet-derived g< rowth factor stimulus [GO:0036120]; endothelial cell chemotaxis [GO:0035767]; negative regulation of Arp2/3 complex-mediated actin nucleation [GO:0034316]; negative regulation of smooth muscle cell chemotaxis [GO:0071672]; positive regulation of lamellipodium morphogenesis [GO:2000394]; protein localization to cell leading edge [GO:1902463]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; ruffle organization [GO:0031529]; wound healing [GO:0042060]pactin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; identical protein binding [GO:0042802]kactin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cell leading edge [GO:0031252]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]FUNCTION: Regulates leading edge dynamics and cell motility in fibroblasts. May be involved in cytokinesis and signal transduction (By similarity). {ECO:0000250}.P07900HS90AHeat shock protein HSP 90-alphaSUBCELLULAR LOCATION: Cytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.'axon guidance [GO:0007411]; cellular response to heat [GO:0034605]; chaperone-mediated protein complex assembly [GO:0051131]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; G2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; mitochondrial transport [GO:0006839]; mitotic cell cycle [GO:0000278]; nitric oxide metabolic process [GO:0046209]; organelle organization [GO:0006996]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; protein import into mitochondrial outer membrane [GO:0045040]; protein refolding [GO:0042026]; receptor-mediated endocytosis [GO:0006898]; regulation of cellular response to heat [GO:1900034]; regulation of nitric-oxide synthase activity [GO:0050999]; response to antibiotic [GO:0046677]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]yATPase activity [GO:0016887]; ATP binding [GO:0005524]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; MHC class II protein complex binding [GO:0023026]; nitric-oxide synthase regulator activity [GO:0030235]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; TPR domain binding [GO:0030911]Qcytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; melanosome [GO:0042470]; membrane [GO:0016020]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123}.Q92734TFG Protein TFGipositive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]'signal transducer activity [GO:0004871]FUNCTION: Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules. {ECO:0000269|PubMed:23479643}.Q07866KLC1Kinesin light chain 1SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:14970196}.Gantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon cargo transport [GO:0008088]; blood coagulation [GO:0007596]; microtubule-based movement [GO:0007018]; small GTPase mediated signal transduction [GO:0007264]; stress granule disassembly [GO:0035617]; viral process [GO:0016032]Dmicrotubule motor activity [GO:0003777]; motor activity [GO:0003774]axon [GO:0030424]; ciliary rootlet [GO:0035253]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.Q16543CDC37Hsp90 co-chaperone Cdc37 Enhencer AKT=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9482106}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; posttranscriptional regulation of gene expression [GO:0010608]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; protein targeting [GO:0006605]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of type I interferon-mediated signaling pathway [GO:0060338]chaperone binding [GO:0051087]; heat shock protein binding [GO:0031072]; kinase binding [GO:0019900]; protein kinase regulator activity [GO:0019887]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; HSP90-CDC37 chaperone complex [GO:1990565]; ruffle membrane [GO:0032587]FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. {ECO:0000269|PubMed:8666233}.P49023PAXIPaxillin OrganizerSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20489202}. Cell junction, focal adhesion {ECO:0000269|PubMed:20489202}. Cytoplasm, cell cortex {ECO:0000250}. Note=Colocalizes with integrins at the cell periphery. {ECO:0000250}.activation of MAPK activity [GO:0000187]; branching morphogenesis of an epithelial tube [GO:0048754]; cell adhesion [GO:0007155]; cell junction assembly [GO:0034329]; cellular response to reactive oxygen species [GO:0034614]; cytoskeleton organization [GO:0007010]; epidermal growth factor receptor signaling pathway [GO:0007173]; focal adhesion assembly [GO:0048041]; growth hormone receptor signaling pathway [GO:0060396]; integrin-mediated signaling pathway [GO:0007229]; lamellipodium assembly [GO:0030032]; muscle contraction [GO:0006936]; peptidyl-tyrosine phosphorylation [GO:0018108]; regulation of cell shape [GO:0008360]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]; substrate adhesion-dependent cell spreading [GO:0034446]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]_beta-catenin binding [GO:0008013]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; microtubule associated complex [GO:0005875]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]FUNCTION: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).Q8WZA9IRGQ(Immunity-related GTPase family Q proteinGTP binding [GO:0005525]Q9Y281COF2 Cofilin-2ZSUBCELLULAR L< OCATION: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.actin filament depolymerization [GO:0030042]; muscle cell cellular homeostasis [GO:0046716]; positive regulation of actin filament depolymerization [GO:0030836]; sarcomere organization [GO:0045214]actin cytoskeleton [GO:0015629]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; I band [GO:0031674]; nuclear matrix [GO:0016363]FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods (By similarity). {ECO:0000250}.Q96SU4OSBL9+Oxysterol-binding protein-related protein 9SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:20599956}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:20599956}. Note=Localizes at the Golgi-late endosome interface.lipid transport [GO:0006869]Ycytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]P46926GNPI1#Glucosamine-6-phosphate isomerase 1carbohydrate metabolic process [GO:0005975]; generation of precursor metabolites and energy [GO:0006091]; glucosamine catabolic process [GO:0006043]; N-acetylglucosamine metabolic process [GO:0006044]; single fertilization [GO:0007338]Xglucosamine-6-phosphate deaminase activity [GO:0004342]; hydrolase activity [GO:0016787]FUNCTION: Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). {ECO:0000250}.O95747OXSR1$Serine/threonine-protein kinase OSR1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22361696}.activation of protein kinase activity [GO:0032147]; cellular hypotonic response [GO:0071476]; intracellular signal transduction [GO:0035556]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of rubidium ion transmembrane transporter activity [GO:2000687]; peptidyl-threonine phosphorylation [GO:0018107]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; response to oxidative stress [GO:0006979]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine/threonine kinase activity [GO:0004674]; receptor signaling protein serine/threonine kinase activity [GO:0004702]FUNCTION: Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton. {ECO:0000269|PubMed:14707132, ECO:0000303|PubMed:14707132}.P23526SAHHAdenosylhomocysteinase"Cysteine and methionine metabolismJcellular nitrogen compound metabolic process [GO:0034641]; chronic inflammatory response to antigenic stimulus [GO:0002439]; circadian sleep/wake cycle [GO:0042745]; homocysteine biosynthetic process [GO:0071268]; methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]; S-adenosylhomocysteine catabolic process [GO:0019510]; S-adenosylmethionine cycle [GO:0033353]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; xenobiotic metabolic process [GO:0006805]nadenosylhomocysteinase activity [GO:0004013]; adenyl nucleotide binding [GO:0030554]; NAD binding [GO:0051287]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; neuron projection [GO:0043005]; nucleus [GO:0005634]:FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000269|PubMed:12590576}.Q9Y4E1FA21CWASH complex subunit FAM21CSUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:20498093}. Cell membrane. Note=Partially colocalizes with RAB11A, a recycling endosome marker. Associates with lipid raft microdomains on the plasma membrane.#negative regulation of barbed-end actin filament capping [GO:2000813]; protein transport [GO:0015031]; regulation of substrate adhesion-dependent cell spreading [GO:1900024]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde transport, endosome to plasma membrane [GO:1990126]phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; plasma membrane [GO:0005886]; WASH complex [GO:0071203]FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission (PubMed:19922874, PubMed:20498093, PubMed:22513087, PubMed:23331060). Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552). Required for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC subunit VPS35 (PubMed:24980502). Required for the endosomal recruitment of CCC complex subunits COMMD1, CCDC93 AND C16orf62 (PubMed:25355947). Plays a role in fluid-phase endocytosis, a process exploited by vaccinia intracellular mature virus (IMV) to enter cells. As a result, may facilitate the penetration of IMV into cells (PubMed:18550675). {ECO:0000269|PubMed:18550675, ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:22513087, ECO:0000269|PubMed:23331060, ECO:0000269|PubMed:24980502, ECO:0000269|PubMed:25278552, ECO:0000269|PubMed:25355947}.Q99836MYD886Myeloid differentiation primary response protein MyD88NFKappaBIL1B/R[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15492225}.M3'-UTR-mediated mRNA stabilization [GO:0070935]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of apoptotic process [GO:0043066]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of interleukin-23 production [GO:0032747]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of type I interferon production [GO:0032481]; regulation of inflammatory response [GO:0050727]; response to interleukin-1 [GO:0070555]; signal transduction [GO:0007165]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-l< ike receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]ldeath receptor binding [GO:0005123]; identical protein binding [GO:0042802]; TIR domain binding [GO:0070976] FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine. {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:24316379, ECO:0000269|PubMed:9013863}.Q6NSW5FA45BProtein FAM45BP13798ACPHAcylamino-acid-releasing enzymeEbeta-amyloid metabolic process [GO:0050435]; proteolysis [GO:0006508]xomega peptidase activity [GO:0008242]; poly(A) RNA binding [GO:0044822]; serine-type endopeptidase activity [GO:0004252]Ycytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965](FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. {ECO:0000269|PubMed:1861871, ECO:0000269|PubMed:2006156}.Q8TDQ7GNPI2#Glucosamine-6-phosphate isomerase 2_carbohydrate metabolic process [GO:0005975]; N-acetylglucosamine metabolic process [GO:0006044]Q9P2Y5UVRAG/UV radiation resistance-associated gene proteinSUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:18843052}. Lysosome {ECO:0000269|PubMed:18843052}. Early endosome {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:18843052}. Endoplasmic reticulum {ECO:0000269|PubMed:24056303}. Midbody {ECO:0000269|PubMed:20643123}. Chromosome, centromere {ECO:0000269|PubMed:22542840}. Note=Colocalizes with RAB9-positive compartments involved in retrograde transport from late endosomes to trans-Golgi network. Colocalization with early endosomes is only partial.]autophagy [GO:0006914]; centrosome organization [GO:0051297]; DNA repair [GO:0006281]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; maintenance of Golgi location [GO:0051684]; positive regulation of autophagy [GO:0010508]; receptor catabolic process [GO:0032801]; regulation of cytokinesis [GO:0032465]; regulation of protein serine/threonine kinase activity [GO:0071900]; regulation of vesicle-mediated transport [GO:0060627]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; SNARE complex assembly [GO:0035493]; viral entry into host cell [GO:0046718]SNARE binding [GO:0000149]%centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; late endosome [GO:0005770]; lysosome [GO:0005764]; midbody [GO:0030496]; phagocytic vesicle [GO:0045335]; protein complex [GO:0043234]UFUNCTION: Versatile protein that is involved in regulation of differenent cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:24056303). During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2 (PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events (PubMed:18552835). Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion (PubMed:24550300). In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly (PubMed:24550300). {ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:24056303, ECO:0000305}.; FUNCTION: Involved in maintaining chromosomal stability. Promotes DNA double-strand break (DSB) repair by association with DNA-dependent protein kinase complex DNA-PK and activating it in non-homologous end joining (NHEJ) (PubMed:22542840). Required for centrosome stability and proper chromosome segregation (PubMed:22542840). {ECO:0000269|PubMed:22542840}.P37837TALDO TransaldolaseLcarbohydrate metabolic process [GO:0005975]; energy reserve metabolic process [GO:0006112]; fructose 6-phosphate metabolic process [GO:0006002]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]; small molecule metabolic process [GO:0044281]; xylulose biosynthetic process [GO:0005999]monosaccharide binding [GO:0048029]; sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity [GO:0004801]eFUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.P41214EIF2D+Eukaryotic translation initiation factor 2D>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20566627}.formation of translation preinitiation complex [GO:0001731]; intracellular protein transport [GO:0006886]; IRES-dependent translational initiation [GO:0002192]; ribosome disassembly [GO:0032790]Sreceptor activity [GO:0004872]; translation initiation factor activity [GO:0003743]$FUNCTION: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. {ECO:0000269|PubMed:20566627, ECO:0000269|PubMed:20713520}.P23588IF4B+Eukaryotic translation initiation factor 4Bcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]Vcytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:00< 16281]FUNCTION: Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.Q86XX4FRAS1"Extracellular matrix protein FRAS1 glycoproteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.cell communication [GO:0007154]; embryonic limb morphogenesis [GO:0030326]; metanephros morphogenesis [GO:0003338]; morphogenesis of an epithelium [GO:0002009]; palate development [GO:0060021]; protein transport [GO:0015031]; skin development [GO:0043588]metal ion binding [GO:0046872]gintegral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; sublamina densa [GO:0061618]P50452SPB8 Serpin B8rcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]Q8N0X7SPG20SpartinjSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19580544}. Note=Transiently associated with endosomes.qabscission [GO:0009838]; adipose tissue development [GO:0060612]; cell division [GO:0051301]; lipid particle organization [GO:0034389]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of collateral sprouting in absence of injury [GO:0048698]; neuromuscular process [GO:0050905]; regulation of mitochondrial membrane potential [GO:0051881]cytoplasm [GO:0005737]; lipid particle [GO:0005811]; midbody [GO:0030496]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]; synapse [GO:0045202]WFUNCTION: May be implicated in endosomal trafficking, or microtubule dynamics, or both.P33176KINHKinesin-1 heavy chainSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Uniformly distributed between soma and neurites in hippocampal neurons. {ECO:0000250}.axon guidance [GO:0007411]; cellular protein metabolic process [GO:0044267]; cytoplasm organization [GO:0007028]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; plus-end-directed vesicle transport along microtubule [GO:0072383]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of potassium ion transport [GO:0043268]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; protein localization [GO:0008104]; regulation of membrane potential [GO:0042391]; stress granule disassembly [GO:0035617]; vesicle transport along microtubule [GO:0047496]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]3ciliary rootlet [GO:0035253]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; vesicle [GO:0031982]tFUNCTION: Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. {ECO:0000250}.Q6VY07PACS1-Phosphofurin acidic cluster sorting protein 1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes in the perinuclear region, probably the TGN. {ECO:0000250}.positive regulation of protein binding [GO:0032092]; protein targeting to Golgi [GO:0000042]; protein targeting to plasma membrane [GO:0072661]; regulation of defense response to virus by virus [GO:0050690]; viral process [GO:0016032] ion channel binding [GO:0044325]dCOPI-coated vesicle [GO:0030137]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Coat protein that is involved in the localization of trans-Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster-containing cytoplasmic domain of these molecules with the adapter-protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits. Involved in HIV-1 nef-mediated removal of MHC-I from the cell surface to the TGN. {ECO:0000269|PubMed:11331585}.Q99759M3K30Mitogen-activated protein kinase kinase kinase 3MAPKKKmactivation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; blood vessel development [GO:0001568]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of p38MAPK cascade [GO:1900745]; protein autophosphorylation [GO:0046777]ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]0cytosol [GO:0005829]; intracellular [GO:0005622] FUNCTION: Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. {ECO:0000269|PubMed:12912994, ECO:0000269|PubMed:14661019, ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:9006902}.Q9NTM9CUTC'Copper homeostasis protein cutC homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16182249}. Nucleus {ECO:0000269|PubMed:16182249}. Note=The overexpressed protein is detected in the cytoplasm, and depending on the cell line, also in the nucleus.copper ion homeostasis [GO:0055070]; copper ion transport [GO:0006825]; ion transmembrane transport [GO:0034220]; protein tetramerization [GO:0051262]; transmembrane transport [GO:0055085]^cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: May play a role in copper homeostasis. Can bind one Cu(1+) per subunit. {ECO:0000269|PubMed:16182249, ECO:0000269|PubMed:19878721}.Q68CZ2TENS3Tensin-3Invadopodia MoleculesoSUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:17643115}.{cell migration [GO:0016477]; lung alveolus development [GO:0048286]; positive regulation of cell proliferation [GO:0008284]3cytoplasm [GO:0005737]; focal adhesion [GO:0005925]OFUNCTION: May play a role in actin remodeling. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Seems to be involved in mammary cell migration. May be involved in cell migration and bone development (By similarity). {ECO:0000250}.Q15365PCBP1Poly(rC)-binding protein 1Common componentSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.dgene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]]FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.Q6XZF7DNMBPDynamin-binding proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Localized to synapses and Golgi stacks. {ECO:0000250}.jintracellular signal transduction [GO:0035556]; regulation of Rho protein signal transduction [GO:0035023];Rho guanyl-nucleotide exchange factor activity [GO:0005089]ecell junction [GO:0030054]; cytoskeleton [GO:0005856]; Golgi stack [GO:0005795]; synapse [GO:0045202]FUNCTION: Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). {ECO:0000250}.< O94979SC31A Protein transport protein Sec31A3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associates with membranes in a GTP-dependent manner. {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER to Golgi vesicle-mediated transport [GO:0006888]; IRE1-mediated unfolded protein response [GO:0036498]; membrane organization [GO:0061024]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; protein transport [GO:0015031]; response to calcium ion [GO:0051592].calcium-dependent protein binding [GO:0048306]COPII vesicle coat [GO:0030127]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle [GO:0030134]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; vesicle coat [GO:0030120]EFUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). {ECO:0000250}.P48637GSHBGlutathione synthetaseaging [GO:0007568]; cellular amino acid metabolic process [GO:0006520]; glutathione biosynthetic process [GO:0006750]; glutathione derivative biosynthetic process [GO:1901687]; nervous system development [GO:0007399]; response to amino acid [GO:0043200]; response to cadmium ion [GO:0046686]; response to nutrient levels [GO:0031667]; response to oxidative stress [GO:0006979]; response to tumor necrosis factor [GO:0034612]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]ATP binding [GO:0005524]; glutathione binding [GO:0043295]; glutathione synthase activity [GO:0004363]; glycine binding [GO:0016594]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]P13639EF2Elongation factor 2SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:24648518}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000269|PubMed:24648518}.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; hematopoietic progenitor cell differentiation [GO:0002244]; peptidyl-diphthamide biosynthetic process from peptidyl-histidine [GO:0017183]; positive regulation of translation [GO:0045727]; post-translational protein modification [GO:0043687]; translation [GO:0006412]; translational elongation [GO:0006414]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; translation elongation factor activity [GO:0003746]aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.Q9HC38GLOD4&Glyoxalase domain-containing protein 4BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:12897971}.Q14181DPOA2DNA polymerase alpha subunit BDNA replicationDNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; protein import into nucleus, translocation [GO:0000060]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]}DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; protein heterodimerization activity [GO:0046982]calpha DNA polymerase:primase complex [GO:0005658]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery. {ECO:0000250}.O75223GGCTGamma-glutamylcyclotransferaseglutathione biosynthetic process [GO:0006750]; glutathione derivative biosynthetic process [GO:1901687]; release of cytochrome c from mitochondria [GO:0001836]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]dgamma-glutamylcyclotransferase activity [GO:0003839]; protein homodimerization activity [GO:0042803]!FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis. {ECO:0000269|PubMed:16765912, ECO:0000269|PubMed:18515354}.P61081UBC12NEDD8-conjugating enzyme Ubc12hcellular protein modification process [GO:0006464]; innate immune response [GO:0045087]; positive regulation of neuron apoptotic process [GO:0043525]; protein neddylation [GO:0045116]; protein ubiquitination [GO:0016567]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; transforming growth factor beta receptor signaling pathway [GO:0007179]ATP binding [GO:0005524]; NEDD8 transferase activity [GO:0019788]; ribosomal S6-glutamic acid ligase activity [GO:0018169]; ubiquitin-protein transferase activity [GO:0004842]FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:15361859}.O14579COPECoatomer subunit epsilonCOPI coating of Golgi vesicle [GO:0048205]; ER to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane organization [GO:0061024]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]lCOPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.Q13442HAP28+28 kDa heat- and acid-stable phosphoproteinAcell proliferation [GO:0008283]; signal transduction [GO:0007< 165]zFUNCTION: Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. {ECO:0000250}.Q9NQR4NIT2Omega-amidase NIT2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17488281}.asparagine metabolic process [GO:0006528]; glutamine metabolic process [GO:0006541]; oxaloacetate metabolic process [GO:0006107]#omega-amidase activity [GO:0050152]ocentrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]FUNCTION: Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. Overexpression decreases the colony-forming capacity of cultured cells by arresting cells in the G2 phase of the cell cycle. {ECO:0000269|PubMed:17488281, ECO:0000269|PubMed:19595734}.Q9Y4X5ARI1!E3 ubiquitin-protein ligase ARIH1WSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278816}. Note=Mainly cytoplasmic.cytokine-mediated signaling pathway [GO:0019221]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]ligase activity [GO:0016874]; ubiquitin-like protein transferase activity [GO:0019787]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]Scytoplasm [GO:0005737]; cytosol [GO:0005829]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. {ECO:0000269|PubMed:14623119, ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:17289916, ECO:0000269|PubMed:21532592}.Q13029PRDM2PR domain zinc finger protein 2K-methyltransferases(27)tSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14633678, ECO:0000269|PubMed:7538672, ECO:0000269|PubMed:9006946}.determination of adult lifespan [GO:0008340]; regulation of transcription, DNA-templated [GO:0006355]; response to estradiol [GO:0032355]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; histone-lysine N-methyltransferase activity [GO:0018024]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]2Golgi apparatus [GO:0005794]; nucleus [GO:0005634]hFUNCTION: S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene. {ECO:0000269|PubMed:14633678}.Q9H009NACA26Nascent polypeptide-associated complex subunit alpha-2ESUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.?myoblast migration [GO:0051451]; protein transport [GO:0015031]/transcription coactivator activity [GO:0003713]FUNCTION: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). {ECO:0000250}.Q96TA1NIBL1Niban-like protein 1ESUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell junction, adherens junction. Note=In exponentially growing cells, exclusively cytoplasmic. Cell membrane localization is observed when cells reach confluency and during telophase. In melanoma cells, targeting to the plasma membrane may be impaired by C-terminal phosphorylation.5negative regulation of apoptotic process [GO:0043066]actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May play a role in apoptosis suppression. May promote melanoma cell invasion in vitro. {ECO:0000269|PubMed:19362540, ECO:0000269|PubMed:21148485}.Q9BW62KATL1.Katanin p60 ATPase-containing subunit A-like 1mSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03024, ECO:0000269|PubMed:22654668}.rcytoplasmic microtubule organization [GO:0031122]; microtubule severing [GO:0051013]; spermatogenesis [GO:0007283]KATP binding [GO:0005524]; microtubule-severing ATPase activity [GO:0008568] FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity). {ECO:0000250}.O94903PROSC9Proline synthase co-transcribed bacterial homolog protein(pyridoxal phosphate binding [GO:0030170]rcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; mitochondrion [GO:0005739]P24666PPAC8Low molecular weight phosphotyrosine protein phosphataseAdherens junction(73)pacid phosphatase activity [GO:0003993]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]lcytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; extracellular exosome [GO:0070062]FUNCTION: Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity.Q15370ELOB/Transcription elongation factor B polypeptide 2cellular response to hypoxia [GO:0071456]; gene expression [GO:0010467]; positive regulation of viral transcription [GO:0050434]; protein complex assembly [GO:0006461]; protein ubiquitination [GO:0016567]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Cul2-RING ubiquitin ligase complex [GO:0031462]; Cul5-RING ubiquitin ligase complex [GO:0031466]; cytosol [GO:0005829]; elongin complex [GO:0070449]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; VCB complex [GO:0030891]FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).; FUNCTION: The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.Q9BYX2TBD2ATBC1 domain family member 2ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20116244}. Cytoplasmic vesicle {ECO:0000269|PubMed:20116244}. Cell junction {ECO:0000269|PubMed:20116244}.3positive regulation of GTPase activity [GO:0043547]Ecadherin binding [GO:0045296]; GTPase activator activity [GO:0005096]ocell junction [GO:0030054]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle [GO:0031410]FUNCTION: Acts as GTPase-activating protein for RAB7A. Signal effector acting as a linker between RAC1 and RAB7A, leading to RAB7A inactivation and subsequent inhibition of cadherin degradation and reduced cell-cell adhesion. {ECO:0000269|PubMed:20116244}.Q8N392RHG18 Rho GTPase-activating protein 18< >SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21865595}.|regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]@FUNCTION: Rho GTPase activating protein that suppresses F-actin polymerization by inhibiting Rho. Rho GTPase activating proteins act by converting Rho-type GTPases to an inactive GDP-bound state (PubMed:21865595). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts downstream of YAP1 and inhibits actin polymerization, which in turn reduces nuclear localization of YAP1 (PubMed:25778702). Regulates cell shape, spreading, and migration (PubMed:21865595). {ECO:0000269|PubMed:21865595, ECO:0000269|PubMed:25778702}.P49815TSC2Tuberinregulator mTorSUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=At steady state found in association with membranes.@cell cycle arrest [GO:0007050]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; glucose import [GO:0046323]; heart development [GO:0007507]; innate immune response [GO:0045087]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin receptor signaling pathway [GO:0008286]; negative regulation of cell proliferation [GO:0008285]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; negative regulation of Wnt signaling pathway [GO:0030178]; neural tube closure [GO:0001843]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-mediated signaling [GO:0048015]; positive chemotaxis [GO:0050918]; positive regulation of GTPase activity [GO:0043547]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein import into nucleus [GO:0006606]; protein kinase B signaling [GO:0043491]; protein localization [GO:0008104]; protein transport into plasma membrane raft [GO:0044861]; regulation of cell cycle [GO:0051726]; regulation of endocytosis [GO:0030100]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of small GTPase mediated signal transduction [GO:0051056]; response to hypoxia [GO:0001666]; transcription initiation from RNA polymerase II promoter [GO:0006367]; vesicle-mediated transport [GO:0016192]; viral process [GO:0016032]GTPase activator activity [GO:0005096]; phosphatase binding [GO:0019902]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; TSC1-TSC2 complex [GO:0033596]5FUNCTION: In complex with TSC1, this tumor suppressor inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. May also play a role in microtubule-mediated protein transport. Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:16707451}.Q00796DHSOSorbitol dehydrogenaseSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q64442}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64442}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q64442}. Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. {ECO:0000250|UniProtKB:Q64442}.Pcarbohydrate metabolic process [GO:0005975]; fructose biosynthetic process [GO:0046370]; fructose metabolic process [GO:0006000]; glucose metabolic process [GO:0006006]; L-xylitol catabolic process [GO:0051160]; L-xylitol metabolic process [GO:0051164]; response to cadmium ion [GO:0046686]; response to copper ion [GO:0046688]; response to drug [GO:0042493]; response to hormone [GO:0009725]; response to nutrient levels [GO:0031667]; response to osmotic stress [GO:0006970]; small molecule metabolic process [GO:0044281]; sorbitol catabolic process [GO:0006062]; sperm motility [GO:0030317]carbohydrate binding [GO:0030246]; L-iditol 2-dehydrogenase activity [GO:0003939]; NAD binding [GO:0051287]; zinc ion binding [GO:0008270]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; motile cilium [GO:0031514]FUNCTION: Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm. {ECO:0000250|UniProtKB:Q64442}.Q96K76UBP47(Ubiquitin carboxyl-terminal hydrolase 47>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21362556}.*base-excision repair [GO:0006284]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to UV [GO:0034644]; monoubiquitinated protein deubiquitination [GO:0035520]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cell growth [GO:0030307]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of proteasomal protein catabolic process [GO:0061136]; response to drug [GO:0042493]cysteine-type endopeptidase activity [GO:0004197]; ubiquitin-specific protease activity [GO:0004843]; WD40-repeat domain binding [GO:0071987]Wcytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005]}FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulates CDC25A expression at a transcriptional level. {ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:21362556}.P55039DRG2/Developmentally-regulated GTP-binding protein 2 signal transduction [GO:0007165]Icytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrion [GO:0005739]KFUNCTION: May play a role in cell proliferation, differentiation and death.P273481433T14-3-3 protein theta^SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally transported to the nerve terminals.`apoptotic process [GO:0006915]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway [GO:0097193]; membrane organization [GO:0061024]; negative regulation of ion transmembrane transport [GO:0034766]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; small GTPase mediated signal transduction [GO:0007264]; substantia nigra development [GO:0021762]; transcription initiation from RNA polymerase II promoter [GO:0006367]'protein N-terminus binding [GO:0047485]cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:00< 16020]; protein complex [GO:0043234]FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}.Q6NW29RWDD4RWD domain-containing protein 4Q9HB71CYBPCalcyclin-binding proteinDSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12895292}. Cytoplasm {ECO:0000269|PubMed:12895292}. Note=Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated.aging [GO:0007568]; cardiac muscle cell differentiation [GO:0055007]; cellular response to calcium ion [GO:0071277]; negative regulation of cell death [GO:0060548]; positive regulation of DNA replication [GO:0045740]; response to growth hormone [GO:0060416].protein homodimerization activity [GO:0042803]beta-catenin destruction complex [GO:0030877]; cell body [GO:0044297]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; neuron projection [GO:0043005]; nuclear envelope lumen [GO:0005641]; nucleoplasm [GO:0005654]%FUNCTION: May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1). {ECO:0000269|PubMed:16085652}.P04406G3P(Glyceraldehyde-3-phosphate dehydrogenaseSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions. {ECO:0000250}.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; cellular response to interferon-gamma [GO:0071346]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of translation [GO:0017148]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; protein stabilization [GO:0050821]; small molecule metabolic process [GO:0044281] glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; GAIT complex [GO:0097452]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:0030529]; vesicle [GO:0031982]IFUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000250, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:3170585}.P17174AATC'Aspartate aminotransferase, cytoplasmic=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1974457}.2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; carbohydrate metabolic process [GO:0005975]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to insulin stimulus [GO:0032869]; fatty acid homeostasis [GO:0055089]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; glutamate catabolic process to aspartate [GO:0019550]; glutamate metabolic process [GO:0006536]; glycerol biosynthetic process [GO:0006114]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; oxaloacetate metabolic process [GO:0006107]; polyamine metabolic process [GO:0006595]; response to glucocorticoid [GO:0051384]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]Rcarboxylic acid binding [GO:0031406]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine:2-oxoglutarate aminotransferase activity [GO:0047801]; L-phenylalanine:2-oxoglutarate aminotransferase activity [GO:0080130]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170]axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; nucleus [GO:0005634]FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. {ECO:0000269|PubMed:16039064}.Q99471PFD5Prefoldin subunit 5SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Nucleus.zde novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of transcription, DNA-templated [GO:0045892]; protein folding [GO:0006457]; regulation of transcription, DNA-templated [GO:0006355]; retina development in camera-type eye [GO:0060041]/transcription corepressor activity [GO:0003714]Lcytoplasm [GO:0005737]; nucleus [GO:0005634]; prefoldin complex [GO:0016272];FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC. {ECO:0000269|PubMed:9630229}.P12081SYHC#Histidine--tRNA ligase, cytoplasmicgene expression [GO:0010467]; histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial tran< slation [GO:0032543]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]EATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]Q9BZL1UBL5Ubiquitin-like protein 5>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11161819}.cellular protein modification process [GO:0006464]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of protein targeting to mitochondrion [GO:1903955]protein tag [GO:0031386]Q8WVJ2NUDC2 NudC domain-containing protein 2dSUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20133715}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20133715}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20133715}. Note=Associates with centrosomes in interphase and to spindle poles and kinetochores during mitosis.condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; spindle pole [GO:0000922]wFUNCTION: May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000269|PubMed:20133715}.O15357SHIP28Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, lamellipodium. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.actin filament organization [GO:0007015]; cell adhesion [GO:0007155]; endochondral ossification [GO:0001958]; endocytosis [GO:0006897]; glucose metabolic process [GO:0006006]; immune system process [GO:0002376]; inositol phosphate metabolic process [GO:0043647]; negative regulation of cell proliferation [GO:0008285]; negative regulation of gene expression [GO:0010629]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; post-embryonic development [GO:0009791]; response to insulin [GO:0032868]; ruffle assembly [GO:0097178]; small molecule metabolic process [GO:0044281]@hydrolase activity [GO:0016787]; SH2 domain binding [GO:0042169]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]b FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification. {ECO:0000269|PubMed:11349134, ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12235291, ECO:0000269|PubMed:12676785, ECO:0000269|PubMed:12690104, ECO:0000269|PubMed:15668240, ECO:0000269|PubMed:17135240, ECO:0000269|PubMed:21624956, ECO:0000269|PubMed:23273569, ECO:0000269|PubMed:9660833}.Q15185TEBPProstaglandin E synthase 3arachidonic acid metabolic process [GO:0019369]; cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0070389]; cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of cellular response to heat [GO:1900034]; RNA-dependent DNA replication [GO:0006278]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; telomere maintenance [GO:0000723]wprostaglandin-E synthase activity [GO:0050220]; telomerase activity [GO:0003720]; unfolded protein binding [GO:0051082]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448). {ECO:0000269|PubMed:10922363, ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:12077419, ECO:0000269|PubMed:24711448}.Q07960RHG01Rho GTPase-activating protein 1 AngiogenesisRhoGAPpositive regulation of GTPase activity [GO:0043547]; positive regulation of signal transduction [GO:0009967]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]MGTPase activator activity [GO:0005096]; SH3/SH2 adaptor activity [GO:0005070]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.Q6IBS0TWF2 Twinfilin-2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10406962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10406962}. Cell projection, stereocilium {ECO:0000250}. Note=Perinuclear a< nd G-actin-rich cortical actin structure sublocalization.Rbarbed-end actin filament capping [GO:0051016]; cell projection organization [GO:0030030]; cellular response to growth factor stimulus [GO:0071363]; cellular response to retinoic acid [GO:0071300]; negative regulation of actin filament polymerization [GO:0030837]; positive regulation of axon extension [GO:0045773]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of neuron projection development [GO:0010976]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of microvillus length [GO:0032532]; sequestering of actin monomers [GO:0042989]actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; poly(A) RNA binding [GO:0044822]; protein kinase C binding [GO:0005080]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; myofibril [GO:0030016]; perinuclear region of cytoplasm [GO:0048471]; stereocilium [GO:0032420]FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia (By similarity). {ECO:0000250}.Q9HA65TBC17TBC1 domain family member 17WSUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24752605}.lautophagy [GO:0006914]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]Rautophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]'FUNCTION: Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known. {ECO:0000269|PubMed:22854040, ECO:0000269|PubMed:24752605}.P53621COPACoatomer subunit alphaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.; SUBCELLULAR LOCATION: Xenin: Secreted {ECO:0000250}.COPI coating of Golgi vesicle [GO:0048205]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; pancreatic juice secretion [GO:0030157]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]COPI vesicle coat [GO:0030126]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.Q13596SNX1Sorting nexin-1SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:18088323}; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium {ECO:0000269|PubMed:20604901}. Note=Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:15498486). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles (PubMed:18088323). Colocalizes with DNAJC13 and Shiginella dysenteria toxin stxB on early endosomes (PubMed:19874558). Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}.Eearly endosome to Golgi transport [GO:0034498]; intracellular protein transport [GO:0006886]; lamellipodium morphogenesis [GO:0072673]; positive regulation of protein catabolic process [GO:0045732]; receptor internalization [GO:0031623]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle organization [GO:0016050]epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802]; insulin receptor binding [GO:0005158]; leptin receptor binding [GO:1990460]; phosphatidylinositol binding [GO:0035091]; transferrin receptor binding [GO:1990459]|cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane [GO:0016020]; protein complex [GO:0043234]; retromer complex [GO:0030904]FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:12198132). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:19816406, PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1) and Shiginella dysenteria toxin stxB. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi (PubMed:12198132, PubMed:15498486, PubMed:17550970, PubMed:17101778, PubMed:18088323, PubMed:21040701). Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R (PubMed:16407403, PubMed:20070609). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901). Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (PubMed:2315< 2498). {ECO:0000269|PubMed:12198132, ECO:0000269|PubMed:15498486, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:17101778, ECO:0000269|PubMed:17550970, ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:19816406, ECO:0000269|PubMed:20070609, ECO:0000269|PubMed:20604901, ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:23085988, ECO:0000269|PubMed:23152498, ECO:0000303|PubMed:15498486}.P09417DHPRDihydropteridine reductasecellular amino acid metabolic process [GO:0006520]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to drug [GO:0035690]; dihydrobiopterin metabolic process [GO:0051066]; liver development [GO:0001889]; L-phenylalanine catabolic process [GO:0006559]; response to aluminum ion [GO:0010044]; response to glucagon [GO:0033762]; response to lead ion [GO:0010288]; small molecule metabolic process [GO:0044281]; tetrahydrobiopterin biosynthetic process [GO:0006729]6,7-dihydropteridine reductase activity [GO:0004155]; electron carrier activity [GO:0009055]; NADH binding [GO:0070404]; NADPH binding [GO:0070402]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.P42574CASP3 Caspase-3 activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; B cell homeostasis [GO:0001782]; cell fate commitment [GO:0045165]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to organic cyclic compound [GO:0071407]; erythrocyte differentiation [GO:0030218]; execution phase of apoptosis [GO:0097194]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; glial cell apoptotic process [GO:0034349]; heart development [GO:0007507]; hippocampus development [GO:0021766]; hippo signaling [GO:0035329]; intrinsic apoptotic signaling pathway [GO:0097193]; keratinocyte differentiation [GO:0030216]; learning or memory [GO:0007611]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of apoptotic process [GO:0043066]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; neuron differentiation [GO:0030182]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet formation [GO:0030220]; positive regulation of neuron apoptotic process [GO:0043525]; programmed cell death [GO:0012501]; proteolysis [GO:0006508]; regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043281]; response to amino acid [GO:0043200]; response to antibiotic [GO:0046677]; response to cobalt ion [GO:0032025]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; response to nicotine [GO:0035094]; response to tumor necrosis factor [GO:0034612]; response to UV [GO:0009411]; response to X-ray [GO:0010165]; sensory perception of sound [GO:0007605]; T cell homeostasis [GO:0043029]; wound healing [GO:0042060]aspartic-type endopeptidase activity [GO:0004190]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; peptidase activity [GO:0008233]; phospholipase A2 activator activity [GO:0016005]cytoplasm [GO:0005737]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; membrane raft [GO:0045121]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]NFUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. {ECO:0000269|PubMed:21357690, ECO:0000269|PubMed:7596430}.Q15126PMVKPhosphomevalonate kinase Isoprenoid biosynthesis?SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10191291}.cholesterol biosynthetic process [GO:0006695]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; response to cholesterol [GO:0070723]; small molecule metabolic process [GO:0044281]; sterol biosynthetic process [GO:0016126]HATP binding [GO:0005524]; phosphomevalonate kinase activity [GO:0004631]hcytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; peroxisome [GO:0005777]Q9Y3F4STRAP3Serine-threonine kinase receptor-associated proteinvSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized predominantly in the cytoplasm but also found in the nucleus.~maintenance of gastrointestinal epithelium [GO:0030277]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of pathway-restricted SMAD protein phosphorylation [GO:0060394]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; spliceosomal snRNP assembly [GO:0000387]; transforming growth factor beta receptor signaling pathway [GO:0007179]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]{FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein. {ECO:0000269|PubMed:16251192, ECO:0000269|PubMed:18984161}.P40763STAT32Signal transducer and activator of transcription 38Signaling pathways regulating pluripotency of stem cells_SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory facto< r (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1.acute-phase response [GO:0006953]; aging [GO:0007568]; astrocyte differentiation [GO:0048708]; cell proliferation [GO:0008283]; cellular response to hormone stimulus [GO:0032870]; cytokine-mediated signaling pathway [GO:0019221]; eating behavior [GO:0042755]; eye photoreceptor cell differentiation [GO:0001754]; glucose homeostasis [GO:0042593]; growth hormone receptor signaling pathway [GO:0060396]; interleukin-6-mediated signaling pathway [GO:0070102]; intracellular receptor signaling pathway [GO:0030522]; JAK-STAT cascade [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; movement of cell or subcellular component [GO:0006928]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of glycolytic process [GO:0045820]; negative regulation of hydrogen peroxide biosynthetic process [GO:0010730]; negative regulation of neuron death [GO:1901215]; negative regulation of neuron migration [GO:2001223]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nervous system development [GO:0007399]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphorylation [GO:0016310]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of growth factor dependent skeletal muscle satellite cell proliferation [GO:1902728]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein import into nucleus [GO:0006606]; radial glial cell differentiation [GO:0060019]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of multicellular organism growth [GO:0040014]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; sexual reproduction [GO:0019953]; signal transduction [GO:0007165]; somatic stem cell maintenance [GO:0035019]; temperature homeostasis [GO:0001659]; viral process [GO:0016032]DNA binding [GO:0003677]; ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0004879]; protein dimerization activity [GO:0046983]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II repressing transcription factor binding [GO:0001103]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RNA polymerase II transcription factor complex [GO:0090575]yFUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (By similarity). {ECO:0000250}.Q9UBQ0VPS29.Vacuolar protein sorting-associated protein 29SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane {ECO:0000250|UniProtKB:Q9QZ88}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QZ88}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}.intracellular protein transport [GO:0006886]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde transport, endosome to plasma membrane [GO:1990126]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; retromer complex [GO:0030904];FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (Probable). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27 (PubMed:24856514). {ECO:0000250|UniProtKB:Q9QZ88, ECO:0000269|PubMed:16737443, ECO:0000269|PubMed:24856514, ECO:0000303|PubMed:15247922, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491}.Q147X3NAA30N-alpha-acetyltransferase 30>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19398576}.7N-terminal peptidyl-methionine acetylation [GO:0017196]7peptide alpha-N-acetyltransferase activity [GO:0004596]1cytoplasm [GO:0005737]; NatC complex [GO:0031417]NFUNCTION: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate. {ECO:0000269|PubMed:19398576}.O95989NUDT32Diphosphoinositol polyphosphate phosphohydrolase 1cell-cell signaling [GO:0007267]; diadenosine polyphosphate catabolic process [GO:0015961]; diphosphoinositol polyphosphate catabolic process [GO:0071544]; inositol phosphate metabolic process [GO:0043647]; small molecule metabolic process [GO:0044281]diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity [GO:0052846]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052847]; inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity [GO:0052843]; inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052848]; inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity [GO:0052844]; inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity [GO:0052845]; inositol diphosphate tetrakisphosphate diphosphatase activity [GO:0052840]; magnesium ion binding [GO:0000287]lFUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bis< diphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. InsP6 (inositol hexakisphophate) is not a substrate. Acts as a negative regulator of the ERK1/2 pathway. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. {ECO:0000269|PubMed:9822604}.P62993GRB2&Growth factor receptor-bound protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}. Cytoplasm {ECO:0000269|PubMed:21179510}. Endosome {ECO:0000269|PubMed:21179510}. Golgi apparatus {ECO:0000250}.aging [GO:0007568]; anatomical structure formation involved in morphogenesis [GO:0048646]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; branching involved in labyrinthine layer morphogenesis [GO:0060670]; cell-cell signaling [GO:0007267]; cellular response to ionizing radiation [GO:0071479]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; leukocyte migration [GO:0050900]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet activation [GO:0030168]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of signal transduction [GO:0009967]; protein heterooligomerization [GO:0051291]; Ras protein signal transduction [GO:0007265]; receptor internalization [GO:0031623]; regulation of MAPK cascade [GO:0043408]; signal transduction in response to DNA damage [GO:0042770]; small GTPase mediated signal transduction [GO:0007264]; T cell costimulation [GO:0031295]; viral process [GO:0016032]tephrin receptor binding [GO:0046875]; epidermal growth factor receptor binding [GO:0005154]; identical protein binding [GO:0042802]; insulin receptor substrate binding [GO:0043560]; neurotrophin TRKA receptor binding [GO:0005168]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; SH3/SH2 adaptor activity [GO:0005070]; SH3 domain binding [GO:0017124]jcell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Grb2-EGFR complex [GO:0070436]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506]FUNCTION: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.; FUNCTION: Isoform 2 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced transactivation of a RAS-responsive element. Isoform 2 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death.Q9Y570PPME1$Protein phosphatase methylesterase 1negative regulation of catalytic activity [GO:0043086]; protein demethylation [GO:0006482]; regulation of protein phosphatase type 2A activity [GO:0034047]protein C-terminal methylesterase activity [GO:0051722]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase binding [GO:0019903]; protein phosphatase inhibitor activity [GO:0004864]; protein phosphatase type 2A regulator activity [GO:0008601]FUNCTION: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme. {ECO:0000269|PubMed:10318862}.Q6PD74AAGAB,Alpha- and gamma-adaptin-binding protein p34dSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23000146, ECO:0000269|PubMed:23064416}.xFUNCTION: May be involved in endocytic recycling of growth factor receptors such as EGFR. {ECO:0000269|PubMed:23064416}.P319461433B14-3-3 protein beta/alphaFactivation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; cytoplasmic sequestering of protein [GO:0051220]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; hippo signaling [GO:0035329]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway [GO:0097193]; MAPK cascade [GO:0000165]; membrane organization [GO:0061024]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of transcription, DNA-templated [GO:0045892]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of catalytic activity [GO:0043085]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; protein heterooligomerization [GO:0051291]; protein targeting [GO:0006605]; Ras protein signal transduction [GO:0007265]; small GTPase mediated signal transduction [GO:0007264]; transcription initiation from RNA polymerase II promoter [GO:0006367]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; phosphoprotein binding [GO:0051219]; phosphoserine binding [GO:0050815]; protein domain specific binding [GO:0019904]; transcription corepressor activity [GO:0003714]<cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; transcriptional repressor complex [GO:0017053]iFUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491}.P53041PPP5&Serine/threonine-protein phosphatase 5 phosphataserSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane. Note=Predominantly nuclear. But also present in the cytoplasm.cellular response to cadmium ion [GO:0071276]; cellular response to hydrogen peroxide [GO:0070301]; DNA repair [GO:0006281]; histone dephosphorylation [GO:0016576]; mitotic nuclear division [GO:0007067]; negative regulation of neuron death [GO:1901215]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of glucocorticoid receptor signaling pathway [GO:2000324]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein dephosphorylation [GO:0006470]; protein heterooligomerization [GO:0051291]; response to lead ion [GO:0010288]; response to morphine [GO:0043278]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]identical protein binding [GO:0042802]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine phosphatase activity [GO:0004722]; RNA binding [GO:0003723]; signal transducer activity [GO:0004871]cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO< :0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; proximal dendrite [GO:1990635]6FUNCTION: Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2. {ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:9000529}.Q5JSH3WDR44WD repeat-containing protein 44SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia. {ECO:0000250}.cytosol [GO:0005829]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]mFUNCTION: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). {ECO:0000250}.Q06190P2R3ALSerine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha?eye photoreceptor cell differentiation [GO:0001754]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein catabolic process [GO:0045732]; protein dephosphorylation [GO:0006470]; regulation of cell motility involved in somitogenic axis elongation [GO:0090249]; regulation of protein phosphatase type 2A activity [GO:0034047]; somatic muscle development [GO:0007525]; somite development [GO:0061053]; Wnt signaling pathway involved in somitogenesis [GO:0090244]]calcium ion binding [GO:0005509]; protein phosphatase type 2A regulator activity [GO:0008601]0protein phosphatase type 2A complex [GO:0000159]FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.Q9Y2Z0SUGT1'Suppressor of G2 allele of SKP1 homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21864708}. Nucleus {ECO:0000269|PubMed:21864708}. Note=Translocates to the nucleus upon heat shock, requiring S100A6.$innate immune response [GO:0045087]; mitotic nuclear division [GO:0007067]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; positive regulation by host of symbiont catalytic activity [GO:0043947]; regulation of protein stability [GO:0031647]cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]fFUNCTION: May play a role in ubiquitination and subsequent proteasomal degradation of target proteins.P31751AKT2(RAC-beta serine/threonine-protein kinaseSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Note=Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3.activation of GTPase activity [GO:0090630]; carbohydrate transport [GO:0008643]; cellular protein modification process [GO:0006464]; cellular response to insulin stimulus [GO:0032869]; cellular response to organic cyclic compound [GO:0071407]; fat cell differentiation [GO:0045444]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; insulin receptor signaling pathway [GO:0008286]; intracellular protein transmembrane transport [GO:0065002]; mammary gland epithelial cell differentiation [GO:0060644]; membrane organization [GO:0061024]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of plasma membrane long-chain fatty acid transport [GO:0010748]; negative regulation of RNA splicing [GO:0033119]; peripheral nervous system myelin maintenance [GO:0032287]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147]; positive regulation of fatty acid beta-oxidation [GO:0032000]; positive regulation of glucose import [GO:0046326]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of signal transduction [GO:0009967]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of vesicle fusion [GO:0031340]; protein kinase B signaling [GO:0043491]; protein localization to plasma membrane [GO:0072659]; regulation of cell cycle arrest [GO:0071156]; regulation of cell migration [GO:0030334]; regulation of translation [GO:0006417]; response to muscle activity [GO:0014850]; response to nutrient levels [GO:0031667]; response to osmotic stress [GO:0006970]; signal transduction [GO:0007165]mATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]cell cortex [GO:0005938]; cytosol [GO:0005829]; insulin-responsive compartment [GO:0032593]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for in< sulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; FUNCTION: One of the few specific substrates of AKT2 identified recently is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.O43237DC1L2/Cytoplasmic dynein 1 light intermediate chain 2antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; centrosome localization [GO:0051642]; microtubule-based movement [GO:0007018]; microtubule cytoskeleton organization [GO:0000226]; transport [GO:0006810]AATP binding [GO:0005524]; microtubule motor activity [GO:0003777]centrosome [GO:0005813]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.P63241IF5A1-Eukaryotic translation initiation factor 5A-1vSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex. Note=Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions.apoptotic process [GO:0006915]; cellular protein metabolic process [GO:0044267]; mRNA export from nucleus [GO:0006406]; nucleocytoplasmic transport [GO:0006913]; peptidyl-lysine modification to peptidyl-hypusine [GO:0008612]; positive regulation of cell proliferation [GO:0008284]; positive regulation of translational elongation [GO:0045901]; positive regulation of translational termination [GO:0045905]; post-translational protein modification [GO:0043687]; protein export from nucleus [GO:0006611]; translational frameshifting [GO:0006452]poly(A) RNA binding [GO:0044822]; protein N-terminus binding [GO:0047485]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746]; U6 snRNA binding [GO:0017070]annulate lamellae [GO:0005642]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear pore [GO:0005643]; nucleus [GO:0005634]FUNCTION: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. {ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064, ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:17360499}.Q15750TAB18TGF-beta-activated kinase 1 and MAP3K7-binding protein 1activation of MAPK activity [GO:0000187]; activation of MAPKKK activity [GO:0000185]; Fc-epsilon receptor signaling pathway [GO:0038095]; heart morphogenesis [GO:0003007]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; innate immune response [GO:0045087]; in utero embryonic development [GO:0001701]; JNK cascade [GO:0007254]; lung development [GO:0030324]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein dephosphorylation [GO:0006470]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]< ; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]enzyme activator activity [GO:0008047]; kinase activator activity [GO:0019209]; protein serine/threonine phosphatase activity [GO:0004722]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]FUNCTION: May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis.Q96AA8JKIP22Janus kinase and microtubule-interacting protein 2DSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17572408}.Golgi apparatus [GO:0005794]O43432IF4G32Eukaryotic translation initiation factor 4 gamma 3cytokine-mediated signaling pathway [GO:0019221]; regulation of translational initiation [GO:0006446]; viral process [GO:0016032]poly(A) RNA binding [GO:0044822]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743] FUNCTION: Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1. {ECO:0000269|PubMed:9418880}.P41227NAA10N-alpha-acetyltransferase 10SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=According to PubMed:12464182 it is cytoplasmic. According to PubMed:15496142, it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes.DNA packaging [GO:0006323]; internal protein amino acid acetylation [GO:0006475]; N-terminal peptidyl-glutamic acid acetylation [GO:0018002]; N-terminal peptidyl-serine acetylation [GO:0017198]; N-terminal protein amino acid acetylation [GO:0006474]N-acetyltransferase activity [GO:0008080]; peptide-glutamate-N-acetyltransferase activity [GO:1990190]; peptide-serine-N-acetyltransferase activity [GO:1990189]cytoplasm [GO:0005737]; cytosolic ribosome [GO:0022626]; intracellular [GO:0005622]; membrane [GO:0016020]; NatA complex [GO:0031415]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development. {ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:15496142, ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20145209}.O43776SYNC$Asparagine--tRNA ligase, cytoplasmicasparaginyl-tRNA aminoacylation [GO:0006421]; gene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]iasparagine-tRNA ligase activity [GO:0004816]; ATP binding [GO:0005524]; nucleic acid binding [GO:0003676]lcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]Q16626MEA1Male-enhanced antigen 1dcell differentiation [GO:0030154]; male gonad development [GO:0008584]; spermatogenesis [GO:0007283]RFUNCTION: May play an important role in spermatogenesis and/or testis development.Q9NR46SHLB2 Endophilin-B2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11161816}.O94804STK10"Serine/threonine-protein kinase 10}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19255442}; Peripheral membrane protein {ECO:0000269|PubMed:19255442}.activation of protein kinase activity [GO:0032147]; cell cycle [GO:0007049]; lymphocyte aggregation [GO:0071593]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of lymphocyte migration [GO:2000401]; regulation of mitotic cell cycle [GO:0007346]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; polo kinase kinase activity [GO:0042801]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]Xcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:11903060, ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:19255442}.O14986PI51B5Phosphatidylinositol 4-phosphate 5-kinase type-1 betagSUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Note=Associated with membranes. {ECO:0000250}.phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281][1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]bcytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; uropod [GO:0001931]FFUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion (By similarity). {ECO:0000250}.Q8WUM4PDC6I+Programmed cell death 6-interacting proteinGSUBCELLULAR LOCATION: Cytoplasm, cytosol. Melanosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Colocalized with CEP55 in the midbody during cytokinesis. Colocalized with CEP55 at centrosomes of non-dividing cells.Iapoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell separation after cytokinesis [GO:0000920]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of extracellular exosome assembly [GO:1903551]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]calcium-dependent protein binding [GO:0048306]; proteinase activated receptor binding [GO:0031871]; protein homodimerization activity [GO:0042803][cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; melanosome [GO:0042470]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; myelin sheath [GO:0043209]FUNCTION: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appear< s to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation. {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17428861, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.P63098CANB1Calcineurin subunit B type 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}. Cell membrane, sarcolemma. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocytes hypertrophy. {ECO:0000250}.wapoptotic process [GO:0006915]; calcineurin-NFAT signaling cascade [GO:0033173]; dephosphorylation [GO:0016311]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; positive regulation of NFAT protein import into nucleus [GO:0051533]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; programmed cell death [GO:0012501]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]calcium-dependent protein serine/threonine phosphatase activity [GO:0004723]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; protein domain specific binding [GO:0019904]icalcineurin complex [GO:0005955]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; sarcolemma [GO:0042383]FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.Q13409DC1I2)Cytoplasmic dynein 1 intermediate chain 25antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; transport [GO:0006810]; viral process [GO:0016032]'microtubule motor activity [GO:0003777]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; microtubule [GO:0005874]; vesicle [GO:0031982]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.Q3KQU3MA7D1 MAP7 domain-containing protein 1USUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15561729}.2microtubule cytoskeleton organization [GO:0000226]Scytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; spindle [GO:0005819]P16591FERTyrosine-protein kinase FerSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Note=Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts.actin cytoskeleton reorganization [GO:0031532]; cell adhesion [GO:0007155]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cellular response to insulin stimulus [GO:0032869]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to reactive oxygen species [GO:0034614]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; diapedesis [GO:0050904]; extracellular matrix-cell signaling [GO:0035426]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; insulin receptor signaling pathway via phosphatidylinositol 3-kinase [GO:0038028]; interleukin-6-mediated signaling pathway [GO:0070102]; intracellular signal transduction [GO:0035556]; Kit signaling pathway [GO:0038109]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; negative regulation of mast cell activation involved in immune response [GO:0033007]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of epidermal growth factor receptor signaling pathway [GO:0042058]; regulation of fibroblast migration [GO:0010762]; regulation of lamellipodium assembly [GO:0010591]; regulation of mast cell degranulation [GO:0043304]; regulation of protein phosphorylation [GO:0001932]; response to lipopolysaccharide [GO:0032496]; response to platelet-derived growth factor [GO:0036119]; substrate adhesion-dependent cell spreading [GO:0034446]; tyrosine phosphorylation of Stat3 protein [GO:0042503]ATP binding [GO:0005524]; epidermal growth factor receptor binding [GO:0005154]; lipid binding [GO:0008289]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]cell cortex [GO:0005938]; cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]*FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus. {ECO:0000269|PubMed:12972546, ECO:0000269|PubMed:14517306, ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:19738202, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21518868, ECO:0000269|PubMed:22223638, ECO:0000269|PubMed:7623846, ECO:0000269|PubMed:9722593}.Q9UL15BAG5*BAG family molecular chaperone regulator 5cellular response to heat [GO:0034605]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO< :0032435]; negative regulation of protein refolding [GO:0061084]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; neuron death [GO:0070997]; protein folding [GO:0006457]; regulation of cellular response to heat [GO:1900034]; regulation of inclusion body assembly [GO:0090083]; regulation of ubiquitin-protein transferase activity [GO:0051438]rchaperone binding [GO:0051087]; protein kinase binding [GO:0019901]; ubiquitin protein ligase binding [GO:0031625]cytosol [GO:0005829]; inclusion body [GO:0016234]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. {ECO:0000250, ECO:0000269|PubMed:20223214}.Q9H492MLP3A4Microtubule-associated proteins 1A/1B light chain 3ASUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:23459205}. Note=LC3-II binds to the autophagic membranes.autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; membrane fusion [GO:0061025]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]rmicrotubule binding [GO:0008017]; phosphatidylethanolamine binding [GO:0008429]; phospholipid binding [GO:0005543]'autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; late endosome [GO:0005770]; microtubule [GO:0005874]; organelle membrane [GO:0031090]; pre-autophagosomal structure [GO:0000407]!FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:20713600}.Q9Y316MEMO1 Protein MEMO14regulation of microtubule-based process [GO:0032886]FUNCTION: May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration. {ECO:0000269|PubMed:15156151, ECO:0000269|PubMed:20937854}.Q92696PGTA/Geranylgeranyl transferase type-2 subunit alphaFUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. {ECO:0000269|PubMed:7991565}.Q6ZS30NBEL1Neurobeachin-like protein 1 endosomal transport [GO:0016197]jendomembrane system [GO:0012505]; extrinsic component of membrane [GO:0019898]; intracellular [GO:0005622]Q9BQE3TBA1CTubulin alpha-1C chain,de novo' posttranslational protein folding [GO:0051084]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based process [GO:0007017]; protein folding [GO:0006457]; protein polymerization [GO:0051258]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]jcytoplasmic microtubule [GO:0005881]; microtubule [GO:0005874]; nucleus [GO:0005634]; vesicle [GO:0031982]P22061PIMT7Protein-L-isoaspartate(D-aspartate) O-methyltransferase=protein methylation [GO:0006479]; protein repair [GO:0030091]Nprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity [GO:0004719]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein. {ECO:0000250|UniProtKB:P23506}.Q9NVG8TBC13TBC1 domain family member 13KFUNCTION: May act as a GTPase-activating protein for Rab family protein(s).Q9Y608LRRF24Leucine-rich repeat flightless-interacting protein 2"Wnt signaling pathway [GO:0016055]LRR domain binding [GO:0030275][FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269|PubMed:15677333, ECO:0000269|PubMed:19265123}.Q9BSD7NTPCR(Cancer-related nucleoside-triphosphataseATP binding [GO:0005524]; nucleoside-triphosphatase activity [GO:0017111]; nucleotide phosphatase activity, acting on free nucleotides [GO:0098519]; poly(A) RNA binding [GO:0044822]9extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency. {ECO:0000269|PubMed:17291528}.Q92616GCN1LTranslational activator GCN1@regulation of translation [GO:0006417]; translation [GO:0006412]Wpoly(A) RNA binding [GO:0044822]; translation factor activity, RNA binding [GO:0008135]Dcytoplasm [GO:0005737]; membrane [GO:0016020]; ribosome [GO:0005840]FUNCTION: Acts as a translation activator that mediates translational control and perform an EF3-related function on the ribosome by regulating GCN2 protein kinase (EIF2AK1-4) activity. {ECO:0000250}.Q9P0P0RN181"E3 ubiquitin-protein ligase RNF181'protein autoubiquitination [GO:0051865]pligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269|PubMed:18331836}.Q712K3UB2R2"Ubiquitin-conjugating enzyme E2 R2proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein monoubiquitination [GO:0006513]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin. {ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:20061386}.P46109CRKLCrk-like proteinactivation of MAPKK activity [GO:0000186]; anterior/posterior pattern specification [GO:0009952]; blood vessel development [GO:0001568]; heart development [GO:0007507]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ morphogenesis [GO:0009887]; parathyroid gland development [GO:0060017]; positive regulation of cell proliferation [GO:0008284]; Ras protein signal transduction [GO:0007265]; thymus development [GO:0048538]ppoly(A) RNA binding [GO:0044822]; SH3/SH2 adaptor activity [GO:0005070]; signal transducer activity [GO:0004871]Ocytosol [GO:0005829]; endoso< me [GO:0005768]; extracellular exosome [GO:0070062]@FUNCTION: May mediate the transduction of intracellular signals.Q8IVM0CCD50(Coiled-coil domain-containing protein 50|SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with microtubules of the cytoskeleton and mitotic apparatus. {ECO:0000250}.DFUNCTION: Involved in EGFR signaling. {ECO:0000269|PubMed:15314609}.O76003GLRX3Glutaredoxin-3OSUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:10636891}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Under the plasma membrane. After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area. In the Z line, found associated with CSRP3 (By similarity). {ECO:0000250}.cell redox homeostasis [GO:0045454]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; regulation of the force of heart contraction [GO:0002026]electron carrier activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein disulfide oxidoreductase activity [GO:0015035]~cell cortex [GO:0005938]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; Z disc [GO:0030018]FUNCTION: Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Crucial regulator of cellular iron homeostasis and hemoglobin maturation. May play a role in regulating the function of the thioredoxin system. Does not posses any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. {ECO:0000250, ECO:0000269|PubMed:23615448}.P02787TRFESerotransferrinactin filament organization [GO:0007015]; activation of JUN kinase activity [GO:0007257]; blood coagulation [GO:0007596]; cellular iron ion homeostasis [GO:0006879]; ERK1 and ERK2 cascade [GO:0070371]; osteoclast differentiation [GO:0030316]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of bone resorption [GO:0045780]; positive regulation of cell motility [GO:2000147]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of protein stability [GO:0031647]; retina homeostasis [GO:0001895]; SMAD protein signal transduction [GO:0060395]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]ferric iron binding [GO:0008199]; ferric iron transmembrane transporter activity [GO:0015091]; transferrin receptor binding [GO:1990459]apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; basal plasma membrane [GO:0009925]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; coated pit [GO:0005905]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; HFE-transferrin receptor complex [GO:1990712]; late endosome [GO:0005770]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; secretory granule lumen [GO:0034774]; vesicle [GO:0031982]lFUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.P49137MAPK2%MAP kinase-activated protein kinase 2 p38targetSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20932473}. Nucleus {ECO:0000269|PubMed:20932473}. Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm.3'-UTR-mediated mRNA stabilization [GO:0070935]; activation of MAPK activity [GO:0000187]; arachidonic acid metabolic process [GO:0019369]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to heat [GO:0034605]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; G2 DNA damage checkpoint [GO:0031572]; gene expression [GO:0010467]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; leukotriene metabolic process [GO:0006691]; macropinocytosis [GO:0044351]; MAPK cascade [GO:0000165]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; neurotrophin TRK receptor signaling pathway [GO:0048011]; p38MAPK cascade [GO:0038066]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of tumor necrosis factor biosynthetic process [GO:0042535]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of cellular response to heat [GO:1900034]; regulation of interleukin-6 production [GO:0032675]; regulation of tumor necrosis factor production [GO:0032680]; response to cytokine [GO:0034097]; response to lipopolysaccharide [GO:0032496]; response to stress [GO:0006950]; small molecule metabolic process [GO:0044281]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]zATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; signal transducer activity [GO:0004871]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: re< quired for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:11844797, ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:12565831, ECO:0000269|PubMed:14499342, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:16456544, ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:18021073, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8280084, ECO:0000269|PubMed:8774846}.P78560CRADD%Death domain-containing protein CRADDactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cellular response to mechanical stimulus [GO:0071260]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; positive regulation of apoptotic signaling pathway [GO:2001235]hdeath domain binding [GO:0070513]; protease binding [GO:0002020]; protein binding, bridging [GO:0030674]FUNCTION: Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex.Q9Y2I7FYV1+1-phosphatidylinositol 3-phosphate 5-kinaseSUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:11706043, ECO:0000269|PubMed:17556371}. Note=Mainly associated with membranes of the late endocytic pathway.intracellular signal transduction [GO:0035556]; myelin assembly [GO:0032288]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; protein localization to nucleus [GO:0034504]; retrograde transport, endosome to Golgi [GO:0042147]; small molecule metabolic process [GO:0044281] 1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813])cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17556371}.Q8WUW1BRK1Protein BRICK1Arp2/3 activatorsactin cytoskeleton organization [GO:0030036]; cell motility [GO:0048870]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; in utero embryonic development [GO:0001701]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; positive regulation of cell proliferation [GO:0008284]; positive regulation of lamellipodium assembly [GO:0010592]; protein homotrimerization [GO:0070207]; Rac protein signal transduction [GO:0016601]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]$protein complex binding [GO:0032403]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; SCAR complex [GO:0031209]FUNCTION: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. {ECO:0000269|PubMed:18560548}.Q5VWZ2LYPL1 Lysophospholipase-like protein 1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol {ECO:0000269|PubMed:22399288}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol {ECO:0000269|PubMed:22399288}.unegative regulation of Golgi to plasma membrane protein transport [GO:0042997]; protein depalmitoylation [GO:0002084]'lysophospholipase activity [GO:0004622]FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. {ECO:0000269|PubMed:22052940, ECO:0000269|PubMed:22399288}.Q06124PTN111Tyrosine-protein phosphatase non-receptor type 11STATSHP2 Phosphotase- abortive mitotic cell cycle [GO:0033277]; activation of MAPK activity [GO:0000187]; atrioventricular canal development [GO:0036302]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; brain development [GO:0007420]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage checkpoint [GO:0000077]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB signaling pathway [GO:0038127]; face morphogenesis [GO:0060325]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; genitalia development [GO:0048806]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; homeostasis of number of cells within a tissue [GO:0048873]; hormone-mediated signaling pathway [GO:0009755]; hormone metabolic process [GO:0042445]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; insulin receptor signaling pathway [GO:0008286]; integrin-mediated signaling pathway [GO:0007229]; interferon-gamma-mediated signaling pathway [GO:0060333]; intestinal epithelial cell migration [GO:0061582]; leukocyte migration [GO:0050900]; megakaryocyte development [GO:0035855]; microvillus organization [GO:0032528]; multicellular organismal reproductive process [GO:0048609]; multicellular organism growth [GO:0035264]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of cortisol secretion [GO:0051463]; negative regulation of growth hormone secretion [GO:0060125]; negative regulation of insulin secretion [GO:0046676]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ growth [GO:0035265]; peptidyl-tyrosine dephosphorylation [GO:0035335]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; platelet formation [GO:0030220]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of hormone secretion [GO:0046887]; positive regulation of mitotic cell cycle [GO:0045931]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of multicellular organism growth [GO:0040014]; regulation of protein export from nucleus [GO:0046825]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; T cell costimulation [GO:0031295]; triglyceride metabolic process [GO:0006641]; type I interferon signaling pathway [GO:0060337]insulin receptor binding [GO:0005158]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725]; SH3/SH2 adaptor activity [GO:0005070]|cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein complex [GO:0043234]ZFUNCTION: Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:18829< 466}.Q16539MK14#Mitogen-activated protein kinase 143'-UTR-mediated mRNA stabilization [GO:0070935]; activation of MAPK activity [GO:0000187]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; blood coagulation [GO:0007596]; cartilage condensation [GO:0001502]; cell morphogenesis [GO:0000902]; cell surface receptor signaling pathway [GO:0007166]; cellular response to ionizing radiation [GO:0071479]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; cellular response to virus [GO:0098586]; chemotaxis [GO:0006935]; chondrocyte differentiation [GO:0002062]; DNA damage checkpoint [GO:0000077]; fatty acid oxidation [GO:0019395]; gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; mitochondrion organization [GO:0007005]; movement of cell or subcellular component [GO:0006928]; muscle cell differentiation [GO:0042692]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; myoblast differentiation involved in skeletal muscle regeneration [GO:0014835]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; osteoclast differentiation [GO:0030316]; p38MAPK cascade [GO:0038066]; peptidyl-serine phosphorylation [GO:0018105]; placenta development [GO:0001890]; platelet activation [GO:0030168]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cyclase activity [GO:0031281]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of interleukin-12 secretion [GO:2001184]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein autophosphorylation [GO:0046777]; Ras protein signal transduction [GO:0007265]; regulation of cytokine production involved in inflammatory response [GO:1900015]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to glucose [GO:0009749]; response to muramyl dipeptide [GO:0032495]; response to muscle stretch [GO:0035994]; signal transduction [GO:0007165]; signal transduction in response to DNA damage [GO:0042770]; skeletal muscle tissue development [GO:0007519]; stress-activated MAPK cascade [GO:0051403]; stress-induced premature senescence [GO:0090400]; striated muscle cell differentiation [GO:0051146]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; enzyme binding [GO:0019899]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708]; NFAT protein binding [GO:0051525]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of th< e cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:16932740, ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:19893488, ECO:0000269|PubMed:20188673, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9792677, ECO:0000269|PubMed:9858528}.Q8IV50LYSM2CLysM and putative peptidoglycan-binding domain-containing protein 2Q9Y5L0TNPO3 Transportin-3eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10713112}. Nucleus {ECO:0000269|PubMed:10713112}.8splicing factor protein import into nucleus [GO:0035048]Fidentical protein binding [GO:0042802]; receptor activity [GO:0004872]ccytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]PFUNCTION: Seems to function in nuclear protein import as nuclear transport receptor. In vitro, mediates the nuclear import of splicing factor SR proteins RBM4, SFRS1 and SFRS2, by recognizing phosphorylated RS domains. {ECO:0000269|PubMed:10366588, ECO:0000269|PubMed:10713112, ECO:0000269|PubMed:11517331, ECO:0000269|PubMed:12628928}.O75155CAND2-Cullin-associated NEDD8-dissociated protein 2positive regulation of transcription, DNA-templated [GO:0045893]; protein ubiquitination [GO:0016567]; SCF complex assembly [GO:0010265]; transcription, DNA-templated [GO:0006351]0intracellular [GO:0005622]; nucleus [GO:0005634]FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. {ECO:0000250}.O95433AHSA17Activator of 90 kDa heat shock protein ATPase homolog 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11554768}. Endoplasmic reticulum {ECO:0000269|PubMed:11554768}. Note=May transiently interact with the endoplasmic reticulum.Tpositive regulation of ATPase activity [GO:0032781]; response to stress [GO:0006950]FATPase activator activity [GO:0001671]; chaperone binding [GO:0051087]tcytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]FUNCTION: Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking. {ECO:0000250}.Q9NUQ8ABCF3*ATP-binding cassette sub-family F member 3&defense response to virus [GO:0051607]6ATPase activity [GO:0016887]; ATP binding [GO:0005524]FUNCTION: Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B. {ECO:0000250}.P48147PPCEProlyl endopeptidaseproteolysis [GO:0006508]serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008]; serine-type peptidase activity [GO:0008236]Ccytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.Q9H2L5RASF4+Ras association domain-containing protein 49cell cycle [GO:0007049]; signal transduction [GO:0007165]FUNCTION: Potential tumor suppressor. May act as a KRAS effector protein. May promote apoptosis and cell cycle arrest. {ECO:0000269|PubMed:15574778}.Q08752PPID%Peptidyl-prolyl cis-trans isomerase DJSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm.dapoptotic process [GO:0006915]; cellular response to UV-A [GO:0071492]; chaperone-mediated protein folding [GO:0061077]; lipid particle organization [GO:0034389]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein secretion [GO:0050714]; positive regulation of viral genome replication [GO:0045070]; protein complex assembly [GO:0006461]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; protein transport [GO:0015031]; viral release from host cell [GO:0019076]!cyclosporin A binding [GO:0016018]; estrogen receptor binding [GO:0030331]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; transcription factor binding [GO:0008134]>FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis C virus (HCV) replication and release. {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059, ECO:0000269|PubMed:19932913, ECO:0000269|PubMed:21711559, ECO:0000269|PubMed:22681779, ECO:0000269|PubMed:23220213, ECO:0000269|PubMed:9659917}.P13807GYS1"Glycogen [starch] synthase, musclecarbohydrate metabolic process [GO:0005975]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; heart development [GO:0007507]; small molecule metabolic process [GO:0044281]glucose binding [GO:0005536]; glycogen (starch) synthase activity [GO:0004373]; glycogen synthase activity, transferring glucose-1-phosphate [GO:0061547]; protein kinase binding [GO:0019901]`cytoplasm [GO:0005737]; cytosol [GO:0005829]; inclusion body [GO:0016234]; membrane [GO:0016020]bFUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.Q86X76NIT1Nitrilase homolog 1=SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion {ECO:0000250}.0nitrogen compound metabolic process [GO:0006807]nitrilase activity [GO:0000257]Textracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Plays a role in cell growth and apoptosis: loss of expression< promotes cell growth and resistance to DNA damage stress. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. Has apparently no omega-amidase activity such as NIT2 (By similarity). {ECO:0000250}.Q9ULH1ASAP1FArf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Predominantly cytoplasmic. Partially membrane-associated. {ECO:0000250}.Fcilium morphogenesis [GO:0060271]; organelle organization [GO:0006996]GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]+cytosol [GO:0005829]; membrane [GO:0016020]FUNCTION: Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:20393563}.Q9Y5X2SNX8Sorting nexin-8SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:19782049}; Peripheral membrane protein {ECO:0000269|PubMed:19782049}; Cytoplasmic side {ECO:0000269|PubMed:19782049}. Note=Colocalizes with retromer components.early endosome to Golgi transport [GO:0034498]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; vesicle organization [GO:0016050]Qidentical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]early endosome membrane [GO:0031901]; endosome [GO:0005768]; extrinsic component of membrane [GO:0019898]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network. {ECO:0000269|PubMed:19782049}.Q86X83COMD2 COMM domain-containing protein 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21778237}.FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.Q9UQ13SHOC2"Leucine-rich repeat protein SHOC-2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19684605}. Nucleus {ECO:0000269|PubMed:19684605}. Note=Translocates from cytoplasm to nucleus upon growth factor stimulation.fibroblast growth factor receptor signaling pathway [GO:0008543]; positive regulation of Ras protein signal transduction [GO:0046579]; Ras protein signal transduction [GO:0007265]; regulation of catalytic activity [GO:0050790]]protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888]wcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein phosphatase type 1 complex [GO:0000164]~FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that acts as a M-Ras/MRAS effector and participates in MAPK pathway activation. Upon M-Ras/MRAS activation, targets PP1c to specifically dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and stimulate RAF1 activity at specialized signaling complexes. {ECO:0000269|PubMed:10783161, ECO:0000269|PubMed:16630891}.P08237PFKAM0ATP-dependent 6-phosphofructokinase, muscle typeBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; fructose 6-phosphate metabolic process [GO:0006002]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; muscle cell cellular homeostasis [GO:0046716]; positive regulation of insulin secretion [GO:0032024]; protein oligomerization [GO:0051259]; small molecule metabolic process [GO:0044281]6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]6-phosphofructokinase complex [GO:0005945]; apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; sperm principal piece [GO:0097228]FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.P19623SPEESpermidine synthase! Amine and polyamine biosynthesiscellular nitrogen compound metabolic process [GO:0034641]; polyamine metabolic process [GO:0006595]; small molecule metabolic process [GO:0044281]; spermidine biosynthetic process [GO:0008295]Yprotein homodimerization activity [GO:0042803]; spermidine synthase activity [GO:0004766]*FUNCTION: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine. {ECO:0000269|PubMed:17585781}.P42025ACTYBeta-centractinrSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.^antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome.Q9NQY0BIN3Bridging integrator 3aactin filament organization [GO:0007015]; barrier septum assembly [GO:0000917]; cytokinesis [GO:0000910]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; protein localization [GO:0008104]; regulation of lamellipodium assembly [GO:0010591]; skeletal muscle fiber development [GO:0048741]; unidimensional cell growth [GO:0009826]*cytoskeletal adaptor activity [GO:0008093]3actin filament [GO:0005884]; cytoplasm [GO:0005737]cFUNCTION: Involved in cytokinesis and septation where it has a role in the localization of F-actin.P21333FLNA Filamin-AFSUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.actin crosslink formation [GO:0051764]; actin cytoskeleton reorganization [GO:0031532]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; blood coagulation [GO:0007596]; cell junction assembly [GO:0034329]; cilium assembly [GO:0042384]; cytoplasmic sequestering of protein [GO:0051220]; early endosome to late endosome transport [GO:0045022]; epithelial to mesenchymal transition [GO:0001837]; establishment of protein localization [GO:0045184]; mitotic spindle assembly [GO:0090307]; mRNA transcription from RNA polymerase II promoter [GO:0042789]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription from RNA polymerase I promoter [GO:0016479]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of transcription factor import into nucleus [GO:0042993]; protein localization to cell surface [GO:0034394]; protein stabilization [GO:0050821]; receptor clustering [GO:0043113]; smal< l GTPase mediated signal transduction [GO:0007264]actin filament binding [GO:0051015]; Fc-gamma receptor I complex binding [GO:0034988]; glycoprotein binding [GO:0001948]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; Rac GTPase binding [GO:0048365]; Ral GTPase binding [GO:0017160]; Rho GTPase binding [GO:0017048]; signal transducer activity [GO:0004871]; small GTPase binding [GO:0031267]; transcription factor binding [GO:0008134]@actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; actin filament bundle [GO:0032432]; apical dendrite [GO:0097440]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; membrane [GO:0016020]; Myb complex [GO:0031523]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]2FUNCTION: Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. {ECO:0000250, ECO:0000269|PubMed:22121117}.Q86V21AACSAcetoacetyl-CoA synthetaseButanoate metabolism7SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.Uadipose tissue development [GO:0060612]; cellular response to cholesterol [GO:0071397]; cellular response to glucose stimulus [GO:0071333]; cellular response to testosterone stimulus [GO:0071394]; fatty acid metabolic process [GO:0006631]; liver development [GO:0001889]; positive regulation of insulin secretion [GO:0032024]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to nutrient [GO:0007584]; response to oleic acid [GO:0034201]; response to purine-containing compound [GO:0014074]; response to starvation [GO:0042594]; white fat cell differentiation [GO:0050872]racetoacetate-CoA ligase activity [GO:0030729]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]FUNCTION: Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development (By similarity). {ECO:0000250}.Q8TF05PP4R1;Serine/threonine-protein phosphatase 4 regulatory subunit 1fdephosphorylation [GO:0016311]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]:protein phosphatase type 4 regulator activity [GO:0030362]*protein phosphatase 4 complex [GO:0030289]FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. {ECO:0000269|PubMed:15805470}.P34947GRK5#G protein-coupled receptor kinase 5(SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Note=Predominantly localized at the plasma membrane; targeted to the cell surface through the interaction with phospholipids. Nucleus localization is regulated in a GPCR and Ca(2+)/calmodulin-dependent fashion.adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; apoptotic process [GO:0006915]; desensitization of G-protein coupled receptor protein signaling pathway [GO:0002029]; fat cell differentiation [GO:0045444]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell proliferation [GO:0008284]; protein autophosphorylation [GO:0046777]; regulation of cell cycle [GO:0051726]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; response to drug [GO:0042493]; tachykinin receptor signaling pathway [GO:0007217]; termination of G-protein coupled receptor signaling pathway [GO:0038032]; Wnt signaling pathway [GO:0016055] ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; G-protein coupled receptor kinase activity [GO:0004703]; phospholipid binding [GO:0005543]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]1FUNCTION: Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro). {ECO:0000269|PubMed:19661922, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20038610, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:21728385}.Q7Z4I7LIMS2?LIM and senescent cell antigen-like-containing domain protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction, focal adhesion {ECO:0000269|PubMed:12167643}. Cell membrane {ECO:0000269|PubMed:12167643}; Peripheral membrane protein {ECO:0000269|PubMed:12167643}; Cytoplasmic side {ECO:0000269|PubMed:12167643}.cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; negative regulation of apoptotic process [GO:0043066]; negative regulation of hepatocyte proliferation [GO:2000346]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; single organismal cell-cell adhesion [GO:0016337]ecytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Plays a role in modulating cell spreading and migration. {ECO:0000269|PubMed:12167643}.Q9Y485DMXL1DmX-like protein 1Q16401PSMD5.26S proteasome non-ATPase regulatory subunit 5panaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell c< ycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome regulatory particle assembly [GO:0070682]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]zcytosol [GO:0005829]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5. {ECO:0000269|PubMed:19412159, ECO:0000269|PubMed:19490896}.Q6P996PDXD1=Pyridoxal-dependent decarboxylase domain-containing protein 1.carboxylic acid metabolic process [GO:0019752]Mcarboxy-lyase activity [GO:0016831]; pyridoxal phosphate binding [GO:0030170]SGolgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]P46108CRKAdapter molecule crkSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocated to the plasma membrane upon cell adhesion. {ECO:0000250}.activation of MAPKK activity [GO:0000186]; blood coagulation [GO:0007596]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of GTPase activity [GO:0043087]; regulation of Rac protein signal transduction [GO:0035020]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]Eephrin receptor binding [GO:0046875]; SH2 domain binding [GO:0042169]FUNCTION: The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. {ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:1630456, ECO:0000269|PubMed:17515907}.Q9BY32ITPA$Inosine triphosphate pyrophosphatase_SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:11278832}.chromosome organization [GO:0051276]; deoxyribonucleoside triphosphate catabolic process [GO:0009204]; ITP catabolic process [GO:0006193]; nucleobase-containing small molecule metabolic process [GO:0055086]; small molecule metabolic process [GO:0044281]dITP diphosphatase activity [GO:0035870]; ITP diphosphatase activity [GO:0036220]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; XTP diphosphatase activity [GO:0036222]FFUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_03148, ECO:0000269|PubMed:17090528}.Q96CX2KCD12(BTB/POZ domain-containing protein KCTD12SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}.(protein homooligomerization [GO:0051260]cell junction [GO:0030054]; extracellular exosome [GO:0070062]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity). {ECO:0000250}.Q9H9A6LRC40)Leucine-rich repeat-containing protein 40Q96C19EFHD2$EF-hand domain-containing protein D2pSUBCELLULAR LOCATION: Membrane raft {ECO:0000250}. Note=In a mouse immature B-cell line WEHI-231. {ECO:0000250}.membrane raft [GO:0045121]FUNCTION: May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. {ECO:0000250}.Q3KQV9UAP1L7UDP-N-acetylhexosamine pyrophosphorylase-like protein 19UDP-N-acetylglucosamine biosynthetic process [GO:0006048]=UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977]Q9BRT3MIEN1!Migration and invasion enhancer 1SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Lipid-anchor; Cytoplasmic side. Note=Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions.apoptotic process [GO:0006915]; cell redox homeostasis [GO:0045454]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell migration [GO:0030335]; positive regulation of filopodium assembly [GO:0051491]selenium binding [GO:0008430]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; nucleoplasm [GO:0005654]FUNCTION: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process. {ECO:0000269|PubMed:19503095, ECO:0000269|PubMed:21628459}.Q9Y3C0CCD53WASH complex subunit CCDC533SUBCELLULAR LOCATION: Early endosome {ECO:0000305}.actin cytoskeleton [GO:0015629]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]; WASH complex [GO:0071203]FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.O95396MOCS3/Adenylyltransferase and sulfurtransferase MOCS3Sulfur relay system tRNA modification_SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332}.enzyme active site formation via L-cysteine persulfide [GO:0018192]; molybdopterin cofactor biosynthetic process [GO:0032324]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein adenylylation [GO:0018117]; protein urmylation [GO:0032447]; small molecule metabolic process [GO:0044281]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase acti< vity [GO:0016779]; protein adenylyltransferase activity [GO:0070733]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292]FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:19017811}.P61221ABCE1*ATP-binding cassette sub-family E member 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}. Mitochondrion {ECO:0000269|PubMed:11585831}. Note=Localized to clusters of virus formation at the plasma membrane.negative regulation of catalytic activity [GO:0043086]; response to virus [GO:0009615]; RNA catabolic process [GO:0006401]; transmembrane transport [GO:0055085]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; iron-sulfur cluster binding [GO:0051536]; ribonuclease inhibitor activity [GO:0008428]lcytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway. May act as a chaperone for post-translational events during HIV-1 capsid assembly. {ECO:0000269|PubMed:11585831, ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.Q9NYB9ABI2Abl interactor 2<SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Isoform 1 but not isoform 3 is localized to protruding lamellipodia and filopodia tips. {ECO:0000250}.zactin polymerization or depolymerization [GO:0008154]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; movement of cell or subcellular component [GO:0006928]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; Rac protein signal transduction [GO:0016601]; viral process [GO:0016032]cytoskeletal adaptor activity [GO:0008093]; DNA binding [GO:0003677]; kinase binding [GO:0019900]; proline-rich region binding [GO:0070064]; protein complex binding [GO:0032403]; SH3 domain binding [GO:0017124]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; SCAR complex [GO:0031209]FUNCTION: May act in regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA. {ECO:0000269|PubMed:10498863, ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}.Q92609TBCD5TBC1 domain family member 5SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:20923837}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:22354992}. Note=During starvation induced autophagy is relocalized from endosomal localization to LC3-positive autophagosomes. {ECO:0000269|PubMed:22354992}.Pactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; autophagy [GO:0006914]; positive regulation of autophagy [GO:0010508]; positive regulation of receptor internalization [GO:0002092]; protein transport [GO:0015031]; response to starvation [GO:0042594]; retrograde transport, endosome to Golgi [GO:0042147]QAP-2 adaptor complex binding [GO:0035612]; GTPase activator activity [GO:0005096]{autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; endosome membrane [GO:0010008]; retromer complex [GO:0030904]FUNCTION: May act as a GTPase-activating protein (GAP) for Rab family protein(s). May act as a GAP for RAB7A. Can displace RAB7A and retromer CSC subcomplex from the endosomal membrane to the cytosol; at least retromer displacement seems to require its catalytic activity (PubMed:19531583, PubMed:20923837). Required for retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN); the function seems to require its catalytic activity. Involved in regulation of autophagy (PubMed:22354992). May act as a molecular switch between endosomal and autophagosomal transport and is involved in reprogramming vesicle trafficking upon autophagy induction. Involved in the trafficking of ATG9A upon activation of autophagy. May regulate the recruitment of ATG9A-AP2-containing vesicles to autophagic membranes (PubMed:24603492). {ECO:0000269|PubMed:19531583, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:24603492, ECO:0000305|PubMed:19531583, ECO:0000305|PubMed:22354992, ECO:0000305|PubMed:24603492}.Q9H2G2SLK*STE20-like serine/threonine-protein kinaseVactivation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; protein autophosphorylation [GO:0046777]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]OFUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.P45974UBP5'Ubiquitin carboxyl-terminal hydrolase 5positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]cysteine-type endopeptidase activity [GO:0004197]; omega peptidase activity [GO:0008242]; ubiquitin binding [GO:0043130]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]lysosome [GO:0005764]FUNCTION: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. {ECO:0000269|PubMed:19098288}.P31948STIP1Stress-induced-phosphoprotein 1response to stress [GO:0006950]lGolgi apparatus [GO:0005794]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; protein complex [GO:0043234]aFUNCTION: Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).Q9NWZ3IRAK4*Interleukin-1 receptor-associated kinase 4>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21325272}.cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755< ]; neutrophil mediated immunity [GO:0002446]; neutrophil migration [GO:1990266]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nucleus [GO:0005634]; plasma membrane [GO:0005886]eFUNCTION: Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates NCF1 and regulates NADPH oxidase activation after LPS stimulation suggesting a similar mechanism during microbial infections. {ECO:0000269|PubMed:11960013, ECO:0000269|PubMed:12538665, ECO:0000269|PubMed:15084582, ECO:0000269|PubMed:17217339, ECO:0000269|PubMed:17337443, ECO:0000269|PubMed:17878374, ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:20400509, ECO:0000269|PubMed:24316379}.P54727RD23B*UV excision repair protein RAD23 homolog B Nucleotide excision repair (NER)"SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; nucleotide-excision repair, DNA damage removal [GO:0000718]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; spermatogenesis [GO:0007283]ndamaged DNA binding [GO:0003684]; polyubiquitin binding [GO:0031593]; single-stranded DNA binding [GO:0003697]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; XPC complex [GO:0071942]FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.Q9BV86NTM1A,N-terminal Xaa-Pro-Lys N-methyltransferase 1uSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:24090352}. Note=Predominantly nuclear.\chromosome segregation [GO:0007059]; N-terminal peptidyl-alanine methylation [GO:0018011]; N-terminal peptidyl-alanine trimethylation [GO:0018012]; N-terminal peptidyl-proline dimethylation [GO:0018016]; N-terminal peptidyl-serine dimethylation [GO:0035572]; N-terminal peptidyl-serine trimethylation [GO:0035573]; spindle organization [GO:0007051]mN-terminal protein N-methyltransferase activity [GO:0071885]; protein methyltransferase activity [GO:0008276]FUNCTION: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1. {ECO:0000269|PubMed:20481588, ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:24090352}.Q9Y371SHLB1 Endophilin-B1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15452144}. Golgi apparatus membrane {ECO:0000269|PubMed:21068542}; Peripheral membrane protein {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:15452144}; Peripheral membrane protein {ECO:0000269|PubMed:15452144}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:17891140}. Midbody {ECO:0000269|PubMed:20643123}. Note=Association with the Golgi apparatus depends on the cell type (By similarity). Following starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on autophagosomal membranes (PubMed:17891140). {ECO:0000250, ECO:0000269|PubMed:17891140}.apoptotic process [GO:0006915]; autophagic cell death [GO:0048102]; autophagy [GO:0006914]; cellular response to amino acid starvation [GO:0034198]; cellular response to glucose starvation [GO:0042149]; membrane fission [GO:0090148]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of autophagy [GO:0010508]; positive regulation of membrane tubulation [GO:1903527]; positive regulation of protein oligomerization [GO:0032461]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein localization to vacuolar membrane [GO:1903778]; protein oligomerization [GO:0051259]; receptor catabolic process [GO:0< 032801]; regulation of cytokinesis [GO:0032465]; regulation of protein stability [GO:0031647]ridentical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; midbody [GO:0030496]; mitochondrial outer membrane [GO:0005741]FUNCTION: May be required for normal outer mitochondrial membrane dynamics (PubMed:15452144). Required for coatomer-mediated retrograde transport in certain cells (By similarity). May recruit other proteins to membranes with high curvature. May promote membrane fusion (PubMed:11604418). Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 acts proapoptotic in fibroblasts (By similarity). Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2) (PubMed:17891140). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation (PubMed:21068542). Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123). Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance of mitochondrial morphology and promotes neuronal viability (By similarity). {ECO:0000250|UniProtKB:Q9JK48, ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:15452144, ECO:0000269|PubMed:17891140, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:21068542}.O60443DFNA5*Non-syndromic hearing impairment protein 5apoptotic process [GO:0006915]; inner ear receptor cell differentiation [GO:0060113]; negative regulation of cell proliferation [GO:0008285]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; sensory perception of sound [GO:0007605]FUNCTION: Involved in apoptosis and cell survival. Plays a role in the TP53-regulated cellular response to DNA damage probably by cooperating with TP53. {ECO:0000269|PubMed:16897187, ECO:0000269|PubMed:18223688, ECO:0000269|PubMed:21522185}.Q0VDF9HSP7EHeat shock 70 kDa protein 14Heat Shock ProteinHSP70GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16002468}.5de novo' cotranslational protein folding [GO:0051083]%FUNCTION: Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. {ECO:0000269|PubMed:16002468}.Q96BY7ATG2B%Autophagy-related protein 2 homolog BSUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:22219374}; Peripheral membrane protein {ECO:0000269|PubMed:22219374}. Lipid droplet {ECO:0000269|PubMed:22219374}.autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]extrinsic component of membrane [GO:0019898]; lipid particle [GO:0005811]; pre-autophagosomal structure [GO:0000407]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. {ECO:0000269|PubMed:22219374}.Q9NU19TB22BTBC1 domain family member 22BZFUNCTION: May act as a GTPase-activating protein for Rab family protein(s). {ECO:0000250}.Q15382RHEBGTP-binding protein RhebRheb activating mTorC+SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:22002721, ECO:0000305}; Lipid-anchor {ECO:0000269|PubMed:22002721, ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:15489334, ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:22002721}; Lipid-anchor {ECO:0000305|PubMed:22002721}; Cytoplasmic side {ECO:0000305|PubMed:22002721}. Cytoplasm, cytosol {ECO:0000269|PubMed:22002721}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22002721}; Lipid-anchor {ECO:0000269|PubMed:22002721}; Cytoplasmic side {ECO:0000269|PubMed:22002721}.cell cycle arrest [GO:0007050]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; positive regulation of TOR signaling [GO:0032008]; regulation of type B pancreatic cell development [GO:2000074]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; transcription initiation from RNA polymerase II promoter [GO:0006367]VGTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]; spliceosomal complex [GO:0005681]FUNCTION: Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:12869586, ECO:0000269|PubMed:15340059, ECO:0000269|PubMed:15854902, ECO:0000269|PubMed:16098514, ECO:0000269|PubMed:20381137}.Q96H79ZCCHL.Zinc finger CCCH-type antiviral protein 1-likeP622581433E14-3-3 protein epsilonSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to heat [GO:0034605]; cerebral cortex development [GO:0021987]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; hippocampus development [GO:0021766]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; membrane organization [GO:0061024]; membrane repolarization during cardiac muscle cell action potential [GO:0086013]; mitotic cell cycle [GO:0000278]; negative regulation of peptidyl-serine dephosphorylation [GO:1902309]; neuron migration [GO:0001764]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; protein targeting [GO:0006605]; regulation of cellular response to heat [GO:1900034]; regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043281]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of heart rate by hormone [GO:0003064]; regulation of membrane repolarization [GO:0060306]; regulation of potassium ion transmembrane transporter activity [GO:1901016]; small GTPase mediated signal transduction [GO:0007264]; substantia nigra development [GO:0021762]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; ion channel binding [GO:0044325]; MHC class II protein complex binding [GO:0023026]; phosphoprotein binding [GO:0051219]; phosphoserine binding [GO:0050815]; poly(A) RNA binding [GO:0044822]; potassium channel regulator activity [GO:0015459]; protein heterodimerization activity [GO:0046982]; ubiquitin protein ligase binding [GO:0031625]axon [GO:0030424]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; kinesin complex [GO:0005871]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]<FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by < recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.Q7Z6M1RABEK'Rab9 effector protein with kelch motifsSUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Note=Interaction with PIP5K3 and subsequent phosphorylation recruits it to the endosomal membrane._receptor-mediated endocytosis [GO:0006898]; vesicle docking involved in exocytosis [GO:0006904]endosome [GO:0005768]; endosome membrane [GO:0010008]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]sFUNCTION: Rab9 effector required for endosome to trans-Golgi network (TGN) transport. {ECO:0000269|PubMed:9230071}.P61758PFD3Prefoldin subunit 3bSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL can translocate to the nucleus.de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; microtubule-based process [GO:0007017]; protein folding [GO:0006457]; tubulin complex assembly [GO:0007021]tubulin binding [GO:0015631]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; polysome [GO:0005844]; prefoldin complex [GO:0016272]Q99704DOK1Docking protein 1uSUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, perinuclear region.cell surface receptor signaling pathway [GO:0007166]; insulin receptor signaling pathway [GO:0008286]; Ras protein signal transduction [GO:0007265]; signal transduction [GO:0007165]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]pcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]jFUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. {ECO:0000269|PubMed:18156175}.Q14204DYHC1"Cytoplasmic dynein 1 heavy chain 1antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cytoplasmic mRNA processing body assembly [GO:0033962]; establishment of spindle localization [GO:0051293]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; mitotic spindle organization [GO:0007052]; organelle organization [GO:0006996]; stress granule assembly [GO:0034063]; transport [GO:0006810]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule motor activity [GO:0003777]; poly(A) RNA binding [GO:0044822]centrosome [GO:0005813]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; membrane [GO:0016020]; microtubule [GO:0005874]FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.Q9NP97DLRB1#Dynein light chain roadblock-type 1microtubule-based movement [GO:0007018]; organelle organization [GO:0006996]; transport [GO:0006810]; visual behavior [GO:0007632]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; membrane [GO:0016020]; microtubule [GO:0005874]; primary cilium [GO:0072372]XFUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.Q9UI30TR112=Multifunctional methyltransferase subunit TRM112-like protein+peptidyl-glutamine methylation [GO:0018364]/protein methyltransferase activity [GO:0008276]@extracellular exosome [GO:0070062]; protein complex [GO:0043234]FUNCTION: Participates both in methylation of protein and tRNA species. The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. {ECO:0000269|PubMed:18539146}.Q9BYM8HOIL1:RanBP-type and C3HC4-type zinc finger-containing protein 1negative regulation of necroptotic process [GO:0060546]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB import into nucleus [GO:0042346]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein linear polyubiquitination [GO:0097039]; protein polyubiquitination [GO:0000209]; T cell receptor signaling pathway [GO:0050852]; viral process [GO:0016032]ligase activity [GO:0016874]; ubiquitin binding [GO:0043130]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]LUBAC complex [GO:0071797]FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types. {ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:18711448, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}.Q01813PFKAP2ATP-dependent 6-phosphofructokinase, platelet typeWactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; fructose 6-phosphate metabolic process [GO:0006002]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein complex binding [GO:0032403]ecytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]P84085ARF5ADP-ribosylation factor 5protein transport [GO:0015031]; small GTPase mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]P23743DGKADiacylglycerol kinase alphaGlycerolipid metabolismblood coagulation [GO:0007596]; intracellular signal transduction [GO:0035556]; platelet acti< vation [GO:0030168]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; diacylglycerol kinase activity [GO:0004143]; phospholipid binding [GO:0005543]Icytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity.O75116ROCK2Rho-associated protein kinase 2SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane. {ECO:0000250}.\actin cytoskeleton organization [GO:0030036]; axon guidance [GO:0007411]; cellular response to testosterone stimulus [GO:0071394]; centrosome duplication [GO:0051298]; cytokinesis [GO:0000910]; dendrite morphogenesis [GO:0048813]; ephrin receptor signaling pathway [GO:0048013]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; negative regulation of angiogenesis [GO:0016525]; neural tube closure [GO:0001843]; positive regulation of centrosome duplication [GO:0010825]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell adhesion [GO:0030155]; regulation of cell motility [GO:2000145]; regulation of circadian rhythm [GO:0042752]; regulation of establishment of cell polarity [GO:2000114]; regulation of focal adhesion assembly [GO:0051893]; regulation of keratinocyte differentiation [GO:0045616]; regulation of stress fiber assembly [GO:0051492]; Rho protein signal transduction [GO:0007266]; rhythmic process [GO:0048511]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle contraction [GO:0006939]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein serine/threonine kinase activity [GO:0004674]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; structural molecule activity [GO:0005198]centrosome [GO:0005813]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle pole centrosome [GO:0031616]=FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:10579722, ECO:0000269|PubMed:15699075, ECO:0000269|PubMed:16574662, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:21147781}.Q5VU43MYOME MyomegalinSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:11374908}. Nucleus {ECO:0000269|PubMed:11374908}..cellular protein complex assembly [GO:0043623]enzyme binding [GO:0019899]{centrosome [GO:0005813]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; myofibril [GO:0030016]; nucleus [GO:0005634]FUNCTION: May function as an anchor sequestering components of the cAMP-dependent pathway to Golgi and/or centrosomes. {ECO:0000250}.Q86TU7SETD3(Histone-lysine N-methyltransferase setd3=SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91WC0}.histone H3-K36 methylation [GO:0010452]; peptidyl-lysine dimethylation [GO:0018027]; peptidyl-lysine monomethylation [GO:0018026]; peptidyl-lysine trimethylation [GO:0018023]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]histone methyltransferase activity (H3-K36 specific) [GO:0046975]; histone methyltransferase activity (H3-K4 specific) [GO:0042800]; transcription coactivator activity [GO:0003713]nuclear chromatin [GO:0000790]&FUNCTION: Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). Acts as a transcriptional activator. Plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.P301532AAAQSerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere {ECO:0000269|PubMed:16580887}. Note=Centromeric localization requires the presence of BUB1.7apoptotic process [GO:0006915]; ceramide metabolic process [GO:0006672]; chromosome segregation [GO:0007059]; female meiotic division [GO:0007143]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; inactivation of MAPK activity [GO:0000188]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; meiotic spindle elongation [GO:0051232]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope reassembly [GO:0007084]; mitotic sister chromatid separation [GO:0051306]; negative regulation of cell growth [GO:0030308]; negative regulation of tyrosine phosphorylation of Stat3 protein [GO:0042518]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; organelle organization [GO:0006996]; peptidyl-serine dephosphorylation [GO:0070262]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein complex assembly [GO:0006461]; protein dephosphorylation [GO:0006470]; regulation of cell adhesion [GO:0030155]; regulation of cell differentiation [GO:0045595]; regulation of DNA replication [GO:0006275]; regulation of growth [GO:0040008]; regulation of meiotic cell cycle process involved in oocyte maturation [GO:1903538]; regulation of protein phosphatase type 2A activity [GO:0034047]; regulation of transcription, DNA-templated [GO:0006355]; regulation of Wnt signaling pathway [GO:0030111]; response to organic substance [GO:0010033]; RNA splicing [GO:0008380]; second-messenger-mediated signaling [GO:0019932]antigen binding [GO:0003823]; protein heterodimerization activity [GO:0046982]; protein phosphatase type 2A regulator activity [GO:0008601]; protein serine/threonine phosphatase activity [GO:0004722]chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159].FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregati< on and for centromeric localization of SGOL1 in mitosis. {ECO:0000269|PubMed:16580887}.Q14232EI2BA2Translation initiation factor eIF-2B subunit alpha cellular protein metabolic process [GO:0044267]; cellular response to stimulus [GO:0051716]; gene expression [GO:0010467]; negative regulation of translational initiation in response to stress [GO:0032057]; oligodendrocyte development [GO:0014003]; positive regulation of GTPase activity [GO:0043547]; regulation of translational initiation [GO:0006446]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to peptide hormone [GO:0043434]; translation [GO:0006412]; translational initiation [GO:0006413]enzyme regulator activity [GO:0030234]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; translation initiation factor activity [GO:0003743]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]; membrane [GO:0016020]; plasma membrane [GO:0005886]UFUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.O60504VINEXVinexinLSUBCELLULAR LOCATION: Isoform Alpha: Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform Beta: Cell junction {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell-extracellular matrix junctions (By similarity). Both isoforms were localized at focal adhesion and cell-cell adhesion sites, vinexin beta was also found in the nucleus. {ECO:0000250}.actin filament organization [GO:0007015]; cell adhesion [GO:0007155]; cell-substrate adhesion [GO:0031589]; muscle contraction [GO:0006936]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cytoskeleton organization [GO:0051495]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of stress fiber assembly [GO:0051496]Rstructural constituent of cytoskeleton [GO:0005200]; vinculin binding [GO:0017166]bcytoskeleton [GO:0005856]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]FUNCTION: Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain.Q9Y5K6CD2APCD2-associated proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles. Located at podocyte slit diaphragm between podocyte foot processes (By similarity). During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase. {ECO:0000250, ECO:0000269|PubMed:15800069}.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; negative regulation of transforming growth factor beta1 production [GO:0032911]; positive regulation of protein localization to nucleus [GO:1900182]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein complex assembly [GO:0006461]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of receptor-mediated endocytosis [GO:0048259]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]; substrate-dependent cell migration, cell extension [GO:0006930]; vesicle organization [GO:0016050]TSH3 domain binding [GO:0017124]; structural constituent of cytoskeleton [GO:0005200]5actin cytoskeleton [GO:0015629]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]gFUNCTION: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis. {ECO:0000269|PubMed:15800069}.Q93008USP9X4Probable ubiquitin carboxyl-terminal hydrolase FAF-X>SUBCELLULAR LOCATION: Cytoplasm. Cell projection, growth cone.axon extension [GO:0048675]; BMP signaling pathway [GO:0030509]; cell division [GO:0051301]; cerebellar cortex structural organization [GO:0021698]; chromosome segregation [GO:0007059]; female gamete generation [GO:0007292]; gene expression [GO:0010467]; hippocampus development [GO:0021766]; in utero embryonic development [GO:0001701]; mitotic nuclear division [GO:0007067]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron migration [GO:0001764]; post-embryonic development [GO:0009791]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]co-SMAD binding [GO:0070410]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; ubiquitin-specific protease activity [GO:0004843]apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; membrane [GO:0016020]DFUNCTION: Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Essential component of TGF-beta/BMP signaling cascade. Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains. Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Involved in axonal growth and neuronal cell migration. {ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18254724, ECO:0000269|PubMed:19135894, ECO:0000269|PubMed:24607389}.Q96P70IPO9 Importin-9(protein import into nucleus [GO:0006606]Ghistone binding [GO:0042393]; protein transporter activity [GO:0008565]*FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of H2B histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains. May also import H2A, H3, H4 histones (By similarity), RPL4 and RPL6. {ECO:0000250, ECO:0000269|PubMed:11823430}.Q9Y2T2AP3M1AP-3 complex subunit mu-1Transport-Aps(22)SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Perip< heral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; protein targeting to lysosome [GO:0006622]clathrin adaptor complex [GO:0030131]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.Q16773KAT1'Kynurenine--oxoglutarate transaminase 1Tryptophan metabolismcellular amino acid biosynthetic process [GO:0008652]; cellular modified amino acid metabolic process [GO:0006575]; cellular nitrogen compound metabolic process [GO:0034641]; kynurenine metabolic process [GO:0070189]; L-kynurenine catabolic process [GO:0097053]; L-phenylalanine catabolic process [GO:0006559]; small molecule metabolic process [GO:0044281]; tryptophan catabolic process [GO:0006569]cysteine-S-conjugate beta-lyase activity [GO:0047804]; glutamine-phenylpyruvate transaminase activity [GO:0047316]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-glutamine:pyruvate aminotransferase activity [GO:0047945]; L-phenylalanine:pyruvate aminotransferase activity [GO:0047312]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483]FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. {ECO:0000269|PubMed:19338303}.Q99417MYCBPC-Myc-binding proteinSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Translocates into the nucleus in the S phase of the cell cycle upon an increase of MYC expression. Found in the mitochondria when associated with AKAP1.regulation of transcription, DNA-templated [GO:0006355]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]acentrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]}FUNCTION: May control the transcriptional activity of MYC. Stimulates the activation of E box-dependent transcription by MYC.Q9NWV8BABA1"BRISC and BRCA1-A complex member 1oSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).chromatin modification [GO:0016568]; double-strand break repair [GO:0006302]; G2 DNA damage checkpoint [GO:0031572]; positive regulation of DNA repair [GO:0045739]; protein K63-linked deubiquitination [GO:0070536]; response to ionizing radiation [GO:0010212]BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]}FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}.O00442RTCA!RNA 3'-terminal phosphate cyclase+SUBCELLULAR LOCATION: Nucleus, nucleoplasm.RNA processing [GO:0006396]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; RNA-3'-phosphate cyclase activity [GO:0003963]; RNA binding [GO:0003723].nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.Q8NBF2NHLC2NHL repeat-containing protein 2Q96CN4EVI5LEVI5-like proteinhnegative regulation of cilium assembly [GO:1902018]; positive regulation of GTPase activity [GO:0043547]GGTPase activator activity [GO:0005096]; Rab GTPase binding [GO:0017137]qFUNCTION: Functions as a GTPase-activating protein (GAP) with a broad specificity. {ECO:0000269|PubMed:16923123}.Q96JG6CC132)Coiled-coil domain-containing protein 132GSUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:25799061}.@endocytic recycling [GO:0032456]; protein transport [GO:0015031]uEARP complex [GO:1990745]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; recycling endosome [GO:0055037]FUNCTION: Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). {ECO:0000269|PubMed:25799061}.O95671ASML2N-acetylserotonin O-methyltransferase-like protein)O-methyltransferase activity [GO:0008171]FUNCTION: Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity.Q9NPH2INO1Inositol-3-phosphate synthase 1 Polyol metabolisminositol biosynthetic process [GO:0006021]; inositol phosphate metabolic process [GO:0043647]; phospholipid biosynthetic process [GO:0008654]; small molecule metabolic process [GO:0044281]3inositol-3-phosphate synthase activity [GO:0004512]FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds. {ECO:0000269|PubMed:15024000}.P30043BLVRBFlavin reductase (NADPH)=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7929092}.heme catabolic process [GO:0042167]; porphyrin-containing compound metabolic process [GO:0006778]; small molecule metabolic process [GO:0044281]^biliverdin reductase activity [GO:0004074]; riboflavin reductase (NADPH) activity [GO:0042602]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin. {ECO:0000269|PubMed:10620517}.Q12802AKP13A-kinase anchor protein 133SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane< .Gapoptotic signaling pathway [GO:0097190]; neurotrophin TRK receptor signaling pathway [GO:0048011]; nuclear export [GO:0051168]; positive regulation of apoptotic process [GO:0043065]; protein phosphorylation [GO:0006468]; regulation of cardiac muscle hypertrophy [GO:0010611]; regulation of glucocorticoid mediated signaling pathway [GO:1900169]; regulation of protein kinase activity [GO:0045859]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]cAMP-dependent protein kinase activity [GO:0004691]; metal ion binding [GO:0046872]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] FUNCTION: Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions. {ECO:0000269|PubMed:11546812, ECO:0000269|PubMed:11579095, ECO:0000269|PubMed:9627117, ECO:0000269|PubMed:9891067}.Q8IXL7MSRB3#Methionine-R-sulfoxide reductase B3hSUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion.Fprotein repair [GO:0030091]; response to oxidative stress [GO:0006979]]peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; zinc ion binding [GO:0008270]>endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]FUNCTION: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. Isoform 2 is essential for hearing. {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:21185009}.Q8WTS6SETD7(Histone-lysine N-methyltransferase SETD7K-methyltransferases8SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.cellular response to DNA damage stimulus [GO:0006974]; chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; negative regulation of transferase activity [GO:0051348]; peptidyl-lysine dimethylation [GO:0018027]; peptidyl-lysine monomethylation [GO:0018026]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of histone H3-K9 methylation [GO:0051570]; response to ethanol [GO:0045471]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; histone-lysine N-methyltransferase activity [GO:0018024]; p53 binding [GO:0002039]; protein-lysine N-methyltransferase activity [GO:0016279]Ichromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. {ECO:0000269|PubMed:12540855, ECO:0000269|PubMed:12588998, ECO:0000269|PubMed:15099517, ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16141209, ECO:0000269|PubMed:17108971}.Q13418ILKIntegrin-linked protein kinaseSUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, myofibril, sarcomere.bbranching involved in ureteric bud morphogenesis [GO:0001658]; cell aging [GO:0007569]; cell cycle arrest [GO:0007050]; cell junction assembly [GO:0034329]; cell-matrix adhesion [GO:0007160]; cell proliferation [GO:0008283]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; extracellular fibril organization [GO:0043206]; fibroblast migration [GO:0010761]; integrin-mediated signaling pathway [GO:0007229]; myelin assembly [GO:0032288]; myelination in peripheral nervous system [GO:0022011]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of neural precursor cell proliferation [GO:2000178]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of smooth muscle cell proliferation [GO:0048662]; nerve development [GO:0021675]; neuron projection morphogenesis [GO:0048812]; outflow tract morphogenesis [GO:0003151]; peptidyl-serine phosphorylation [GO:0018105]; platelet aggregation [GO:0070527]; positive regulation of axon extension [GO:0045773]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of transcription, DNA-templated [GO:0045893]; protein heterooligomerization [GO:0051291]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; substrate adhesion-dependent cell spreading [GO:0034446]ATP binding [GO:0005524]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; signal transducer activity [GO:0004871]cell-cell junction [GO:0005911]; cell junction [GO:0030054]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; extracellular matrix [GO:0031012]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; sarcomere [GO:0030017]; stress fiber [GO:0001725]; terminal bouton [GO:0043195]0FUNCTION: Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.P32321DCTDDeoxycytidylate deaminaseEnucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide biosynthetic process [GO:0009165]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; pyrimidine nucleotide metabolic process [GO:0006220]; small molecule metabolic process [GO:0044281]CdCMP deaminase activity [GO:0004132]; zinc ion binding [GO:0008270]GFUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.Q99829CPNE1Copine-1cellular response to calcium ion [GO:0071277]; glycerophospholipid biosynthetic process [GO:0046474]; lipid metabolic process [GO:0006629]; negative regulation of DNA binding [GO:0043392]; negative regulation < of gene expression [GO:0010629]; negative regulation of NIK/NF-kappaB signaling [GO:1901223]; neuron projection extension [GO:1990138]; phospholipid metabolic process [GO:0006644]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; proteolysis [GO:0006508]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; small molecule metabolic process [GO:0044281]; vesicle-mediated transport [GO:0016192]calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; NF-kappaB binding [GO:0051059]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; transporter activity [GO:0005215]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]kFUNCTION: May function in membrane trafficking. Exhibits calcium-dependent phospholipid binding properties.Q9UNZ2NSF1CNSFL1 cofactor p47\SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Chromosome {ECO:0000250}. Note=Predominantly nuclear in interphase cells. Bound to the axial elements of sex chromosomes in pachytene spermatocytes. A small proportion of the protein is cytoplasmic, associated with Golgi stacks (By similarity). {ECO:0000250}. autophagosome assembly [GO:0000045]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; nuclear envelope reassembly [GO:0031468]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of catalytic activity [GO:0050790]}phospholipid binding [GO:0005543]; protein phosphatase type 1 regulator activity [GO:0008599]; ubiquitin binding [GO:0043130]chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi stack [GO:0005795]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; VCP-NSFL1C complex [GO:1990730]KFUNCTION: Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro). {ECO:0000250}.Q6ICG6K0930 Uncharacterized protein KIAA0930Q9UFW8CGBP1$CGG triplet repeat-binding protein 1;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9201980}.|negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]%double-stranded DNA binding [GO:0003690]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]FUNCTION: Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter. {ECO:0000269|PubMed:9201980}.P62158CALM CalmodulinSalivary secretion7SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.V activation of phospholipase C activity [GO:0007202]; blood coagulation [GO:0007596]; carbohydrate metabolic process [GO:0005975]; detection of calcium ion [GO:0005513]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; G-protein coupled receptor signaling pathway [GO:0007186]; innate immune response [GO:0045087]; inositol phosphate metabolic process [GO:0043647]; membrane organization [GO:0061024]; muscle contraction [GO:0006936]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; neurotrophin TRK receptor signaling pathway [GO:0048011]; nitric oxide metabolic process [GO:0046209]; phototransduction, visible light [GO:0007603]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of cyclic nucleotide metabolic process [GO:0030801]; positive regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051343]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of ryanodine-sensitive calcium-release channel activity [GO:0060316]; regulation of cardiac muscle contraction [GO:0055117]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cell communication by electrical coupling involved in cardiac conduction [GO:1901844]; regulation of cytokinesis [GO:0032465]; regulation of heart rate [GO:0002027]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; response to calcium ion [GO:0051592]; rhodopsin mediated signaling pathway [GO:0016056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; substantia nigra development [GO:0021762]; synaptic transmission [GO:0007268]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]calcium ion binding [GO:0005509]; ion channel binding [GO:0044325]; N-terminal myristoylation domain binding [GO:0031997]; phospholipase binding [GO:0043274]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542]; protein serine/threonine kinase activator activity [GO:0043539]; thioesterase binding [GO:0031996]; titin binding [GO:0031432]Ecentrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcomere [GO:0030017]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]; vesicle [GO:0031982]FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133}.Q13561DCTN2Dynactin subunit 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:8647893}. Membrane {ECO:0000269|PubMed:8647893}; Peripheral membrane protein {ECO:0000269|PubMed:8647893}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cell proliferation [GO:0008283]; G2/M transition of mitotic cell cycle [GO:0000086]; melanosome transport [GO:0032402]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic spindle organization [GO:0007052]; organelle organization [GO:0006996]; protein localization to centrosome [GO:0071539]:motor activity [GO:0003774]; spectrin binding [GO:0030507] centrosome [GO:< 0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; vesicle [GO:0031982]FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.Q8WU90ZC3HF-Zinc finger CCCH domain-containing protein 15SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15676025, ECO:0000269|PubMed:19819225}. Nucleus {ECO:0000250}. Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes.0cytokine-mediated signaling pathway [GO:0019221]@metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822].cytoplasm [GO:0005737]; nucleolus [GO:0005730]DFUNCTION: Protects DRG1 from proteolytic degradation. {ECO:0000250}.Q9Y6D6BIG1;Brefeldin A-inhibited guanine nucleotide-exchange protein 1 SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus. Nucleus, nucleolus. Nucleus matrix. Membrane. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment.endomembrane system organization [GO:0010256]; exocytosis [GO:0006887]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; neuron projection development [GO:0031175]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein glycosylation in Golgi [GO:0090284]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of wound healing [GO:0090303]; protein transport [GO:0015031]; regulation of ARF protein signal transduction [GO:0032012]; regulation of establishment of cell polarity [GO:2000114]ARF guanyl-nucleotide exchange factor activity [GO:0005086]; guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237]<cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802]>FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined. {ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15644318, ECO:0000269|PubMed:17227842, ECO:0000269|PubMed:20360857, ECO:0000269|PubMed:22084092}.Q8N668COMD1 COMM domain-containing protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21778237}. Cytoplasm {ECO:0000269|PubMed:21778237}. Endosome membrane {ECO:0000269|PubMed:18940794}. Cytoplasmic vesicle {ECO:0000269|PubMed:18940794}. Early endosome {ECO:0000269|PubMed:21483833, ECO:0000269|PubMed:25355947}. Recycling endosome {ECO:0000269|PubMed:21483833, ECO:0000269|PubMed:21741370}. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins.Dcopper ion homeostasis [GO:0055070]; Golgi to plasma membrane transport [GO:0006893]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of sodium ion transmembrane transport [GO:1902306]; plasma membrane to endosome transport [GO:0048227]; positive regulation of protein ubiquitination [GO:0031398]; protein transport [GO:0015031]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; transcription, DNA-templated [GO:0006351]copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein homodimerization activity [GO:0042803],Cul2-RING ubiquitin ligase complex [GO:0031462]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; recycling endosome [GO:0055037]3 FUNCTION: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2 (PubMed:21778237). Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity (PubMed:15799966, PubMed:17183367, PubMed:20048074). Involved in the regulation of membrane expression and ubiquitination of SLC12A2 (PubMed:23515529). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes (PubMed:14645214, PubMed:20237237, PubMed:21741370). Promotes CFTR cell surface expression through regulation of its ubiquitination (PubMed:21483833). Down-regulates SOD1 activity by interfering with its homodimerization (PubMed:20595380). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947). Can bind one copper ion per monomer (PubMed:17309234). May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:18940794). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1 (PubMed:20458141). {ECO:0000269|PubMed:14645214, ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:17183367, ECO:0000269|PubMed:17309234, ECO:0000269|PubMed:20048074, ECO:0000269|PubMed:20237237, ECO:0000269|PubMed:20458141, ECO:0000269|PubMed:20595380, ECO:0000269|PubMed:21483833, ECO:0000269|PubMed:21741370, ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:23515529, ECO:0000269|PubMed:25355947}.Q92572AP3S1AP-3 complex subunit sigma-1SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; insulin receptor signaling pathway [GO:0008286]; intracellular protein transport [GO:0006886]Lprotein transporter activity [GO:0008565]; transporter activity [GO:0005215]AP-3 adaptor complex [GO:0030123]; AP-type membrane coat adaptor complex [GO:0< 030119]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794]; transport vesicle [GO:0030133]O00203AP3B1AP-3 complex subunit beta-1@SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; blood coagulation [GO:0007596]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; positive regulation of NK T cell differentiation [GO:0051138]; protein targeting to lysosome [GO:0006622]TGTP-dependent protein binding [GO:0030742]; protein phosphatase binding [GO:0019903]AP-3 adaptor complex [GO:0030123]; clathrin-coated vesicle membrane [GO:0030665]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.Q9NRF9DPOE3 DNA polymerase epsilon subunit 3hDNA biosynthetic process [GO:0071897]; DNA replication [GO:0006260]; histone H3 acetylation [GO:0043966]]DNA-directed DNA polymerase activity [GO:0003887]; sequence-specific DNA binding [GO:0043565]~Ada2/Gcn5/Ada3 transcription activator complex [GO:0005671]; epsilon DNA polymerase complex [GO:0008622]; nucleus [GO:0005634]FUNCTION: Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1.Q9Y6G9DC1L1/Cytoplasmic dynein 1 light intermediate chain 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19229290}.cell division [GO:0051301]; microtubule-based movement [GO:0007018]; mitotic nuclear division [GO:0007067]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; transport [GO:0006810]; viral process [GO:0016032]cATP binding [GO:0005524]; microtubule motor activity [GO:0003777]; poly(A) RNA binding [GO:0044822] centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; plasma membrane [GO:0005886]; spindle pole [GO:0000922]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores. {ECO:0000269|PubMed:19229290}.Q9H9H4VP37B/Vacuolar protein sorting-associated protein 37BSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:15218037}; Peripheral membrane protein {ECO:0000269|PubMed:15218037}. Note=Recruited to the endosomal membrane in a VPS4A-dependent fashion.endosomal transport [GO:0016197]; intracellular transport of virus [GO:0075733]; membrane organization [GO:0061024]; positive regulation of viral budding via host ESCRT complex [GO:1903774]; positive regulation of viral release from host cell [GO:1902188]; protein transport [GO:0015031]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; midbody [GO:0030496]; plasma membrane [GO:0005886]FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15218037}.P41743KPCIProtein kinase C iota typeeSUBCELLULAR LOCATION: Cytoplasm. Membrane. Endosome. Nucleus. Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A.actin filament organization [GO:0007015]; bicellular tight junction assembly [GO:0070830]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; cellular response to insulin stimulus [GO:0032869]; cytoskeleton organization [GO:0007010]; establishment of apical/basal cell polarity [GO:0035089]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; eye photoreceptor cell development [GO:0042462]; Golgi vesicle budding [GO:0048194]; intracellular signal transduction [GO:0035556]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of glucose import [GO:0046326]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein phosphorylation [GO:0006468]; protein targeting to membrane [GO:0006612]; response to interleukin-1 [GO:0070555]; secretion [GO:0046903]; vesicle-mediated transport [GO:0016192]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phospholipid binding [GO:0005543]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; Schmidt-Lanterman incisure [GO:0043220]FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta pr< otein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. {ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326, ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752, ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248, ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978, ECO:0000269|PubMed:9346882}.A0AVT1UBA6+Ubiquitin-like modifier-activating enzyme 6jamygdala development [GO:0021764]; dendritic spine development [GO:0060996]; hippocampus development [GO:0021766]; learning [GO:0007612]; locomotory behavior [GO:0007626]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; ubiquitin-dependent protein catabolic process [GO:0006511]zATP binding [GO:0005524]; FAT10 activating enzyme activity [GO:0019780]; ubiquitin activating enzyme activity [GO:0004839]FUNCTION: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility. {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759, ECO:0000269|PubMed:17889673}.Q9NR45SIASSialic acid synthasecellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; lipopolysaccharide biosynthetic process [GO:0009103]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]N-acetylneuraminate synthase activity [GO:0050462]; N-acylneuraminate-9-phosphate synthase activity [GO:0047444]; N-acylneuraminate cytidylyltransferase activity [GO:0008781]FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.Q96EK7F120BLConstitutive coactivator of peroxisome proliferator-activated receptor gammacell differentiation [GO:0030154]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]FUNCTION: Functions as a transactivator of PPARG and ESR1. Functions in adipogenesis through PPARG activation (By similarity). {ECO:0000250}.Q13404UB2V1)Ubiquitin-conjugating enzyme E2 variant 1E2zSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076860, ECO:0000269|PubMed:9305758}. Note=Excluded from the nucleolus.cell differentiation [GO:0030154]; error-free postreplication DNA repair [GO:0042275]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription, DNA-templated [GO:0045893]; postreplication repair [GO:0006301]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; regulation of DNA repair [GO:0006282]; regulation of transcription, DNA-templated [GO:0006355]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein complex [GO:0043234]; UBC13-UEV1A complex [GO:0035370]; ubiquitin conjugating enzyme complex [GO:0031371]; ubiquitin ligase complex [GO:0000151]mFUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000269|PubMed:11057907, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:9305758, ECO:0000269|PubMed:9418904, ECO:0000269|PubMed:9580084, ECO:0000269|PubMed:9705497}.P52735VAV2'Guanine nucleotide exchange factor VAV2}angiogenesis [GO:0001525]; apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; lamellipodium assembly [GO:0030032]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; regulation of blood coagulation [GO:0030193]; regulation of cell size [GO:0008361]; regulation of gene expression [GO:0010468]; regulation of GTPase activity [GO:0043087]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth< factor receptor signaling pathway [GO:0048010]guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]2cytosol [GO:0005829]; plasma membrane [GO:0005886]2FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity). {ECO:0000250}.Q9GZQ3COMD5 COMM domain-containing protein 5FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Negatively regulates cell proliferation. Negatively regulates cell cycle G2/M phase transition probably by transactivating p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved in kidney proximal tubule morphogenesis (By similarity). Down-regulates activation of NF-kappa-B (PubMed:15799966). {ECO:0000250|UniProtKB:Q9ERR2, ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.Q9Y3R5DOP2Protein dopey-2cognition [GO:0050890]; endoplasmic reticulum organization [GO:0007029]; Golgi to endosome transport [GO:0006895]; multicellular organismal development [GO:0007275]; protein transport [GO:0015031]?extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]cFUNCTION: May be involved in protein traffic between late Golgi and early endosomes. {ECO:0000250}.Q5F1R6DJC21"DnaJ homolog subfamily C member 21 HSP40/DnaJ.FUNCTION: May act as a co-chaperone for HSP70.O95155UBE4B!Ubiquitin conjugation factor E4 BgSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES00}. Nucleus {ECO:0000250|UniProtKB:Q9ES00}.granzyme-mediated apoptotic signaling pathway [GO:0008626]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; response to UV [GO:0009411]kenzyme binding [GO:0019899]; ligase activity [GO:0016874]; ubiquitin-ubiquitin ligase activity [GO:0034450]Scytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]EFUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.P22059OSBP1Oxysterol-binding protein 1SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Note=When bound to oxysterols, translocates to the periphery of Golgi membranes.\lipid transport [GO:0006869]; positive regulation of growth of symbiont in host [GO:0044128]Loxysterol binding [GO:0008142]; protein domain specific binding [GO:0019904]cell junction [GO:0030054]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749). {ECO:0000269|PubMed:15746430, ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:18450749}.O43592XPOT Exportin-TSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm.Sintracellular protein transport [GO:0006886]; tRNA export from nucleus [GO:0006409]tRNA binding [GO:0000049]2FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:12138183, ECO:0000269|PubMed:9512417, ECO:0000269|PubMed:9660920}.P11441UBL4AUbiquitin-like protein 4AGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20676083}.cellular protein modification process [GO:0006464]; maintenance of unfolded protein involved in ERAD pathway [GO:1904378]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; transport [GO:0006810]Xchaperone binding [GO:0051087]; ubiquitin-like protein transferase activity [GO:0019787]tBAT3 complex [GO:0071818]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FFUNCTION: Component of the BAT3 complex, a multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. The complex acts by facilitating TA proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and transfers them to ASNA1/TRC40 for targeting. {ECO:0000269|PubMed:20676083}.O94822LTN1$E3 ubiquitin-protein ligase listerinkligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23685075, PubMed:25132172, PubMed:25578875). Ubiquitination leads to VCP/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity). {ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:23685075, ECO:0000269|PubMed:25132172, ECO:0000269|PubMed:25578875}.Q10567AP1B1AP-1 complex subunit beta-1SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.?antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of defense response to virus by virus [GO:0050690]; viral process [GO:0016032]qprotein kinase binding [GO:0019901]; protein transporter activity [GO:0008565]; transporter activity [GO:0005215]clathrin adaptor complex [GO:0030131]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; trans-Golgi network membrane [GO:0032588]PFUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.Q9ULT8HECD1"E3 ubiquitin-protein ligase HECTD1natural killer cell differentiation [GO:0001779]; negative regulation of protein localization to plasma membrane [GO:1903077]; neural tube closure [GO:0001843]; protein aut< oubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; spongiotrophoblast differentiation [GO:0060708]; trophoblast giant cell differentiation [GO:0060707]ligase activity [GO:0016874]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]:FUNCTION: Probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. May be required for development of the head mesenchyme and neural tube closure (By similarity). {ECO:0000250}.Q9NRY5F1142Protein FAM114A2&purine nucleotide binding [GO:0017076]Q9HBK9AS3MTArsenite methyltransferaselarsonoacetate metabolic process [GO:0018872]; methylation [GO:0032259]; toxin metabolic process [GO:0009404]arsenite methyltransferase activity [GO:0030791]; methylarsonite methyltransferase activity [GO:0030792]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH (By similarity). {ECO:0000250}.Q05397FAK1Focal adhesion kinase 1=SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=Constituent of focal adhesions. Detected at microtubules.- angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell motility [GO:0048870]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; central nervous system neuron axonogenesis [GO:0021955]; cytoskeleton organization [GO:0007010]; embryo development [GO:0009790]; endothelial cell migration [GO:0043542]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; establishment of cell polarity [GO:0030010]; establishment of nucleus localization [GO:0040023]; extracellular matrix organization [GO:0030198]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; growth hormone receptor signaling pathway [GO:0060396]; heart morphogenesis [GO:0003007]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of organ growth [GO:0046621]; negative regulation of synapse assembly [GO:0051964]; netrin-activated signaling pathway [GO:0038007]; neuron migration [GO:0001764]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; placenta development [GO:0001890]; platelet activation [GO:0030168]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; programmed cell death [GO:0012501]; protein autophosphorylation [GO:0046777]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cell proliferation [GO:0042127]; regulation of cell shape [GO:0008360]; regulation of cytoskeleton organization [GO:0051493]; regulation of endothelial cell migration [GO:0010594]; regulation of epithelial cell migration [GO:0010632]; regulation of focal adhesion assembly [GO:0051893]; regulation of GTPase activity [GO:0043087]; regulation of osteoblast differentiation [GO:0045667]; regulation of protein phosphorylation [GO:0001932]; regulation of substrate adhesion-dependent cell spreading [GO:1900024]; signal complex assembly [GO:0007172]; small GTPase mediated signal transduction [GO:0007264]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vasculogenesis [GO:0001570]}actin binding [GO:0003779]; ATP binding [GO:0005524]; JUN kinase binding [GO:0008432]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; SH2 domain binding [GO:0042169]; signal transducer activity [GO:0004871]apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; stress fiber [GO:0001725] FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to < enhance serum response factor (SRF)-dependent gene transcription. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11980671, ECO:0000269|PubMed:15166238, ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:15895076, ECO:0000269|PubMed:16919435, ECO:0000269|PubMed:16927379, ECO:0000269|PubMed:17395594, ECO:0000269|PubMed:17431114, ECO:0000269|PubMed:17968709, ECO:0000269|PubMed:18006843, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:18256281, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:18677107, ECO:0000269|PubMed:19138410, ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19224453, ECO:0000269|PubMed:20332118, ECO:0000269|PubMed:20495381, ECO:0000269|PubMed:21454698}.Q9H2J4PDCL3Phosducin-like protein 3>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15371430}.angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; protein folding [GO:0006457]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; viral process [GO:0016032]8protein binding involved in protein folding [GO:0044183]wFUNCTION: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, controlling its abundance and inhibiting its ubiquitination and degradation. Modulates the activation of caspases during apoptosis. Is a substrate for Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV) IAP-mediated ubiquitination. {ECO:0000269|PubMed:15371430, ECO:0000269|PubMed:23792958}.Q9NP77SSU72?RNA polymerase II subunit A C-terminal domain phosphatase SSU72LSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly in the cytosol.hdephosphorylation of RNA polymerase II C-terminal domain [GO:0070940]; mRNA polyadenylation [GO:0006378]%CTD phosphatase activity [GO:0008420]CFUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK. {ECO:0000269|PubMed:15659578, ECO:0000269|PubMed:20861839, ECO:0000269|PubMed:23070812}.Q5EBL4RIPL1RILP-like protein 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14668488}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, cilium {ECO:0000250}.epithelial cell morphogenesis [GO:0003382]; intracellular protein transport [GO:0006886]; protein transport from ciliary membrane to plasma membrane [GO:1903445]; regulation of neuron death [GO:1901214]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; primary cilium [GO:0072372]FUNCTION: Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH (By similarity). Does not regulate lysosomal morphology and distribution. {ECO:0000250}.P49841GSK3BGlycogen synthase kinase-3 betaSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.c axon guidance [GO:0007411]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in positive regulation of apoptotic process [GO:0044337]; cell migration [GO:0016477]; cellular response to heat [GO:0034605]; cellular response to interleukin-3 [GO:0036016]; circadian rhythm [GO:0007623]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial to mesenchymal transition [GO:0001837]; ER overload response [GO:0006983]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fat cell differentiation [GO:0045444]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glycogen metabolic process [GO:0005977]; hippocampus development [GO:0021766]; hypermethylation of CpG island [GO:0044027]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; myoblast fusion [GO:0007520]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of glycogen (starch) synthase activity [GO:2000466]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulation of neuron maturation [GO:0014043]; negative regulation of neuron projection development [GO:0010977]; negative regulation of NFAT protein import into nucleus [GO:0051534]; negative regulation of protein binding [GO:0032091]; negative regulation of protein complex assembly [GO:0031333]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of type B pancreatic cell development [GO:2000077]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ morphogenesis [GO:0009887]; peptidyl-serine phosphorylation [GO:0018105]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of axon extension [GO:0045773]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of GTPase activity [GO:0043547]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein binding [GO:0032092]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein complex assembly [GO:0031334]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of stem cell differentiation [GO:2000738]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein autophosphorylation [GO:0046777]; protein export from nucleus [GO:0006611]; protein localization to microtubule [GO:0035372]; protein phosphorylation [GO:0006468]; re-entry into mitotic cell cycle [GO:0000320]; regulation of cellular response to heat [GO:1900034]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of microtubule-based process [GO:0032886]; superior temporal gyrus development [GO:0071109]ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; kinase activity [GO:0016301]; NF-kappaB binding [GO:0051059]; p53 binding [GO:0002039]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II transcription factor binding [GO:0001085]; tau-protein kinase activity [GO:0050321]; ubiquitin protein ligase binding [GO:0031625]beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:0030529]FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2),< EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). {ECO:0000269|PubMed:11430833, ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:18348280, ECO:0000269|PubMed:1846781, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:22514281, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:8397507, ECO:0000269|PubMed:9072970, ECO:0000269|PubMed:9819408}.Q9H3S7PTN231Tyrosine-protein phosphatase non-receptor type 23SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic vesicle. Endosome. Cytoplasm, cytoskeleton, cilium basal body. Early endosome.cilium morphogenesis [GO:0060271]; negative regulation of epithelial cell migration [GO:0010633]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of adherens junction organization [GO:1903393]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of homophilic cell adhesion [GO:1903387]; protein transport [GO:0015031]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]Wprotein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis. {ECO:0000269|PubMed:18434552, ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:21757351}.O95630STABPSTAM-binding protein`SUBCELLULAR LOCATION: Nucleus. Membrane; Peripheral membrane protein. Cytoplasm. Early endosome.nJAK-STAT cascade [GO:0007259]; mitotic cytokinesis [GO:0000281]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of cell proliferation [GO:0008284]; protein deubiquitination [GO:0016579]metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; protein domain specific binding [GO:0019904]; ubiquitin-specific protease activity [GO:0004843]cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]pFUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways. {ECO:0000250, ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583, ECO:0000269|PubMed:23542699}.O14617AP3D1AP-3 complex subunit delta-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.xanterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; endosome to melanosome transport [GO:0035646]; eye pigment biosynthetic process [GO:0006726]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; positive regulation of NK T cell differentiation [GO:0051138]; protein localization to membrane [GO:0072657]; protein localization to organelle [GO:0033365]; regulation of sequestering of zinc ion [GO:0061088]; synaptic vesicle membrane organization [GO:0048499]endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane coat [GO:0030117]; nucleoplasm [GO:0005654]; terminal bouton [GO:0043195]Q04323UBXN1UBX domain-containing protein 1negative regulation of ERAD pathway [GO:1904293]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein K48-linked deubiquitination [GO:1903094]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of ubiquitin-specific protease activity [GO:2000157]; proteasome-mediated ubiquitin-dependent protein< catabolic process [GO:0043161]ATPase binding [GO:0051117]; K48-linked polyubiquitin binding [GO:0036435]; K6-linked polyubiquitin binding [GO:0071796]; polyubiquitin binding [GO:0031593]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1-BARD1 heterodimer, and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol.Q9Y450HBS1LHBS1-like protein:signal transduction [GO:0007165]; translation [GO:0006412]kGTPase activity [GO:0003924]; GTP binding [GO:0005525]; translation elongation factor activity [GO:0003746]P00492HPRT.Hypoxanthine-guanine phosphoribosyltransferase-adenine salvage [GO:0006168]; central nervous system neuron development [GO:0021954]; cerebral cortex neuron differentiation [GO:0021895]; cytolysis [GO:0019835]; dendrite morphogenesis [GO:0048813]; dopamine metabolic process [GO:0042417]; GMP catabolic process [GO:0046038]; GMP salvage [GO:0032263]; grooming behavior [GO:0007625]; guanine salvage [GO:0006178]; hypoxanthine metabolic process [GO:0046100]; hypoxanthine salvage [GO:0043103]; IMP metabolic process [GO:0046040]; IMP salvage [GO:0032264]; locomotory behavior [GO:0007626]; lymphocyte proliferation [GO:0046651]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of dopamine metabolic process [GO:0045964]; protein homotetramerization [GO:0051289]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]; purine ribonucleoside salvage [GO:0006166]; response to amphetamine [GO:0001975]; small molecule metabolic process [GO:0044281]; striatum development [GO:0021756]guanine phosphoribosyltransferase activity [GO:0052657]; hypoxanthine phosphoribosyltransferase activity [GO:0004422]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.A1X283SPD2B'SH3 and PX domain-containing protein 2BSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. {ECO:0000250}.adipose tissue development [GO:0060612]; bone development [GO:0060348]; cell differentiation [GO:0030154]; extracellular matrix disassembly [GO:0022617]; eye development [GO:0001654]; heart development [GO:0007507]; podosome assembly [GO:0071800]; positive regulation of fat cell differentiation [GO:0045600]; protein localization to membrane [GO:0072657]; skeletal system development [GO:0001501]; superoxide metabolic process [GO:0006801]phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; SH2 domain binding [GO:0042169]gcell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; podosome [GO:0002102]FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation (By similarity). {ECO:0000250}.Q8TAT6NPL4.Nuclear protein localization protein 4 homolog Protein degradationSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with the endoplasmic reticulum and nuclear. {ECO:0000250}.KDNA repair [GO:0006281]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; error-free translesion synthesis [GO:0070987]; Golgi organization [GO:0007030]; retrograde protein transport, ER to cytosol [GO:0030970]; translesion synthesis [GO:0019985]; ubiquitin-dependent protein catabolic process [GO:0006511]lubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; UFD1-NPL4 complex [GO:0036501]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]FUNCTION: The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). {ECO:0000250}.O95373IPO7 Importin-7innate immune response [GO:0045087]; protein import into nucleus [GO:0006606]; regulation of catalytic activity [GO:0050790]; signal transduction [GO:0007165]; viral process [GO:0016032]jGTPase regulator activity [GO:0030695]; Ran GTPase binding [GO:0008536]; transporter activity [GO:0005215]bcytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]FUNCTION: Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In vitro, mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:12853482, ECO:0000269|PubMed:9687515}.Q15436SC23A Protein transport protein Sec23ASUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=In the ribosome-free transitional face of the ER and associated vesicles.Yantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; ER < to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]; vesicle-mediated transport [GO:0016192]:COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; smooth endoplasmic reticulum membrane [GO:0030868]2FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.O95486SC24A Protein transport protein Sec24ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; positive regulation of cholesterol homeostasis [GO:2000189]; positive regulation of protein secretion [GO:0050714]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045714]; small molecule metabolic process [GO:0044281]COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]Q9NZN3EHD3EH domain-containing protein 3SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:17233914}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:17233914}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000269|PubMed:25686250}.blood coagulation [GO:0007596]; endocytic recycling [GO:0032456]; protein homooligomerization [GO:0051260]; protein targeting to plasma membrane [GO:0072661]; regulation of cardiac muscle cell membrane potential [GO:0086036]wATP binding [GO:0005524]; calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; nucleic acid binding [GO:0003676]cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (PubMed:25686250). Plays a role in endocytic transport (PubMed:16251358, PubMed:17233914). Also plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis (PubMed:25686250). {ECO:0000269|PubMed:16251358, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:25686250}.P12429ANXA3 Annexin A3defense response to bacterium [GO:0042742]; hippocampus development [GO:0021766]; neutrophil degranulation [GO:0043312]; organ regeneration [GO:0031100]; phagocytosis [GO:0006909]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA metabolic process [GO:0051054]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; response to glucocorticoid [GO:0051384]; response to growth factor [GO:0070848]calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; phospholipase A2 inhibitor activity [GO:0019834]axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; specific granule [GO:0042581]FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate.O95379TFIP8-Tumor necrosis factor alpha-induced protein 8>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14724590}.defense response to Gram-positive bacterium [GO:0050830]; interleukin-1 beta production [GO:0032611]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]Ycysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]sFUNCTION: Acts as a negative mediator of apoptosis and may play a role in tumor progression. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation. {ECO:0000269|PubMed:10644768, ECO:0000269|PubMed:11346652, ECO:0000269|PubMed:14724590}.O00743PPP68Serine/threonine-protein phosphatase 6 catalytic subunit[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:17568194}.ZG1/S transition of mitotic cell cycle [GO:0000082]; protein dephosphorylation [GO:0006470]FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7. {ECO:0000269|PubMed:10227379, ECO:0000269|PubMed:17079228, ECO:0000269|PubMed:17568194, ECO:0000269|PubMed:9013334}.Q86X27RGPS28Ras-specific guanine nucleotide-releasing factor RalGPS2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Associates with membranes through the PH domain. {ECO:0000250}.rregulation of Ral protein signal transduction [GO:0032485]; small GTPase mediated signal transduction [GO:0007264]7guanyl-nucleotide exchange factor activity [GO:0005085]FUNCTION: Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion (By similarity). {ECO:0000250}.P34932HSP74Heat shock 70 kDa protein 4HSP110chaperone-mediated protein complex assembly [GO:0051131]; protein import into mitochondrial outer membrane [GO:0045040]; response to unfolded protein [GO:0006986]Q7L5D6GET4%Golgi to ER traffic protein 4 homologcytoplasmic sequestering of protein [GO:0051220]; maintenance of unfolded protein involved in ERAD pathway [GO:1904378]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; transport [GO:0006810]GBAT3 complex [GO:0071818]; cytoplasm [GO:0005737]; cytosol [GO:0005829]Q9C035TRIM5%Tripartite motif-containing protein 5SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:20357094}. Note=Closely associates with proteasomal subunits in cytoplasmic bodies (By similarity). Colocalizes with SQSTM1 in cytoplasmic bodies. {ECO:0000250}.activation of innate immune response [GO:0002218]; cytokine-mediated signaling pathway [GO:00< 19221]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral release from host cell [GO:1902187]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein K63-linked ubiquitination [GO:0070534]; protein trimerization [GO:0070206]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; viral process [GO:0016032]identical protein binding [GO:0042802]; ligase activity [GO:0016874]; protein homodimerization activity [GO:0042803]; signaling pattern recognition receptor activity [GO:0008329]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270][cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]FUNCTION: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV) and equine infectious anemia virus (EIAV). {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:18312418, ECO:0000269|PubMed:21035162, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21632761, ECO:0000269|PubMed:22291694}.Q9UG63ABCF2*ATP-binding cassette sub-family F member 2transport [GO:0006810]YATPase activity [GO:0016887]; ATP binding [GO:0005524]; transporter activity [GO:0005215]wATP-binding cassette (ABC) transporter complex [GO:0043190]; membrane [GO:0016020]; mitochondrial envelope [GO:0005740]Q9UK97FBX9F-box only protein 9>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23263282}.fat cell differentiation [GO:0045444]; innate immune response [GO:0045087]; protein ubiquitination [GO:0016567]; regulation of TOR signaling [GO:0032006]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]3ubiquitin-protein transferase activity [GO:0004842]hcytoplasm [GO:0005737]; SCF ubiquitin ligase complex [GO:0019005]; ubiquitin ligase complex [GO:0000151]FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, the SCF(FBXO9) does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1. {ECO:0000269|PubMed:23263282}.Q9UN37VPS4A.Vacuolar protein sorting-associated protein 4ASUBCELLULAR LOCATION: Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Midbody. Note=Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody (PubMed:24814515). Localized in two distinct rings on either side of the Fleming body. {ECO:0000269|PubMed:24814515}. abscission [GO:0009838]; cell division [GO:0051301]; cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; endosomal vesicle fusion [GO:0034058]; intracellular cholesterol transport [GO:0032367]; membrane budding [GO:0006900]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; negative regulation of cytokinesis [GO:0032466]; nucleus organization [GO:0006997]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of viral budding via host ESCRT complex [GO:1903774]; positive regulation of viral life cycle [GO:1903902]; positive regulation of viral release from host cell [GO:1902188]; protein transport [GO:0015031]; regulation of protein localization [GO:0032880]; regulation of protein localization to plasma membrane [GO:1903076]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; vacuole organization [GO:0007033]; vesicle-mediated transport [GO:0016192]; vesicle uncoating [GO:0072319]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral release from host cell [GO:0019076]ATPase activity [GO:0016887]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; protein C-terminus binding [GO:0008022]; protein domain specific binding [GO:0019904]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Flemming body [GO:0090543]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosome [GO:0005764]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle pole [GO:0000922]; vacuolar membrane [GO:0005774]FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission (PubMed:24814515). {ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:11595185, ECO:0000269|PubMed:15075231, ECO:0000269|PubMed:24814515}.P29401TKT Transketolasexcarbohydrate metabolic process [GO:0005975]; energy reserve metabolic process [GO:0006112]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]; regulation of growth [GO:0040008]; small molecule metabolic process [GO:0044281]; xylulose biosynthetic process [GO:0005999]cofactor binding [GO:0048037]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; transketolase activity [GO:0004802]< cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisome [GO:0005777]; vesicle [GO:0031982]FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.Q9NXR7BREBRCA1-A complex subunit BREIapoptotic process [GO:0006915]; cellular response to DNA damage stimulus [GO:0006974]; chromatin modification [GO:0016568]; double-strand break repair [GO:0006302]; G2 DNA damage checkpoint [GO:0031572]; positive regulation of DNA repair [GO:0045739]; response to ionizing radiation [GO:0010212]; signal transduction [GO:0007165]peroxisome targeting sequence binding [GO:0000268]; polyubiquitin binding [GO:0031593]; tumor necrosis factor receptor binding [GO:0005164]BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]FUNCTION: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins. May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect. {ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:15465831, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}.Q9Y217MTMR6Myotubularin-related protein 6ESUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:16787938}.Upeptidyl-tyrosine dephosphorylation [GO:0035335]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; potassium ion transmembrane transport [GO:0071805]; protein dephosphorylation [GO:0006470]; small molecule metabolic process [GO:0044281]calcium-activated potassium channel activity [GO:0015269]; phosphatidylinositol phosphate phosphatase activity [GO:0052866]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]Kcytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]hFUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4+ T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3 phosphatase. Negatively regulates proliferation of reactivated CD4+ T-cells. {ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:16847315}.P82979SARNP'SAP domain-containing ribonucleoprotein/SUBCELLULAR LOCATION: Nucleus. Nucleus speckle.mRNA export from nucleus [GO:0006406]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; transcription, DNA-templated [GO:0006351]intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription export complex [GO:0000346]FFUNCTION: Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:15338056, ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015}.Q15369ELOC/Transcription elongation factor B polypeptide 1cellular response to hypoxia [GO:0071456]; gene expression [GO:0010467]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of viral transcription [GO:0050434]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Lcytosol [GO:0005829]; elongin complex [GO:0070449]; nucleoplasm [GO:0005654]TFUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). {ECO:0000269|PubMed:15590694}.; FUNCTION: The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. {ECO:0000269|PubMed:15590694}.Q8TD19NEK9$Serine/threonine-protein kinase Nek9eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14660563}. Nucleus {ECO:0000269|PubMed:14660563}.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; protein phosphorylation [GO:0006468]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]LFUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively. {ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:19941817}.Q9Y6E2BZW27Basic leucine zipper and W2 domain-containing protein 2Jcell differentiation [GO:0030154]; nervous system development [GO:0007399]EFUNCTION: May be involved in neuronal differentiation. {ECO:0000250}.Q9Y5X1SNX9Sorting nexin-9 SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi < network. Cell projection, ruffle. Cytoplasm. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation. Colocalizes with the actin cytoskeleton at the cell membrane.hcleavage furrow formation [GO:0036089]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; intracellular protein transport [GO:0006886]; lipid tube assembly [GO:0060988]; membrane tubulation [GO:0097320]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0007067]; positive regulation of GTPase activity [GO:0043547]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein oligomerization [GO:0032461]; receptor-mediated endocytosis [GO:0006898]; vesicle organization [GO:0016050]1-phosphatidylinositol binding [GO:0005545]; Arp2/3 complex binding [GO:0071933]; phosphatidylinositol binding [GO:0035091]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]sclathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle membrane [GO:0030659]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; trans-Golgi network [GO:0005802]~FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate. {ECO:0000269|PubMed:11799118, ECO:0000269|PubMed:12952949, ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:17609109, ECO:0000269|PubMed:17948057, ECO:0000269|PubMed:18388313, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.P54578UBP14(Ubiquitin carboxyl-terminal hydrolase 14DUBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19106094}. Cell membrane {ECO:0000269|PubMed:19106094}; Peripheral membrane protein {ECO:0000269|PubMed:19106094}.negative regulation of endopeptidase activity [GO:0010951]; negative regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903070]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of chemotaxis [GO:0050920]; regulation of proteasomal protein catabolic process [GO:0061136]; synaptic transmission [GO:0007268]cysteine-type endopeptidase activity [GO:0004197]; endopeptidase inhibitor activity [GO:0004866]; proteasome binding [GO:0070628]; tRNA guanylyltransferase activity [GO:0008193]; ubiquitin-specific protease activity [GO:0004843]cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]; synapse [GO:0045202]:FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). {ECO:0000269|PubMed:18162577, ECO:0000269|PubMed:19106094, ECO:0000269|PubMed:19135427}.Q9H3U1UN45AProtein unc-45 homolog ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16478993}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16478993}. Nucleus {ECO:0000269|PubMed:16478993}. Note=Predominant in the perinuclear region. Little protein in the nucleus.ycell differentiation [GO:0030154]; chaperone-mediated protein folding [GO:0061077]; muscle organ development [GO:0007517]|cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity). {ECO:0000250, ECO:0000305}.Q9ULA0DNPEPAspartyl aminopeptidase=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9632644}.&peptide metabolic process [GO:0006518]kaminopeptidase activity [GO:0004177]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]hblood microparticle [GO:0072562]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. {ECO:0000269|PubMed:9632644}.O60524NEMF#Nuclear export mediator factor NEMFnuclear export [GO:0051168].FUNCTION: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. NEMF is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. NEMF is important for the stable association of LTN1 to the complex (PubMed:25578875). May indirectly play a role in nuclear export (PubMed:16103875). {ECO:0000269|PubMed:16103875, ECO:0000269|PubMed:25578875}.Q96T59CDRTF-CMT1A duplicated region transcript 15 proteinO14530TXND9'Thioredoxin domain-containing protein 9#cell redox homeostasis [GO:0045454][centrosome [GO:0005813]; cytoplasm [GO:0005737]; midbody [GO:0030496]; nucleus [GO:0005634]FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin. {ECO:0000269|PubMed:16415341}.P52630STAT22Signal transducer and activator of transcription 2STAT/activating transcriptionoSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus upon activation by IFN-alpha/beta.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; JAK-STAT cascade [GO:0007259]; positive regulation of defense response to virus by host [GO:0002230]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; transcription, DNA-templated [GO:0006351]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]DNA binding [GO:0003677]; identical protein binding [GO:0042802]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity< [GO:0004871]dcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]dFUNCTION: Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. {ECO:0000269|PubMed:9020188}.Q9UGV2NDRG3 Protein NDRG3cell differentiation [GO:0030154]; negative regulation of cell growth [GO:0030308]; signal transduction [GO:0007165]; spermatogenesis [GO:0007283]Q9P270SLAI2 SLAIN motif-containing protein 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with microtubules. Detected at the plus end of growing microtubules.cytoplasmic microtubule organization [GO:0031122]; microtubule nucleation [GO:0007020]; positive regulation of microtubule polymerization [GO:0031116]centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase. {ECO:0000269|PubMed:21646404}.O60271JIP41C-Jun-amino-terminal kinase-interacting protein 4VSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Note=Perinuclear distribution in response to stress signals such as UV radiation.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix.activation of JUN kinase activity [GO:0007257]; muscle cell differentiation [GO:0042692]; negative regulation of protein homodimerization activity [GO:0090074]; positive regulation of cell migration [GO:0030335]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of neuron differentiation [GO:0045666]; protein homooligomerization [GO:0051260]; retrograde transport, endosome to Golgi [GO:0042147]; spermatogenesis [GO:0007283]; striated muscle cell differentiation [GO:0051146]JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; MAP-kinase scaffold activity [GO:0005078]; receptor signaling complex scaffold activity [GO:0030159]acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]AFUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Isoform 5 may play a role in spermatozoa-egg-interaction. {ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15693750}.P07384CAN1Calpain-1 catalytic subunitHSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:8769305}. Cell membrane {ECO:0000269|PubMed:8769305}. Note=Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719). {ECO:0000269|PubMed:21531719}.$extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; mammary gland involution [GO:0060056]; positive regulation of cell proliferation [GO:0008284]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; receptor catabolic process [GO:0032801]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.O60502OGAProtein O-GlcNAcaseSUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000269|PubMed:11341771}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771, ECO:0000269|PubMed:11788610}.aging [GO:0007568]; dATP metabolic process [GO:0046060]; glycoprotein catabolic process [GO:0006516]; N-acetylglucosamine metabolic process [GO:0006044]; necrotic cell death [GO:0070265]; negative regulation of cardiac muscle adaptation [GO:0010616]; negative regulation of protein glycosylation [GO:0060051]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of cell killing [GO:0031343]; positive regulation of DNA metabolic process [GO:0051054]; positive regulation of glucose import [GO:0046326]; positive regulation of growth hormone secretion [GO:0060124]; positive regulation of insulin secretion [GO:0032024]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of protein complex disassembly [GO:0043243]; positive regulation of proteolysis [GO:0045862]; protein deglycosylation [GO:0006517]; protein targeting to membrane [GO:0006612]; response to steroid hormone [GO:0048545]beta-N-acetylglucosaminidase activity [GO:0016231]; histone acetyltransferase activity [GO:0004402]; hyalurononglucosaminidase activity [GO:0004415]]cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714). {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600, ECO:0000269|PubMed:24088714}.; FUNCTION: Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1. {ECO:0000269|PubMed:20673219}.P45984MK09"Mitogen-activated protein kinase 9eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675674}. Nucleus {ECO:0000269|PubMed:19675674}. cellular response to growth factor stimulus [GO:0071363]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to UV [GO:0034644]; central nervous system development [GO:0007417]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; neuron projection development [GO:0031175]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell morphogenesis involved in differentiation [GO:0010770]; positive regulation of chemokine production [GO:0032722]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of prostaglandin secretion [GO:0032308]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription, DNA-templated [GO:0045893]; protein phosphorylation [GO:0006468]; protein targeting to mitochondrion [GO:0006626]; regu< lation of circadian rhythm [GO:0042752]; regulation of JNK cascade [GO:0046328]; regulation of protein ubiquitination [GO:0031396]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; release of cytochrome c from mitochondria [GO:0001836]; response to amine [GO:0014075]; response to cadmium ion [GO:0046686]; response to drug [GO:0042493]; response to mechanical stimulus [GO:0009612]; response to stress [GO:0006950]; response to toxic substance [GO:0009636]; rhythmic process [GO:0048511]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; JUN kinase activity [GO:0004705]; transcription factor binding [GO:0008134]Jcytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]zFUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:22441692}.; FUNCTION: MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.P22681CBLE3 ubiquitin-protein ligase CBLpSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane.}cell surface receptor signaling pathway [GO:0007166]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein ubiquitination [GO:0016567]; regulation of transcription, DNA-templated [GO:0006355]; transforming growth factor beta receptor signaling pathway [GO:0007179]|calcium ion binding [GO:0005509]; ephrin receptor binding [GO:0046875]; ligase activity [GO:0016874]; sequence-specific DNA binding transcription factor activity [GO:0003700]; SH3 domain binding [GO:0017124]; signal transducer activity [GO:0004871]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; flotillin complex [GO:0016600]; nucleus [GO:0005634]; plasma membrane [GO:0005886]:FUNCTION: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. {ECO:0000269|PubMed:10514377, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:21596750}.Q9H1Y0ATG5Autophagy protein 5ySUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Note=Colocalizes with nonmuscle actin. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed (By similarity). Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}. apoptotic process [GO:0006915]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; blood vessel remodeling [GO:0001974]; cellular response to nitrogen starvation [GO:0006995]; C-terminal protein lipidation [GO:0006501]; heart contraction [GO:0060047]; innate immune response [GO:0045087]; mitochondrion degradation [GO:0000422]; negative regulation of apoptotic process [GO:0043066]; negative regulation of histone H4-K16 acetylation [GO:2000619]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of type I interferon production [GO:0032480]; negative stranded viral RNA replication [GO:0039689]; nucleophagy [GO:0044804]; otolith development [GO:0048840]; positive regulation of mitochondrion degradation [GO:1903599]; positive regulation of mucus secretion [GO:0070257]; post-translational protein modification [GO:0043687]; regulation of cilium assembly [GO:1902017]; regulation of cytokine secretion involved in immune response [GO:0002739]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; response to drug [GO:0042493]; response to fungus [GO:0009620]; vasodilation [GO:0042311]; ventricular cardiac muscle cell development [GO:0055015]Atg12-Atg5-Atg16 complex [GO:0034274]; autophagosome [GO:0005776]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; ER-mitochondrion membrane contact site [GO:0044233]; membrane [GO:0016020]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzym< e which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. The ATG12-ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.; FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD.Q9P260K14687LisH domain and HEAT repeat-containing protein KIAA1468Q6Y7W6PERQ29PERQ amino acid-rich with GYF domain-containing protein 2Badult locomotory behavior [GO:0008344]; cellular protein metabolic process [GO:0044267]; feeding behavior [GO:0007631]; homeostasis of number of cells within a tissue [GO:0048873]; insulin-like growth factor receptor signaling pathway [GO:0048009]; mitotic G1 DNA damage checkpoint [GO:0031571]; multicellular organism growth [GO:0035264]; musculoskeletal movement [GO:0050881]; negative regulation of translation [GO:0017148]; neuromuscular process controlling balance [GO:0050885]; post-embryonic development [GO:0009791]; spinal cord motor neuron differentiation [GO:0021522]FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors. {ECO:0000269|PubMed:12771153}.Q92974ARHG2(Rho guanine nucleotide exchange factor 2SUBCELLULAR LOCATION: Cytoplasm. Cell junction, tight junction. Golgi apparatus. Cytoplasm, cytoskeleton, spindle. Cell projection, ruffle membrane. Cytoplasmic vesicle. Note=Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization. Recruited into membrane ruffles induced by S.flexneri at tight junctions of polarized epithelial cells. Colocalized with NOD2 and RIPK2 in vesicles and with the cytoskeleton.Uactin filament organization [GO:0007015]; apoptotic signaling pathway [GO:0097190]; cell division [GO:0051301]; cell morphogenesis [GO:0000902]; cellular hyperosmotic response [GO:0071474]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to tumor necrosis factor [GO:0071356]; establishment of mitotic spindle orientation [GO:0000132]; innate immune response [GO:0045087]; intracellular protein transport [GO:0006886]; mitotic nuclear division [GO:0007067]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902219]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of necroptotic process [GO:0060546]; negative regulation of neurogenesis [GO:0050768]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell proliferation [GO:0042127]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]&microtubule binding [GO:0008017]; Rac GTPase binding [GO:0048365]; Rac guanyl-nucleotide exchange factor activity [GO:0030676]; Rho GTPase binding [GO:0017048]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]; neuronal postsynaptic density [GO:0097481]; protein complex [GO:0043234]; ruffle membrane [GO:0032587]; spindle [GO:0005819]; vesicle [GO:0031982]FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. {ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:9857026}.Q8WVY7UBCP12Ubiquitin-like domain-containing CTD phosphatase 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15883030, ECO:0000269|PubMed:21949367}. Note=Colocalizes with nuclear proteasomes.&protein dephosphorylation [GO:0006470]:protein serine/threonine phosphatase activity [GO:0004722],nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome. {ECO:0000269|PubMed:21949367}.O75312ZPR1Zinc finger protein ZPR1RSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR< in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. {ECO:0000250}.apoptotic process involved in development [GO:1902742]; axon development [GO:0061564]; Cajal body organization [GO:0030576]; cell proliferation [GO:0008283]; cellular response to epidermal growth factor stimulus [GO:0071364]; DNA endoreduplication [GO:0042023]; inner cell mass cell proliferation [GO:0001833]; microtubule cytoskeleton organization [GO:0000226]; mRNA processing [GO:0006397]; negative regulation of motor neuron apoptotic process [GO:2000672]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of RNA splicing [GO:0033120]; positive regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0071931]; pre-mRNA catabolic process [GO:1990261]; regulation of myelination [GO:0031641]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]; spinal cord development [GO:0021510]; trophectodermal cell proliferation [GO:0001834]Qtranslation initiation factor binding [GO:0031369]; zinc ion binding [GO:0008270]Laxon [GO:0030424]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; Gemini of coiled bodies [GO:0097504]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; SMN complex [GO:0032797]JFUNCTION: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death. {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:17068332, ECO:0000269|PubMed:22422766}.Q9H8M7F188AProtein FAM188A<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12054670}.apoptotic process [GO:0006915]7nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]FUNCTION: May have pro-apoptotic function. Overexpression significantly inhibits cell proliferation in several tumor cell lines.Q99816TS101%Tumor susceptibility gene 101 proteinVSUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Late endosome membrane; Peripheral membrane protein. Note=Mainly cytoplasmic. Membrane-associated when active and soluble when inactive. Depending on the stage of the cell cycle, detected in the nucleus. Colocalized with CEP55 in the midbody during cytokinesis.cell cycle arrest [GO:0007050]; cell division [GO:0051301]; endosomal transport [GO:0016197]; endosome to lysosome transport [GO:0008333]; intracellular transport of virus [GO:0075733]; keratinocyte differentiation [GO:0030216]; membrane organization [GO:0061024]; negative regulation of cell proliferation [GO:0008285]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of ubiquitin-dependent endocytosis [GO:2000397]; positive regulation of viral budding via host ESCRT complex [GO:1903774]; positive regulation of viral process [GO:0048524]; positive regulation of viral release from host cell [GO:1902188]; protein monoubiquitination [GO:0006513]; protein transport [GO:0015031]; regulation of cell growth [GO:0001558]; regulation of extracellular exosome assembly [GO:1903551]; regulation of MAP kinase activity [GO:0043405]; regulation of viral budding via host ESCRT complex [GO:1903772]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; viral budding [GO:0046755]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]hcalcium-dependent protein binding [GO:0048306]; DNA binding [GO:0003677]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; protein homodimerization activity [GO:0042803]; transcription corepressor activity [GO:0003714]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; virion binding [GO:0046790]Ecytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; multivesicular body [GO:0005771]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]+FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:21070952, ECO:0000269|PubMed:21757351}.Q14155ARHG7(Rho guanine nucleotide exchange factor 7Destabilizer(18)SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Detected at cell adhesions. A small proportion is detected at focal adhesions. apoptotic signaling pathway [GO:0097190]; astrocyte cell migration [GO:0043615]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; focal adhesion assembly [GO:0048041]; hematopoietic progenitor cell differentiation [GO:0002244]; lamellipodium assembly [GO:0030032]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of GTPase activity [GO:0043547]; positive regulation of lamellipodium morphogenesis [GO:2000394]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]cell cortex [GO:0005938]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; protein complex [GO:0043234]; ruffle [GO:0001726]FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.P22314UBA1+Ubiquitin-like modifier-activating enzyme 1SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Nucleus.; SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.cellular response to DNA damage stimulus [GO:0006974]; modificat< ion-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; ubiquitin activating enzyme activity [GO:0004839]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleus [GO:0005634]6FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites. {ECO:0000269|PubMed:22456334}.Q9NWQ9CN119!Uncharacterized protein C14orf119BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22361696}.O43318M3K70Mitogen-activated protein kinase kinase kinase 7Adherens junction{SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242293}. Cell membrane {ECO:0000269|PubMed:12242293}; Peripheral membrane protein {ECO:0000269|PubMed:12242293}; Cytoplasmic side {ECO:0000269|PubMed:12242293}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane.activation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; Fc-epsilon receptor signaling pathway [GO:0038095]; histone H3 acetylation [GO:0043966]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; I-kappaB phosphorylation [GO:0007252]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of ripoptosome assembly involved in necroptotic process [GO:1902443]; neural tube formation [GO:0001841]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell cytokine production [GO:0002726]; regulation of reactive oxygen species metabolic process [GO:2000377]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase activity [GO:0004708]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]Ada2/Gcn5/Ada3 transcription activator complex [GO:0005671]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity. {ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:12589052, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9079627}.Q9UNH6SNX7Sorting nexin-7SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.[endocytosis [GO:0006897]; protein transport [GO:0015031]; vesicle organization [GO:0016050])phosphatidylinositol binding [GO:0035091]ncytoplasmic vesicle membrane [GO:0030659]; endosome [GO:0005768]; extrinsic component of membrane [GO:0019898]IFUNCTION: May be involved in several stages of intracellular trafficking.O15498YKT6Synaptobrevin homolog YKT6)SNARE interactions in vesicular transportSUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Note=Probably cycles through vesicles between Golgi and endosomes.ER to Golgi vesicle-mediated transport [GO:0006888]; exocytosis [GO:0006887]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking involved in exocytosis [GO:0006904]; vesicle fusion [GO:0006906]; vesicle targeting [GO:0006903]~protein-cysteine S-palmitoyltransferase activity [GO:0019706]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]]cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; mitochondrion [GO:0005739]; SNARE complex [GO:0031201]FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:9211930}.Q9UPQ9TNR6B/Trinucleotide repeat-containing gene 6B proteinSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:19167051}. Note=Mammalian P-bodies are also known as GW bodies (GWBs).epidermal growth facto< r receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; innate immune response [GO:0045087]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; posttranscriptional gene silencing [GO:0016441]; regulation of translation [GO:0006417]Ccytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]+FUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:19304925, ECO:0000269|PubMed:21981923}.Q14203DCTN1Dynactin subunit 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17828277}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17828277}. Note=Colocalizes with microtubules.Pantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; G2/M transition of mitotic cell cycle [GO:0000086]; IRE1-mediated unfolded protein response [GO:0036498]; melanosome transport [GO:0032402]; microtubule-based transport [GO:0010970]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; nervous system development [GO:0007399]; organelle organization [GO:0006996]; retrograde transport, endosome to Golgi [GO:0042147]motor activity [GO:0003774]cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle pole [GO:0000922]FUNCTION: Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein-dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.Q9Y4K4M4K57Mitogen-activated protein kinase kinase kinase kinase 5=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9038372}.activation of JUN kinase activity [GO:0007257]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000269|PubMed:9038372}.Q92882OSTF1Osteoclast-stimulating factor 1;ossification [GO:0001503]; signal transduction [GO:0007165]Vcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]FUNCTION: Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity. {ECO:0000269|PubMed:10092216}.Q99598TSNAXTranslin-associated protein XSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi apparatus {ECO:0000250}. Nucleus. Note=Accumulate in the Golgi complex of mid-late pachytene spermatocytes (By similarity). Expressed in the cytoplasm in the presence of TSN. {ECO:0000250}.cell differentiation [GO:0030154]; gene expression [GO:0010467]; multicellular organismal development [GO:0007275]; protein transport [GO:0015031]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; spermatogenesis [GO:0007283]DNA binding [GO:0003677]; endoribonuclease activity [GO:0004521]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein transporter activity [GO:0008565]; sequence-specific DNA binding [GO:0043565]; single-stranded DNA binding [GO:0003697]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis. {ECO:0000269|PubMed:12036294, ECO:0000269|PubMed:21552258}.O00273DFFA&DNA fragmentation factor subunit alphaapoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; negative regulation of apoptotic DNA fragmentation [GO:1902511]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of apoptotic process [GO:0043065]; programmed cell death [GO:0012501]; thymocyte apoptotic process [GO:0070242]|cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634];FUNCTION: Inhibitor of the caspase-activated DNase (DFF40).O94967WDR47WD repeat-containing protein 47SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization along microtubules is mediated by MAP1S. {ECO:0000250}.1multicellular organismal development [GO:0007275]Q16658FSCN1FascinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, filopodium. Cell projection, invadopodium. Cytoplasm, cytosol. Note=In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol.actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cell motility [GO:0048870]; cell proliferation [GO:0008283]|actin binding [GO:0003779]; actin filament binding [GO:0051015]; drug binding [GO:0008144]; poly(A) RNA binding [GO:0044822]actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; invadopodium [GO:0071437]; myelin sheath [GO:0043209]; stress fiber [GO:0001725]FUNCTION: Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}.O14727APAF&Apoptotic protease-activating factor 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12804598}.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; aging [GO:0007568]; apoptotic process [GO:0006915]; cardiac muscle cell apoptotic process [GO:0010659]; cell differentiation [GO:0030154]; cellular response to transforming growth factor beta stimulus [GO:0071560]; forebrain development [GO:0030900]; glial cell apoptotic process [GO:0034349]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; nervous system development [GO:0007399]; neural tube closure [GO:0001843]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; programmed cell death [GO:0012501]; protein homooligomerization [GO:0051260]; regulation of apoptotic DNA fragmentation [GO:1902510]; regulation of apoptotic process [GO:0042981]; response to G1 DNA damage checkpoint signaling [GO:0072432]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]ADP binding [GO:0043531]; ATP binding [GO:0005524]; cysteine-type endopept< idase activator activity involved in apoptotic process [GO:0008656]; nucleotide binding [GO:0000166]gapoptosome [GO:0043293]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]6FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis. {ECO:0000269|PubMed:10393175, ECO:0000269|PubMed:12804598}.Q6PGP7TTC37#Tetratricopeptide repeat protein 37eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16024656}. Nucleus {ECO:0000269|PubMed:16024656}.cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Ski complex [GO:0055087]; transcriptionally active chromatin [GO:0035327]FUNCTION: Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).P52788SPSYSpermine synthasecellular nitrogen compound metabolic process [GO:0034641]; methionine metabolic process [GO:0006555]; polyamine metabolic process [GO:0006595]; small molecule metabolic process [GO:0044281]; spermine biosynthetic process [GO:0006597]'spermine synthase activity [GO:0016768]oFUNCTION: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).Q9NR31SAR1AGTP-binding protein SAR1aYSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}.intracellular protein transport [GO:0006886]; negative regulation of cargo loading into COPII-coated vesicle [GO:1901303]; vesicle-mediated transport [GO:0016192]eextracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus (By similarity). Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES). {ECO:0000250, ECO:0000269|PubMed:17005010}.P56945BCAR10Breast cancer anti-estrogen resistance protein 1SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:12832404}. Cytoplasm {ECO:0000269|PubMed:12832404}. Note=Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation. {ECO:0000250}.actin filament organization [GO:0007015]; antigen receptor-mediated signaling pathway [GO:0050851]; B cell receptor signaling pathway [GO:0050853]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; cell division [GO:0051301]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; epidermal growth factor receptor signaling pathway [GO:0007173]; G-protein coupled receptor signaling pathway [GO:0007186]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; insulin receptor signaling pathway [GO:0008286]; integrin-mediated signaling pathway [GO:0007229]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of cell migration [GO:0030335]; positive regulation of endothelial cell migration [GO:0010595]; regulation of apoptotic process [GO:0042981]; regulation of cell growth [GO:0001558]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]Lprotein kinase binding [GO:0019901]; signal transducer activity [GO:0004871]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; ruffle [GO:0001726]-FUNCTION: Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells. {ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:17038317}.Q9BU02THTPAThiamine-triphosphatase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11827967}.dephosphorylation [GO:0016311]; generation of precursor metabolites and energy [GO:0006091]; small molecule metabolic process [GO:0044281]; thiamine-containing compound metabolic process [GO:0042723]; thiamine diphosphate metabolic process [GO:0042357]; thiamine metabolic process [GO:0006772]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]qhydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; thiamin-triphosphatase activity [GO:0050333]FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP). {ECO:0000269|PubMed:11827967, ECO:0000269|PubMed:23707715}.Q15814TBCCTubulin-specific chaperone CSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12417528}. Note=Detected predominantly in the photoreceptor connecting cilium.de novo' posttranslational protein folding [GO:0051084]; cell morphogenesis [GO:0000902]; cellular protein metabolic process [GO:0044267]; post-chaperonin tubulin folding pathway [GO:0007023]; protein folding [GO:0006457]<chaperone binding [GO:0051087]; GTPase activity [GO:0003924]ycytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microtubule [GO:0005874]; photoreceptor connecting cilium [GO:0032391]|FUNCTION: Tubulin-folding protein; involved in the final step of the tubulin folding pathway. {ECO:0000269|PubMed:11847227}.Q1RMZ1BMT2'Probable methyltransferase BTM2 homolog6rRNA (adenine) methyltransferase activity [GO:0016433]jFUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000255|HAMAP-Rule:MF_03044}.Q9Y263PLAP$Phospholipase A-2-activating proteinqinflammatory response [GO:0006954]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]0phospholipase A2 activator activity [GO:0016005]IFUNCTION: Involved in the maintenance of ubiquitin levels. {ECO:0000250}.O94855SC24D Protein transport protein Sec24D]antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; in utero embryonic development [GO:0001701]; membrane organization [GO:0061024]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]Q15477SKIV2Helicase SKI2WESUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000305}."RNA catabolic process [GO:0006401]Hnucleoplasm [GO:0005654]; nucleus [GO:0005634]; Ski complex [GO:0055087]FUNCTION: Helicase; has ATPase activity. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).O15344TRI18%E3 ubiquitin-protein ligase Midline-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10077590}. Note=Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbodies during mitosis and cytokinesis.cytokine-mediated signaling pathway [GO:0019221]; interferon-gamma-mediated signaling pathway [GO:0060333]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; pattern specification process [GO:0007389]; positive regulation of stress-ac< tivated MAPK cascade [GO:0032874]; protein localization to microtubule [GO:0035372];identical protein binding [GO:0042802]; ligase activity [GO:0016874]; microtubule binding [GO:0008017]; phosphoprotein binding [GO:0051219]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]qcytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; spindle [GO:0005819]>FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}.A6NDG6PGPPhosphoglycolate phosphatase'Glyoxylate and dicarboxylate metabolism}carbohydrate metabolic process [GO:0005975]; dephosphorylation [GO:0016311]; peptidyl-tyrosine dephosphorylation [GO:0035335]magnesium ion binding [GO:0000287]; nucleotide phosphatase activity, acting on free nucleotides [GO:0098519]; phosphoglycolate phosphatase activity [GO:0008967]; protein tyrosine phosphatase activity [GO:0004725]FUNCTION: Phosphatase with broad substrate specificity. Has high phosphatase activity toward ADP, ATP, GDP, GTP and p-nitrophenylphosphate. Has tyrosine-protein phosphatase activity (in vitro). Has very low activity with pyridoxal 5'-phosphate (By similarity). {ECO:0000250}.Q86UU1PHLB11Pleckstrin homology-like domain family B member 1positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gastrulation [GO:0010470]; regulation of microtubule cytoskeleton organization [GO:0070507]basal cortex [GO:0045180]Q9UNF0PACN2AProtein kinase C and casein kinase substrate in neurons protein 2%SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection {ECO:0000250}. Membrane, caveola. Note=Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1.Mactin cytoskeleton organization [GO:0030036]; caveola assembly [GO:0070836]; caveolin-mediated endocytosis [GO:0072584]; cell projection morphogenesis [GO:0048858]; membrane tubulation [GO:0097320]; negative regulation of endocytosis [GO:0045806]; protein localization to endosome [GO:0036010]; regulation of endocytosis [GO:0030100]cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; phosphatidic acid binding [GO:0070300]; transporter activity [GO:0005215] caveola [GO:0005901]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; membrane-bounded vesicle [GO:0031988]; nucleoplasm [GO:0005654]; recycling endosome membrane [GO:0055038]; ruffle membrane [GO:0032587]FUNCTION: Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis. {ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23129763, ECO:0000269|PubMed:23236520, ECO:0000269|PubMed:23596323}.Q92871PMM1Phosphomannomutase 1fcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose biosynthetic process [GO:0009298]; mannose biosynthetic process [GO:0019307]; mannose metabolic process [GO:0006013]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]Hmetal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615]5cytosol [GO:0005829]; neuronal cell body [GO:0043025]FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. {ECO:0000269|PubMed:16540464}.Q9Y5P6GMPPB*Mannose-1-phosphate guanyltransferase beta>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23768512}.WGTP binding [GO:0005525]; mannose-1-phosphate guanylyltransferase activity [GO:0004475]Q9BXS5AP1M1AP-1 complex subunit mu-1antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; endosome to melanosome transport [GO:0035646]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of defense response to virus by virus [GO:0050690]; viral process [GO:0016032]Cclathrin adaptor complex [GO:0030131]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; trans-Golgi network membrane [GO:0032588]=FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.Q96S44PRPKTP53-regulating kinase<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22912744}.}protein phosphorylation [GO:0006468]; threonylcarbamoyladenosine metabolic process [GO:0070525]; tRNA processing [GO:0008033]ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; p53 binding [GO:0002039]; protein serine/threonine kinase activity [GO:0004674]acytosol [GO:0005829]; EKC/KEOPS complex [GO:0000408]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TP53RK has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit OSGEP (By similarity). Atypical protein kinase that phosphorylates 'Ser-15' of p53/TP53 protein and may therefore participate in its activation. {ECO:0000250, ECO:0000269|PubMed:11546806}.Q5W0V3F16B1Protein FAM160B1Q14012KCC1A2Calcium/calmodulin-dependent protein kinase type 1tSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.cell cycle [GO:0007049]; negative regulation of protein binding [GO:0032091]; nucleocytoplasmic transport [GO:0006913]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of neuron projection development [GO:0010976]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein acetylation [GO:1901985]; positive regulation of protein export from nucleus [GO:0046827]; p< ositive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of synapse structural plasticity [GO:0051835]; positive regulation of syncytium formation by plasma membrane fusion [GO:0060143]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of muscle cell differentiation [GO:0051147]; regulation of protein binding [GO:0043393]; regulation of protein localization [GO:0032880]; signal transduction [GO:0007165]SATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I. {ECO:0000250, ECO:0000269|PubMed:11114197, ECO:0000269|PubMed:12193581, ECO:0000269|PubMed:14507913, ECO:0000269|PubMed:14754892, ECO:0000269|PubMed:17056143, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:20181577}.Q92890UFD1.Ubiquitin fusion degradation protein 1 homologNSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.JDNA repair [GO:0006281]; ER-associated misfolded protein catabolic process [GO:0071712]; error-free translesion synthesis [GO:0070987]; retrograde protein transport, ER to cytosol [GO:0030970]; skeletal system development [GO:0001501]; translesion synthesis [GO:0019985]; ubiquitin-dependent protein catabolic process [GO:0006511]1ubiquitin-specific protease activity [GO:0004843]cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; UFD1-NPL4 complex [GO:0036501]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]$FUNCTION: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures.Q9C0C2TB182#182 kDa tankyrase-1-binding proteinSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Chromosome. Note=Colocalizes with chromosomes during mitosis, and in the cytoplasm with cortical actin.gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; telomere maintenance via telomerase [GO:0007004]9ankyrin binding [GO:0030506]; enzyme binding [GO:0019899]CCR4-NOT complex [GO:0030014]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nuclear telomeric heterochromatin [GO:0005724]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]P49189AL9A1+4-trimethylaminobutyraldehyde dehydrogenaseMcarnitine biosynthetic process [GO:0045329]; cellular aldehyde metabolic process [GO:0006081]; cellular nitrogen compound metabolic process [GO:0034641]; hormone metabolic process [GO:0042445]; neurotransmitter biosynthetic process [GO:0042136]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]1-pyrroline dehydrogenase activity [GO:0033737]; 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aldehyde dehydrogenase (NAD) activity [GO:0004029]; aminobutyraldehyde dehydrogenase activity [GO:0019145]FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction. {ECO:0000269|PubMed:10702312}.Q9NPQ8RIC8A Synembryn-ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). {ECO:0000250}.adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; basement membrane organization [GO:0071711]; cell-cell adhesion involved in gastrulation [GO:0070586]; cell migration involved in gastrulation [GO:0042074]; G-protein coupled receptor signaling pathway [GO:0007186]; in utero embryonic development [GO:0001701]; positive regulation of GTPase activity [GO:0043547]; vasculature development [GO:0001944]; visual learning [GO:0008542]G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]bFUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation. {ECO:0000250, ECO:0000269|PubMed:16629901}.Q7Z3J2CP062UPF0505 protein C16orf62SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Early endosome {ECO:0000305|PubMed:25355947}.OGolgi to plasma membrane transport [GO:0006893]; protein transport [GO:0015031]Hearly endosome [GO:0005769]; integral component of membrane [GO:0016021]hFUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability (PubMed:25355947). {ECO:0000269|PubMed:25355947}.Q9H3P7GCP60Golgi resident protein GCP60SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also mitochondrial (via its interaction with PBR). {ECO:0000250}.Asteroid biosynthetic process [GO:0006694]; transport [GO:0006810]]fatty-acyl-CoA binding [GO:0000062]; protein kinase A regulatory subunit binding [GO:0034237]Golgi apparatus [GO:0005794]; Golgi membra< ne [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrion [GO:0005739] FUNCTION: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). {ECO:0000250}.Q8NEB9PK3C36Phosphatidylinositol 3-kinase catalytic subunit type 3SUBCELLULAR LOCATION: Midbody {ECO:0000269|PubMed:20208530}. Late endosome. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes. Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q6PF93, ECO:0000305}.autophagosome assembly [GO:0000045]; cellular response to glucose starvation [GO:0042149]; cytokinesis [GO:0000910]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; endosome organization [GO:0007032]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; macroautophagy [GO:0016236]; peroxisome degradation [GO:0030242]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; protein phosphorylation [GO:0006468]; protein processing [GO:0016485]; regulation of cytokinesis [GO:0032465]; regulation of protein secretion [GO:0050708]; response to leucine [GO:0043201]; small molecule metabolic process [GO:0044281]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]u1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; protein kinase activity [GO:0004672]autophagosome [GO:0005776]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; late endosome [GO:0005770]; membrane [GO:0016020]; midbody [GO:0030496]; peroxisome [GO:0005777]; phagocytic vesicle [GO:0045335]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]; pre-autophagosomal structure [GO:0000407]%FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity). {ECO:0000250|UniProtKB:O88763, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:7628435, ECO:0000305}.Q93100KPBB.Phosphorylase b kinase regulatory subunit betaGPCRPhosphorylase b kinasenSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.7carbohydrate metabolic process [GO:0005975]; generation of precursor metabolites and energy [GO:0006091]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; protein phosphorylation [GO:0006468]; small molecule metabolic process [GO:0044281]*phosphorylase kinase activity [GO:0004689]]cytosol [GO:0005829]; phosphorylase kinase complex [GO:0005964]; plasma membrane [GO:0005886]FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation.Q9H2M9RBGPR4Rab3 GTPase-activating protein non-catalytic subunitbSUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, it is enriched in the synaptic soluble fraction.establishment of protein localization to endoplasmic reticulum membrane [GO:0097051]; intracellular protein transport [GO:0006886]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of catalytic activity [GO:0043085]; positive regulation of endoplasmic reticulum tubular network organization [GO:1903373]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein lipidation [GO:1903061]; regulation of GTPase activity [GO:0043087]enzyme activator activity [GO:0008047]; enzyme regulator activity [GO:0030234]; GTPase activator activity [GO:0005096]; protein heterodimerization activity [GO:0046982]; Rab GTPase binding [GO:0017137]Rcytoplasm [GO:0005737]; plasma membrane [GO:0005886]; protein complex [GO:0043234]CFUNCTION: Regulatory subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Rab3 GTPase-activating complex specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters. {ECO:0000269|PubMed:9733780}.Q96JJ3ELMO2&Engulfment and cell motility protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20679435}. Cytoplasm, cytosol {ECO:0000269|PubMed:20679435}. Membrane {ECO:0000269|PubMed:20679435}.Aapoptotic process [GO:0006915]; cell-cell adhesion [GO:0098609]; cell chemotaxis [GO:0060326]; cytoskeleton organization [GO:0007010]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]-receptor tyrosine kinase binding [GO:0030971]Ccytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. {ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:11703939, ECO:0000269|PubMed:20679435}.O14976GAKCyclin-G-associated kinase Cell CycleCDKsYSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10625686}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10625686}. Cell junction, focal adhesion {ECO:0000305|PubMed:10625686}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions.OATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. {ECO:0000269|PubMed:10625686}.O00429DNM1LDynamin-1-like protein NecroptosisNecroptosis(11)SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome. Membrane, clathrin-coated pit {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Note=Mainly cytosolic. Translocated to the mitochondrial membrane thr< ough O-GlcNAcylation and interaction with FIS1. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Colocalized with MARCH5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types, localizes to the Golgi complex. Binds to phospholipid membranes.apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; dynamin polymerization involved in mitochondrial fission [GO:0003374]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial membrane fission [GO:0090149]; mitochondrion morphogenesis [GO:0070584]; necroptotic process [GO:0070266]; peroxisome fission [GO:0016559]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein secretion [GO:0050714]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; programmed cell death [GO:0012501]; protein homotetramerization [GO:0051289]; protein localization to mitochondrion [GO:0070585]; regulation of ATP metabolic process [GO:1903578]; regulation of mitochondrion degradation [GO:1903146]; regulation of mitochondrion organization [GO:0010821]; regulation of peroxisome organization [GO:1900063]; regulation of protein oligomerization [GO:0032459]; release of cytochrome c from mitochondria [GO:0001836]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]brush border [GO:0005903]; cell junction [GO:0030054]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; protein complex [GO:0043234]; synaptic vesicle membrane [GO:0030672]FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Also required for mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution.; FUNCTION: Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.C4AMC7WASH3%Putative WAS protein family homolog 3/SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:20175130, ECO:0000269|PubMed:20498093}. Early endosome membrane {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Cell projection, lamellipodium {ECO:0000269|PubMed:18159949}. Cell projection, filopodium {ECO:0000269|PubMed:18159949}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome membrane is mediated via its interaction with FAM21. Localizes to MMP14-positive late endosomes and transiently to invadipodia (By similarity). Localized to Salmonella typhimurium entry sites (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8}.Arp2/3 complex-mediated actin nucleation [GO:0034314]; early endosome to late endosome transport [GO:0045022]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; protein targeting to lysosome [GO:0006622]; retrograde transport, endosome to Golgi [GO:0042147]"alpha-tubulin binding [GO:0043014]2autophagosome [GO:0005776]; centriole [GO:0005814]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203]FUNCTION: Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:18159949, PubMed:20175130). Involved in endocytic trafficking of EGF (PubMed:20175130). Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (By similarity). In T cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T cell activation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (By similarity). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:18159949, ECO:0000269|PubMed:20175130}.P49327FASFatty acid synthaseFatty acid biosynthesisacetyl-CoA metabolic process [GO:0006084]; cellular lipid metabolic process [GO:0044255]; cellular response to interleukin-4 [GO:0071353]; energy reserve metabolic process [GO:0006112]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; mammary gland development [GO:0030879]; osteoblast differentiation [GO:0001649]; pantothenate metabolic process [GO:0015939]; positive regulation of cellular metabolic process [GO:0031325]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767][acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity [GO:0047451]; 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[ac< yl-carrier-protein] synthase activity [GO:0004315]; drug binding [GO:0008144]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity [GO:0004319]; fatty acid synthase activity [GO:0004312]; myristoyl-[acyl-carrier-protein] hydrolase activity [GO:0016295]; NADPH binding [GO:0070402]; oleoyl-[acyl-carrier-protein] hydrolase activity [GO:0004320]; palmitoyl-[acyl-carrier-protein] hydrolase activity [GO:0016296]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; glycogen granule [GO:0042587]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.Q8IYB5SMAP1%Stromal membrane-associated protein 1}SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.ypositive regulation of erythrocyte differentiation [GO:0045648]; regulation of clathrin-mediated endocytosis [GO:2000369]FUNCTION: GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis (By similarity). {ECO:0000250}.P30566PUR8Adenylosuccinate lyasede novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; aerobic respiration [GO:0009060]; AMP biosynthetic process [GO:0006167]; nucleobase-containing small molecule metabolic process [GO:0055086]; protein tetramerization [GO:0051262]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to hypoxia [GO:0001666]; response to muscle activity [GO:0014850]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281](S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity [GO:0070626]; N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity [GO:0004018]iFUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.Q049171433F14-3-3 protein eta apoptotic process [GO:0006915]; gene expression [GO:0010467]; glucocorticoid catabolic process [GO:0006713]; glucocorticoid receptor signaling pathway [GO:0042921]; intracellular protein transport [GO:0006886]; intrinsic apoptotic signaling pathway [GO:0097193]; membrane depolarization during action potential [GO:0086010]; membrane organization [GO:0061024]; negative regulation of dendrite morphogenesis [GO:0050774]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of transcription, DNA-templated [GO:0045893]; programmed cell death [GO:0012501]; regulation of neuron differentiation [GO:0045664]; regulation of sodium ion transmembrane transporter activity [GO:2000649]; regulation of sodium ion transport [GO:0002028]; regulation of synaptic plasticity [GO:0048167]; small GTPase mediated signal transduction [GO:0007264]; substantia nigra development [GO:0021762]; transcription initiation from RNA polymerase II promoter [GO:0006367]5enzyme binding [GO:0019899]; glucocorticoid receptor binding [GO:0035259]; insulin-like growth factor receptor binding [GO:0005159]; ion channel binding [GO:0044325]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; sodium channel regulator activity [GO:0017080]cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intercalated disc [GO:0014704]; plasma membrane [GO:0005886]O94885SASH1'SAM and SH3 domain-containing protein 1 positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of NIK/NF-kappaB signaling [GO:1901224]; positive regulation of p38MAPK cascade [GO:1900745]; protein polyubiquitination [GO:0000209]; regulation of protein autoubiquitination [GO:1902498]; regulation of protein K63-linked ubiquitination [GO:1900044]mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein complex scaffold [GO:0032947]; protein C-terminus binding [GO:0008022]; protein kinase binding [GO:0019901]3membrane [GO:0016020]; protein complex [GO:0043234]RFUNCTION: May have a role in a signaling pathway. Could act as a tumor suppressor.Q13144EI2BE4Translation initiation factor eIF-2B subunit epsilonastrocyte development [GO:0014002]; astrocyte differentiation [GO:0048708]; cellular protein metabolic process [GO:0044267]; cellular response to drug [GO:0035690]; gene expression [GO:0010467]; myelination [GO:0042552]; negative regulation of translational initiation in response to stress [GO:0032057]; oligodendrocyte development [GO:0014003]; ovarian follicle development [GO:0001541]; positive regulation of GTPase activity [GO:0043547]; positive regulation of translational initiation [GO:0045948]; response to endoplasmic reticulum stress [GO:0034976]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to peptide hormone [GO:0043434]; translation [GO:0006412]; translational initiation [GO:0006413]guanyl-nucleotide exchange factor activity [GO:0005085]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]; nucleus [GO:0005634]Q9Y3P9RBGP1Rab GTPase-activating protein 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10202141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10202141}. Note=Predominantly cytosolic but also associated with the centrosome. {ECO:0000269|PubMed:10202141}.Lcell cycle [GO:0007049]; positive regulation of GTPase activity [GO:0043547]DNA binding [GO:0003677]; GTPase activator activity [GO:0005096]; Rab GTPase binding [GO:0017137]; tubulin binding [GO:0015631]Zcentrosome [GO:0005813]; cytosol [GO:0005829]; microtubule associated complex [GO:0005875] FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a role in microtubule nucleation by centrosome. May participate in a RAB6A-mediated pathway involved in the metaphase-anaphase transition. {ECO:0000269|PubMed:10202141, ECO:0000269|PubMed:16395330}.O96007MOC2B(Molybdopterin synthase catalytic subunithSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:15073332}.,molybdopterin synthase activity [GO:0030366]ocytoplasm [GO:0005737]; cytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008]; nucleus [GO:0005634]nFUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. {ECO:0000255|HAMAP-Rule:MF_03052, ECO:0000269|PubMed:12732628, ECO:0000269|PubMed:15073332}.Q8N1I0DOCK4"Dedicator of cytokinesis protein 4[SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Cytoplasm, cytosol.cell chemotaxis [GO:0060326]; positive regulation of GTPase activity [GO:0043547]; small GTPase mediated signal transduct< ion [GO:0007264]GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; PDZ domain binding [GO:0030165]; Rac GTPase binding [GO:0048365]; receptor tyrosine kinase binding [GO:0030971]cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; stereocilium [GO:0032420]; stereocilium bundle [GO:0032421]!FUNCTION: Involved in regulation of adherens junction between cells. Plays a role in cell migration. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP. {ECO:0000269|PubMed:12628187, ECO:0000269|PubMed:20679435}.Q9Y223GLCNEKBifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinasecarbohydrate phosphorylation [GO:0046835]; cell adhesion [GO:0007155]; cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; N-acetylglucosamine biosynthetic process [GO:0006045]; N-acetylneuraminate metabolic process [GO:0006054]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-N-acetylglucosamine metabolic process [GO:0006047]ATP binding [GO:0005524]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; metal ion binding [GO:0046872]; N-acylmannosamine kinase activity [GO:0009384]; UDP-N-acetylglucosamine 2-epimerase activity [GO:0008761]FUNCTION: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development (By similarity). Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. {ECO:0000250, ECO:0000269|PubMed:10334995}.Q147382A5DOSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform]SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in interphase, nuclear during mitosis.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; dephosphorylation [GO:0016311]; energy reserve metabolic process [GO:0006112]; glucose metabolic process [GO:0006006]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; nervous system development [GO:0007399]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of protein phosphatase type 2A activity [GO:0034047]; small molecule metabolic process [GO:0044281]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]wprotein phosphatase type 2A regulator activity [GO:0008601]; protein serine/threonine phosphatase activity [GO:0004722]vcytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]Q86VS8HOOK3Protein Hook homolog 3SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11238449}. Golgi apparatus {ECO:0000269|PubMed:11238449}. Note=Enriched at the cis-face of the Golgi complex. Localizes to microtubule asters in prophase. {ECO:0000250}.cytoplasmic microtubule organization [GO:0031122]; early endosome to late endosome transport [GO:0045022]; endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; Golgi localization [GO:0051645]; interkinetic nuclear migration [GO:0022027]; lysosome organization [GO:0007040]; microtubule anchoring at centrosome [GO:0034454]; negative regulation of neurogenesis [GO:0050768]; neuronal stem cell maintenance [GO:0097150]; protein localization to centrosome [GO:0071539]; protein transport [GO:0015031]Hidentical protein binding [GO:0042802]; microtubule binding [GO:0008017]centriolar satellite [GO:0034451]; centrosome [GO:0005813]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; FHF complex [GO:0070695]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; pericentriolar material [GO:0000242]rFUNCTION: Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. {ECO:0000250, ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622}.Q9Y5R8TPPC1.Trafficking protein particle complex subunit 1lSUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.hER to Golgi vesicle-mediated transport [GO:0006888]; positive regulation of GTPase activity [GO:0043547];Rab guanyl-nucleotide exchange factor activity [GO:0017112]|cis-Golgi network [GO:0005801]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; TRAPP complex [GO:0030008]UFUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.P49840GSK3A Glycogen synthase kinase-3 alpha cardiac left ventricle morphogenesis [GO:0003214]; cell migration [GO:0016477]; cellular protein metabolic process [GO:0044267]; cellular response to insulin stimulus [GO:0032869]; cellular response to interleukin-3 [GO:0036016]; cellular response to lithium ion [GO:0071285]; cellular response to organic cyclic compound [GO:0071407]; endoplasmic reticulum unfolded protein response [GO:0030968]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glycogen metabolic process [GO:0005977]; hypermethylation of CpG island [GO:0044027]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; IRE1-mediated unfolded protein response [GO:0036498]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; negative regulation of glucose import [GO:0046325]; negative regulation of glycogen (starch) synthase activity [GO:2000466]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulation of glycogen synthase activity, transferring glucose-1-phosphate [GO:1904227]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of TOR signaling [GO:0032007]; negative regulation of type B pancreatic cell development [GO:2000077]; negative regulation of UDP-glucose catabolic process [GO:0010905]; nervous system development [GO:0007399]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of adrenergic receptor signaling pathway [GO:0071879]; positive regulation of cAMP biosynthetic process [GO:0030819]; positive regulation of glycogen (starch) synthase activity [GO:2000467]; positive regulation of heart contraction [GO:0045823]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of protein catabolic process [GO:0045732< ]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein phosphorylation [GO:0006468]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of mitochondrion degradation [GO:1903146]; regulation of systemic arterial blood pressure [GO:0003073]; Wnt signaling pathway [GO:0016055]ATP binding [GO:0005524]; protein kinase A catalytic subunit binding [GO:0034236]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]Cbeta-catenin destruction complex [GO:0030877]; cytosol [GO:0005829]FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle. May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells. Is necessary for the establishment of neuronal polarity and axon outgrowth. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. {ECO:0000269|PubMed:12761548, ECO:0000269|PubMed:17229088}.Q96H20SNF8Vacuolar-sorting protein SNF8SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane. Nucleus {ECO:0000305}. Late endosome membrane. Note=Recruited to the endosome membrane to participate in vesicle formation.Qearly endosome to late endosome transport [GO:0045022]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; membrane organization [GO:0061024]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of gene expression [GO:0010628]; positive regulation of protein catabolic process [GO:0045732]; protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; regulation of multivesicular body size involved in endosome transport [GO:0010797]; regulation of protein catabolic process [GO:0042176]; regulation of protein complex stability [GO:0061635]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of viral budding via host ESCRT complex [GO:1903772]; transcription, DNA-templated [GO:0006351]channel regulator activity [GO:0016247]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]; protein N-terminus binding [GO:0047485]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; ESCRT II complex [GO:0000814]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; transcription factor complex [GO:0005667];FUNCTION: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. {ECO:0000269|PubMed:17714434, ECO:0000269|PubMed:17959629, ECO:0000269|PubMed:18031739}.Q6ZMI0PPR21+Protein phosphatase 1 regulatory subunit 21 phosphatase binding [GO:0019902]O75592MYCB2"E3 ubiquitin-protein ligase MYCBP2;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9689053}.}branchiomotor neuron axon guidance [GO:0021785]; central nervous system projection neuron axonogenesis [GO:0021952]; negative regulation of protein catabolic process [GO:0042177]; regulation of cytoskeleton organization [GO:0051493]; regulation of protein localization [GO:0032880]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]eaxon [GO:0030424]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]VFUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin. Interacts with the E2 enzymes UBE2D1, UBE2D3 and UBE2L3 (in vitro). May function as a facilitator or regulator of transcriptional activation by MYC. May have a role during synaptogenesis. {ECO:0000269|PubMed:18308511}.Q9Y4E6WDR7WD repeat-containing protein 7:hematopoietic progenitor cell differentiation [GO:0002244]synaptic vesicle [GO:0008021]Q00341VIGLNVigilincSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8605996}. Nucleus {ECO:0000269|PubMed:8605996}.Hcholesterol metabolic process [GO:0008203]; lipid transport [GO:0006869]<lipid binding [GO:0008289]; poly(A) RNA binding [GO:0044822]zcytoplasm [GO:0005737]; high-density lipoprotein particle [GO:0034364]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.P67936TPM4Tropomyosin alpha-4 chainmovement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; osteoblast differentiation [GO:0001649]Ocalcium ion binding [GO:0005509]; structural constituent of muscle [GO:0008307],cortical cytoskeleton [GO:0030863]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; membrane [GO:0016020]; muscle thin filament tropomyosin [GO:0005862]; podosome [GO:0002102]; stress fiber [GO:0001725]FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. {ECO:0000269|PubMed:1836432}.P09497CLCBClathrin light chain BSUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.Xclathrin-mediated endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]rclathrin heavy chain binding [GO:0032050]; peptide binding [GO:0042277]; structural molecule activity [GO:0005198]Qciliary membrane [GO:0060170]; clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin vesicle coat [GO:0030125]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802][FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.Q15042RB3GP0Rab3 GTPase-activating protein catalytic subunitSUBCELLULA< R LOCATION: Cytoplasm {ECO:0000269|PubMed:9852129}. Note=In neurons, it is enriched in the synaptic soluble fraction.brain development [GO:0007420]; camera-type eye development [GO:0043010]; establishment of protein localization to endoplasmic reticulum membrane [GO:0097051]; face morphogenesis [GO:0060325]; hypothalamus development [GO:0021854]; lipid particle organization [GO:0034389]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of endoplasmic reticulum tubular network organization [GO:1903373]; positive regulation of gene expression [GO:0010628]; positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization [GO:0061646]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein lipidation [GO:1903061]; regulation of calcium ion-dependent exocytosis of neurotransmitter [GO:1903233]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of GTPase activity [GO:0043087]; regulation of short-term neuronal synaptic plasticity [GO:0048172]cytoplasm [GO:0005737]; endoplasmic reticulum tubular network [GO:0071782]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lipid particle [GO:0005811]; protein complex [GO:0043234]IFUNCTION: Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters. {ECO:0000269|PubMed:10859313, ECO:0000269|PubMed:9030515}.Q9NX55HYPK Huntingtin-interacting protein K+FUNCTION: Has a chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT. Protects against HTT polyQ-mediated apoptosis in Neuro2a neuronal cells. Required for optimal NAA10-NAA15 complex-mediated N-terminal acetylation. {ECO:0000269|PubMed:17947297, ECO:0000269|PubMed:20154145}.Q13158FADD#FAS-associated death domain protein activation of cysteine-type endopeptidase activity [GO:0097202]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; death-inducing signaling complex assembly [GO:0071550]; defense response to virus [GO:0051607]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; innate immune response [GO:0045087]; lymph node development [GO:0048535]; motor neuron apoptotic process [GO:0097049]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; necroptotic signaling pathway [GO:0097527]; negative regulation of activation-induced cell death of T cells [GO:0070236]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of necroptotic process [GO:0060546]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of apoptotic process [GO:0043065]; positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation [GO:2000454]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of proteolysis [GO:0045862]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein heterooligomerization [GO:0051291]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of necrotic cell death [GO:0010939]; spleen development [GO:0048536]; T cell differentiation in thymus [GO:0033077]; T cell homeostasis [GO:0043029]; thymus development [GO:0048538]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; TRAIL-activated apoptotic signaling pathway [GO:0036462]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; viral process [GO:0016032]death effector domain binding [GO:0035877]; death receptor binding [GO:0005123]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; tumor necrosis factor receptor superfamily binding [GO:0032813]CD95 death-inducing signaling complex [GO:0031265]; cell body [GO:0044297]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; ripoptosome [GO:0097342]8FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling. {ECO:0000269|PubMed:16762833, ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634, ECO:0000269|PubMed:21109225}.P18858DNLI1 DNA ligase 1Kanatomical structure morphogenesis [GO:0009653]; base-excision repair [GO:0006284]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA ligation [GO:0006266]; DNA metabolic process [GO:0006259]; DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; lagging strand elongation [GO:0006273]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; Okazaki fragment processing involved in mitotic DNA replication [GO:1903461]; removal of RNA primer involved in mitotic DNA replication [GO:1903469]; response to hydrogen peroxide [GO:0042542]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA ligase activity [GO:0003909]; metal ion binding [GO:0046872]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]vFUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.Q9BW91NUDT9)ADP-ribose pyrophosphatase, mitochondrial/SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.ADP catabolic process [GO:0046032]; IDP catabolic process [GO:0046709]; nucleobase-containing small molec< ule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; small molecule metabolic process [GO:0044281]adenosine-diphosphatase activity [GO:0043262]; ADP-ribose diphosphatase activity [GO:0047631]; ADP-sugar diphosphatase activity [GO:0019144]aextracellular exosome [GO:0070062]; intracellular [GO:0005622]; mitochondrial matrix [GO:0005759]FFUNCTION: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.Q96T51RUFY1(RUN and FYVE domain-containing protein 1VSUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral membrane protein.@endocytosis [GO:0006897]; regulation of endocytosis [GO:0030100]dlipid binding [GO:0008289]; protein transporter activity [GO:0008565]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking. {ECO:0000269|PubMed:14617813}.O00399DCTN6Dynactin subunit 6SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:23455152}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; mitotic spindle organization [GO:0007052]{centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; dynactin complex [GO:0005869]O00178GTPB1GTP-binding protein 1zimmune response [GO:0006955]; positive regulation of mRNA catabolic process [GO:0061014]; signal transduction [GO:0007165]XGTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]]cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; membrane [GO:0016020]FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}.Q9Y6A4CFA20)Cilia- and flagella-associated protein 20SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Cell projection, cilium.4cilium morphogenesis [GO:0060271]; multicellular organismal development [GO:0007275]; positive regulation of cell motility [GO:2000147]; positive regulation of feeding behavior [GO:2000253]; protein polyglutamylation [GO:0018095]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296]centriole [GO:0005814]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; nucleus [GO:0005634],FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the regulation of the size and morphology of cilia (PubMed:24414207). Required for axonemal microtubules polyglutamylation (PubMed:24414207). {ECO:0000269|PubMed:24414207}.P31153METK2,S-adenosylmethionine synthase isoform type-2methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; S-adenosylmethionine biosynthetic process [GO:0006556]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]nATP binding [GO:0005524]; metal ion binding [GO:0046872]; methionine adenosyltransferase activity [GO:0004478]Icytosol [GO:0005829]; methionine adenosyltransferase complex [GO:0048269]RFUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP.O43617TPPC3.Trafficking protein particle complex subunit 3@endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]Q9Y6E0STK24"Serine/threonine-protein kinase 24SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.%activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; execution phase of apoptosis [GO:0097194]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; negative regulation of cell migration [GO:0030336]; programmed cell death [GO:0012501]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of axon regeneration [GO:0048679]; regulation of mitotic cell cycle [GO:0007346]; response to hydrogen peroxide [GO:0042542]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve. {ECO:0000269|PubMed:16314523, ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:19782762, ECO:0000269|PubMed:19855390}.Q9H0F6SHRPNSharpinSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20179993}. Cell junction, synapse {ECO:0000250}. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1. {ECO:0000250}.apoptotic nuclear changes [GO:0030262]; brain development [GO:0007420]; keratinization [GO:0031424]; mitochondrion organization [GO:0007005]; negative regulation of inflammatory response [GO:0050728]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein homooligomerization [GO:0051260]; protein linear polyubiquitination [GO:0097039]; regulation of CD40 signaling pathway [GO:2000348]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]Apolyubiquitin binding [GO:0031593]; zinc ion binding [GO:0008270]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; LUBAC complex [GO:0071797]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. {ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}.P24534EF1BElongation factor 1-betacellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; translation [< GO:0006412]; translational elongation [GO:0006414]3translation elongation factor activity [GO:0003746]mcytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation elongation factor 1 complex [GO:0005853]\FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.P53396ACLYATP-citrate synthaseCitrate cycle (TCA cycle)Cacetyl-CoA metabolic process [GO:0006084]; cellular carbohydrate metabolic process [GO:0044262]; cellular lipid metabolic process [GO:0044255]; citrate metabolic process [GO:0006101]; coenzyme A metabolic process [GO:0015936]; energy reserve metabolic process [GO:0006112]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cellular metabolic process [GO:0031325]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]ATP binding [GO:0005524]; ATP citrate synthase activity [GO:0003878]; cofactor binding [GO:0048037]; metal ion binding [GO:0046872]citrate lyase complex [GO:0009346]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine. {ECO:0000269|PubMed:23932781}.Q05655KPCDProtein kinase C delta typeSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Endoplasmic reticulum. Mitochondrion. Cell membrane; Peripheral membrane protein.a activation of phospholipase C activity [GO:0007202]; apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; blood coagulation [GO:0007596]; cell cycle [GO:0007049]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular senescence [GO:0090398]; cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; immunoglobulin mediated immune response [GO:0016064]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; interleukin-10 production [GO:0032613]; interleukin-12 production [GO:0032615]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of filopodium assembly [GO:0051490]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of protein binding [GO:0032091]; neurotrophin TRK receptor signaling pathway [GO:0048011]; neutrophil activation [GO:0042119]; peptidyl-threonine phosphorylation [GO:0018107]; platelet activation [GO:0030168]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of glucosylceramide catabolic process [GO:2000753]; positive regulation of phospholipid scramblase activity [GO:1900163]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of response to DNA damage stimulus [GO:2001022]; positive regulation of sphingomyelin catabolic process [GO:2000755]; positive regulation of superoxide anion generation [GO:0032930]; programmed cell death [GO:0012501]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of receptor activity [GO:0010469]; signal transduction [GO:0007165]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; termination of signal transduction [GO:0023021]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; calcium-independent protein kinase C activity [GO:0004699]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; insulin receptor substrate binding [GO:0043560]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]Jcell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]bFUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen< -induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). {ECO:0000250}.Q9BTW9TBCDTubulin-specific chaperone DSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Lateral cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Note=Localized in cell-cell contacts. {ECO:0000250}.de novo' posttranslational protein folding [GO:0051084]; adherens junction assembly [GO:0034333]; bicellular tight junction assembly [GO:0070830]; cellular protein metabolic process [GO:0044267]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of microtubule polymerization [GO:0031115]; positive regulation of GTPase activity [GO:0043547]; post-chaperonin tubulin folding pathway [GO:0007023]; protein folding [GO:0006457]ibeta-tubulin binding [GO:0048487]; chaperone binding [GO:0051087]; GTPase activator activity [GO:0005096]adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; lateral plasma membrane [GO:0016328]; microtubule [GO:0005874]FUNCTION: Tubulin-folding protein; involved in the first step of the tubulin folding pathway. Modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Acts as a GTPase-activating protein (GAP) for ARL2. Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. {ECO:0000269|PubMed:10722852, ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:20740604}.O43149ZZEF1;Zinc finger ZZ-type and EF-hand domain-containing protein 1?calcium ion binding [GO:0005509]; zinc ion binding [GO:0008270]P29353SHC1SHC-transforming protein 1SUBCELLULAR LOCATION: Cytoplasm.; SUBCELLULAR LOCATION: Isoform p46Shc: Mitochondrion matrix {ECO:0000269|PubMed:14573619}. Note=Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization.; SUBCELLULAR LOCATION: Isoform p66Shc: Mitochondrion {ECO:0000250}. Note=In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation. {ECO:0000250}.,actin cytoskeleton reorganization [GO:0031532]; activation of MAPK activity [GO:0000187]; aging [GO:0007568]; angiogenesis [GO:0001525]; blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart development [GO:0007507]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; IRE1-mediated unfolded protein response [GO:0036498]; leukocyte migration [GO:0050900]; MAPK cascade [GO:0000165]; neuron projection development [GO:0031175]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ regeneration [GO:0031100]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet activation [GO:0030168]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA replication [GO:0045740]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of vasoconstriction [GO:0045907]; Ras protein signal transduction [GO:0007265]; regulation of epidermal growth factor-activated receptor activity [GO:0007176]; regulation of growth [GO:0040008]; response to glucocorticoid [GO:0051384]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to nicotine [GO:0035094]; response to toxic substance [GO:0009636]; single organismal cell-cell adhesion [GO:0016337]; viral process [GO:0016032]ephrin receptor binding [GO:0046875]; epidermal growth factor receptor binding [GO:0005154]; insulin-like growth factor receptor binding [GO:0005159]; insulin receptor binding [GO:0005158]; neurotrophin TRKA receptor binding [GO:0005168]; phospholipid binding [GO:0005543]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]cytosol [GO:0005829]; endosome membrane [GO:0010008]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Shc-EGFR complex [GO:0070435]FUNCTION: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis. {ECO:0000250, ECO:0000269|PubMed:14665640}.Q9Y6Y8S23IPSEC23-interacting proteinSUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum {ECO:0000305}.acrosome assembly [GO:0001675]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; single fertilization [GO:0007338]Ccis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ER to Golgi transport vesicle membrane [GO:0012507]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear endoplasmic reticulum [GO:0097038]BFUNCTION: Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P). {ECO:0000269|PubMed:10400679, ECO:0000269|PubMed:15623529, ECO:0000269|PubMed:22922100}.Q9UBC2EP15R4Epidermal growth factor receptor substrate 15-like 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, coated pit {ECO:0000250}. Note=Localized to plasma membrane coated pits. {ECO:0000250}.endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]sclathrin coat of coated pit [GO:0030132]; membrane [GO:0016020]; nucleus< [GO:0005634]; plasma membrane [GO:0005886]mFUNCTION: Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9407958}.Q15654TRIP6&Thyroid receptor-interacting protein 6SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16624523}. Cell junction, focal adhesion {ECO:0000269|PubMed:16624523}. Nucleus {ECO:0000269|PubMed:16624523}. Cytoplasm {ECO:0000269|PubMed:16624523}. Note=Shuttles between nucleus and cytoplasm.focal adhesion assembly [GO:0048041]; positive regulation of cell migration [GO:0030335]; regulation of transcription, DNA-templated [GO:0006355]; release of cytoplasmic sequestered NF-kappaB [GO:0008588]; transcription, DNA-templated [GO:0006351]interleukin-1 receptor binding [GO:0005149]; kinase binding [GO:0019900]; poly(A) RNA binding [GO:0044822]; thyroid hormone receptor binding [GO:0046966]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. {ECO:0000269|PubMed:14688263, ECO:0000269|PubMed:15489293, ECO:0000269|PubMed:16624523, ECO:0000269|PubMed:19017743}.Q14258TRI25 E3 ubiquitin/ISG15 ligase TRIM25Innate immune receptor}SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17392790}. Note=Colocalized with DDX58 at cytoplasmic perinuclear bodies.cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; DNA repair [GO:0006281]; ERAD pathway [GO:0036503]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of type I interferon production [GO:0032480]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral release from host cell [GO:1902187]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein monoubiquitination [GO:0006513]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of viral entry into host cell [GO:0046596]; regulation of viral release from host cell [GO:1902186]; translesion synthesis [GO:0019985]; viral process [GO:0016032]acid-amino acid ligase activity [GO:0016881]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]; ubiquitin protein ligase activity involved in ERAD pathway [GO:1904264]; zinc ion binding [GO:0008270]FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. {ECO:0000269|PubMed:16352599, ECO:0000269|PubMed:17069755, ECO:0000269|PubMed:17392790}.Q16204CCDC6'Coiled-coil domain-containing protein 6kSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000305}. Note=May be a cytoskeletal protein.P26641EF1GElongation factor 1-gammacellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; response to virus [GO:0009615]; translation [GO:0006412]; translational elongation [GO:0006414]}cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]VFUNCTION: Probably plays a role in anchoring the complex to other cellular components.Q96GG9DCNL1DCN1-like protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25349211}.;nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates (PubMed:25349211). Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity). {ECO:0000250, ECO:0000269|PubMed:25349211}.P78362SRPK2SRSF protein kinase 2SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation.angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative regulation of viral genome replication [GO:0045071]; nuclear speck organization [GO:0035063]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]; protein serine/threonine kinase activity [GO:0004674]QFUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:9472028}.Q8N1G4LRC47)Leucine-rich repeat-containing protein 47P54725RD23A*UV excision repair protein RAD23 homolog A'nucleotide-excision repair [GO:0006289]; positive regulation of viral genome replication [GO:0045070]; proteasome-mediated ubiquitin-depende< nt protein catabolic process [GO:0043161]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; viral process [GO:0016032]damaged DNA binding [GO:0003684]; polyubiquitin binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin-specific protease binding [GO:1990381]Qcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; proteasome complex [GO:0000502]5FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: Involved in vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome.Q5T4S7UBR4 E3 ubiquitin-protein ligase UBR4SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Note=Concentrates at the leading edge of membrane structures involved in actin motility.yprotein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; viral process [GO:0016032]centrosome [GO:0005813]; cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleoplasm [GO:0005654]xFUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization. Regulates integrin-mediated signaling. May play a role in activation of FAK in response to cell-matrix interactions. Mediates ubiquitination of ACLY, leading to its subsequent degradation. {ECO:0000269|PubMed:16214886, ECO:0000269|PubMed:23932781}.Q9NS86LANC2LanC-like protein 2SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane. Note=Localizes to the juxta-nuclear vesicles. Associates with the cortical actin cytoskeleton. Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the cell membrane in vitro and an enhanced cell detachment from the matrix in vivo. Membrane-association is important for the increased cellular sensitivity to an anticancer drug (adriamycin).negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of abscisic acid-activated signaling pathway [GO:0009789]ATP binding [GO:0005524]; catalytic activity [GO:0003824]; GTP binding [GO:0005525]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes. {ECO:0000269|PubMed:19667068}.O43353RIPK26Receptor-interacting serine/threonine-protein kinase 2Nervous systemNeurotrophin signaling pathway activation of MAPK activity [GO:0000187]; adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to peptidoglycan [GO:0071224]; defense response to Gram-positive bacterium [GO:0050830]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; neurotrophin TRK receptor signaling pathway [GO:0048011]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070427]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of apoptotic process [GO:0043065]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of immature T cell proliferation [GO:0033091]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of JNK cascade [GO:0046330]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; response to exogenous dsRNA [GO:0043330]; response to interleukin-1 [GO:0070555]; response to interleukin-12 [GO:0070671]; response to interleukin-18 [GO:0070673]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]OATP binding [GO:0005524]; CARD domain binding [GO:0050700]; LIM domain binding [GO:0030274]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]; receptor binding [GO:0005102]; signal transducer activity [GO:0004871]{cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; protein complex [GO:0043234]; vesicle [GO:0031982]FUNCTION: Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated pr< otein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation. {ECO:0000269|PubMed:14638696, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730}.O14964HGS<Hepatocyte growth factor-regulated tyrosine kinase substrateSSUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Endosome, multivesicular body membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments. {ECO:0000269|PubMed:16159959}. endosomal transport [GO:0016197]; endosome to lysosome transport [GO:0008333]; epidermal growth factor receptor signaling pathway [GO:0007173]; membrane invagination [GO:0010324]; membrane organization [GO:0061024]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of JAK-STAT cascade [GO:0046426]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of gene expression [GO:0010628]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization to membrane [GO:0072657]; protein targeting to lysosome [GO:0006622]; regulation of MAP kinase activity [GO:0043405]; regulation of protein catabolic process [GO:0042176]; signal transduction [GO:0007165]Lmetal ion binding [GO:0046872]; protein domain specific binding [GO:0019904],cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; multivesicular body membrane [GO:0032585]; secretory granule [GO:0030141]FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.Q04637IF4G12Eukaryotic translation initiation factor 4 gamma 1behavioral fear response [GO:0001662]; cellular protein metabolic process [GO:0044267]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of neuron differentiation [GO:0045666]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]; viral process [GO:0016032]eukaryotic initiation factor 4E binding [GO:0008190]; poly(A) RNA binding [GO:0044822]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; membrane [GO:0016020]FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.Q13489BIRC3+Baculoviral IAP repeat-containing protein 3eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15665297}. Nucleus {ECO:0000269|PubMed:15665297}.cell surface receptor signaling pathway [GO:0007166]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; innate immune response [GO:0045087]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; NIK/NF-kappaB signaling [GO:0038061]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein ubiquitination [GO:0031398]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of cysteine-type endopeptidase activity [GO:2000116]; regulation of inflammatory response [GO:0050727]; regulation of innate immune response [GO:0045088]; regulation of necroptotic process [GO:0060544]; regulation of necrotic cell death [GO:0010939]; regulation of nucleotide-binding oligomerization domain containing signaling pathway [GO:0070424]; regulation of RIG-I signaling pathway [GO:0039535]; regulation of toll-like receptor signaling pathway [GO:0034121]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. {ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969}.P55263ADKAdenosine kinaseVSUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.WAMP salvage [GO:0044209]; dATP biosynthetic process [GO:0006175]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; ribonucleoside monophosphate biosynthetic process [GO:0009156]; small molecule metabolic process [GO:0044281]adenosine kinase activity [GO:0004001]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as ac< ceptor [GO:0016773]; poly(A) RNA binding [GO:0044822]FUNCTION: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.Q165372A5EQSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoformaregulation of protein phosphatase type 2A activity [GO:0034047]; signal transduction [GO:0007165];protein phosphatase type 2A regulator activity [GO:0008601]Hcytoplasm [GO:0005737]; protein phosphatase type 2A complex [GO:0000159]Q8IXJ6SIR2+NAD-dependent protein deacetylase sirtuin-2Histone deacetylaseA SUBCELLULAR LOCATION: Nucleus. Cytoplasm, perinuclear region. Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle. Midbody. Chromosome. Perikaryon {ECO:0000250}. Cell projection {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Myelin membrane {ECO:0000250}. Note=Deacetylates FOXO3 in the cytoplasm. Colocalizes with PLP1 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat. Colocalizes with CDK5R1 in the perikaryon, neurites and growth cone of hippocampal neurons. Colocalizes with alpha-tubulin in neuronal growth cone. Localizes in the cytoplasm and nucleus of germinal vesicle (GV) stage oocytes. Colocalizes with alpha-tubulin on the meiotic spindle as the oocytes enter into metaphase, and also during meiotic anaphase and telophase, especially with the midbody. Colocalizes with PARD3 in internodal region of axons. Colocalizes with acetylated alpha-tubulin in cell projection processes during primary oligodendrocyte precursor (OLP) differentiation (By similarity). Localizes in the cytoplasm during most of the cell cycle except in the G2/M transition and during mitosis, where it is localized in association with chromatin and induces deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with SETD8 at mitotic foci. Colocalizes with CDK1 at centrosome during prophase and splindle fibers during metaphase. Colocalizes with Aurora kinase AURKA at centrosome during early prophase and in the centrioles and growing mitotic spindle throughout metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis with the midbody. Colocalizes with microtubules. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Shuttles between the cytoplasm and the nucleus through the CRM1 export pathway. Colocalizes with EP300 in the nucleus. Translocates to the nucleus and chromatin upon bacterium Listeria monocytogenes infection in interphase cells. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the cytoplasmic.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm {ECO:0000269|PubMed:24177535}. Nucleus {ECO:0000269|PubMed:24177535}. Note=Predominantly localized in the nucleus. autophagy [GO:0006914]; cell division [GO:0051301]; cellular lipid catabolic process [GO:0044242]; cellular response to caloric restriction [GO:0061433]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to hypoxia [GO:0071456]; cellular response to molecule of bacterial origin [GO:0071219]; cellular response to oxidative stress [GO:0034599]; chromatin silencing [GO:0006342]; chromatin silencing at rDNA [GO:0000183]; chromatin silencing at telomere [GO:0006348]; gene silencing [GO:0016458]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; histone deacetylation [GO:0016575]; histone H3 deacetylation [GO:0070932]; histone H4 deacetylation [GO:0070933]; innate immune response [GO:0045087]; meiotic cell cycle [GO:0051321]; mitotic nuclear division [GO:0007067]; myelination in peripheral nervous system [GO:0022011]; negative regulation of autophagy [GO:0010507]; negative regulation of cell proliferation [GO:0008285]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of NLRP3 inflammasome complex assembly [GO:1900226]; negative regulation of oligodendrocyte progenitor proliferation [GO:0070446]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of striated muscle tissue development [GO:0045843]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061428]; peptidyl-lysine deacetylation [GO:0034983]; phosphatidylinositol 3-kinase signaling [GO:0014065]; positive regulation of attachment of spindle microtubules to kinetochore [GO:0051987]; positive regulation of cell division [GO:0051781]; positive regulation of DNA binding [GO:0043388]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of meiotic nuclear division [GO:0045836]; positive regulation of oocyte maturation [GO:1900195]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia [GO:2000777]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ADP-ribosylation [GO:0006471]; protein deacetylation [GO:0006476]; protein kinase B signaling [GO:0043491]; regulation of cell cycle [GO:0051726]; regulation of exit from mitosis [GO:0007096]; regulation of myelination [GO:0031641]; regulation of phosphorylation [GO:0042325]; response to redox state [GO:0051775]; ripoptosome assembly involved in necroptotic process [GO:1901026]; substantia nigra development [GO:0021762]; transcription, DNA-templated [GO:0006351]; tubulin deacetylation [GO:0090042];chromatin binding [GO:0003682]; histone acetyltransferase binding [GO:0035035]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone deacetylase activity (H4-K16 specific) [GO:0046970]; NAD-dependent protein deacetylase activity [GO:0034979]; protein deacetylase activity [GO:0033558]; transcription factor binding [GO:0008134]; tubulin deacetylase activity [GO:0042903]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270]centriole [GO:0005814]; centrosome [GO:0005813]; chromatin silencing complex [GO:0005677]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glial cell projection [GO:0097386]; growth cone [GO:0030426]; juxtaparanode region of axon [GO:0044224]; lateral loop [GO:0043219]; meiotic spindle [GO:0072687]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; myelin sheath [GO:0043209]; nuclear heterochromatin [GO:0005720]; nucleus [GO:0005634]; paranodal junction [GO:0033010]; paranode region of axon [GO:0033270]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]; spindle [GO:0005819]FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metab< olic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis. Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by SETD8 leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression. Deacetylates SETD8 modulating SETD8 chromatin localization during the mitotic stress response. Deacetylates also histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition. Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection. During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy. Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation. Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor.; FUNCTION: Isoform 1: Deacetylates EP300, alpha-tubulin and histone H3 and H4.; FUNCTION: Isoform 2: Deacetylates EP300, alpha-tubulin and histone H3 and H4.; FUNCTION: Isoform 5: Lacks deacetylation activity.Q53T59H1BP3HCLS1-binding protein 3>FUNCTION: May be a modulator of IL-2 signaling. {ECO:0000250}.P51580TPMTThiopurine S-methyltransferasemethylation [GO:0032259]; nucleobase-containing compound metabolic process [GO:0006139]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]4thiopurine S-methyltransferase activity [GO:0008119]rFUNCTION: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. {ECO:0000269|PubMed:18484748}.P51808DYLT3Dynein light chain Tctex-type 3SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Chromosome, centromere, kinetochore. Note=Colocalizes with BUB3 at kinetochores specifically during prometaphase.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; regulation of mitotic cell cycle [GO:0007346]; transport [GO:0006810]condensed chromosome kinetochore [GO:0000777]; cytoplasmic dynein complex [GO:0005868]; microtubule [GO:0005874]; nucleus [GO:0005634]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis (By similarity). {ECO:0000250}.O60701UGDHUDP-glucose 6-dehydrogenase@carbohydrate metabolic process [GO:0005975]; cellular glucuronidation [GO:0052695]; glycosaminoglycan biosynthetic process [GO:0006024]; small molecule metabolic process [GO:0044281]; UDP-glucose metabolic process [GO:0006011]; UDP-glucuronate biosynthetic process [GO:0006065]; xenobiotic metabolic process [GO:0006805]selectron carrier activity [GO:0009055]; NAD binding [GO:0051287]; UDP-glucose 6-dehydrogenase activity [GO:0003979]Rcytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]sFUNCTION: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.Q5VIR6VPS536Vacuolar protein sorting-associated protein 53 homologSUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:18367545}; Peripheral membrane protein. Endosome membrane {ECO:0000269|PubMed:18367545}; Peripheral membrane protein. Recycling endosome {ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex (PubMed:25799061). {ECO:0000269|PubMed:25799061}.vendocytic recycling [GO:0032456]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]EARP complex [GO:1990745]; endosome membrane [GO:0010008]; GARP complex [GO:0000938]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}.P61163ACTZAlpha-centractinantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996];< vesicle-mediated transport [GO:0016192]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; extracellular exosome [GO:0070062]; microtubule associated complex [GO:0005875]; myelin sheath [GO:0043209]O75822EIF3J4Eukaryotic translation initiation factor 3 subunit JBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.&cellular protein metabolic process [GO:0044267]; cytoplasmic translation [GO:0002181]; formation of translation preinitiation complex [GO:0001731]; gene expression [GO:0010467]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]>FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.Q9P2B4CT2NLCTTNBP2 N-terminal-like proteinpSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with stress fibers. {ECO:0000250}.negative regulation of transmembrane transport [GO:0034763]; negative regulation of transporter activity [GO:0032410]; protein dephosphorylation [GO:0006470]+protein phosphatase 2A binding [GO:0051721]7actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]P78344IF4G22Eukaryotic translation initiation factor 4 gamma 2cell cycle arrest [GO:0007050]; cell death [GO:0008219]; cytokine-mediated signaling pathway [GO:0019221]; regulation of translational initiation [GO:0006446]poly(A) RNA binding [GO:0044822]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]mcytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; membrane [GO:0016020]/FUNCTION: Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases. {ECO:0000269|PubMed:11511540, ECO:0000269|PubMed:11943866, ECO:0000269|PubMed:9032289, ECO:0000269|PubMed:9049310}.Q86WR0CCD25(Coiled-coil domain-containing protein 25P49459UBE2A!Ubiquitin-conjugating enzyme E2 Aantigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; DNA repair [GO:0006281]; histone H2A ubiquitination [GO:0033522]; in utero embryonic development [GO:0001701]; maternal process involved in female pregnancy [GO:0060135]; positive regulation of cell proliferation [GO:0008284]; postreplication repair [GO:0006301]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; response to UV [GO:0009411]; ubiquitin-dependent protein catabolic process [GO:0006511]chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; HULC complex [GO:0033503]; nuclear chromatin [GO:0000790]; XY body [GO:0001741]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:20061386}.Q05086UBE3AUbiquitin-protein ligase E3AgSUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08759}. Cytoplasm {ECO:0000250|UniProtKB:O08759}.Yandrogen receptor signaling pathway [GO:0030521]; brain development [GO:0007420]; ovarian follicle development [GO:0001541]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; prostate gland growth [GO:0060736]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; proteolysis [GO:0006508]; regulation of circadian rhythm [GO:0042752]; regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000058]; sperm entry [GO:0035037]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]ligase activity [GO:0016874]; metal ion binding [GO:0046872]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]ccytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome complex [GO:0000502]aFUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component ARNTL/BMAL1, leading to its proteasomal degradation (PubMed:24728990). {ECO:0000269|PubMed:10373495, ECO:0000269|PubMed:19204938, ECO:0000269|PubMed:19233847, ECO:0000269|PubMed:19325566, ECO:0000269|PubMed:19591933, ECO:0000269|PubMed:22645313, ECO:0000269|PubMed:24728990}.Q9H1K0RBNS5 Rabenosyn-5SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane {ECO:0000269|PubMed:22308388}; Lipid-anchor. Note=Enriched in endosomes that are in close proximity to clathrin-enriched regions at the cell surface. {ECO:0000269|PubMed:22308388}.Gblood coagulation [GO:0007596]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; endosomal vesicle fusion [GO:0034058]; Golgi to endosome transport [GO:0006895]; Golgi to vacuole transport [GO:0006896]; late endosome to vacuole transport [GO:0045324]; protein transport [GO:0015031]; vacuole inheritance [GO:0000011]>Rab GTPase binding [GO:0017137]; zinc ion binding [GO:0008270]cytoplasmic side of endosome membrane [GO:0010009]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a rol< e in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in the recycling of transferrin receptor to the plasma membrane (PubMed:22308388). {ECO:0000269|PubMed:11062261, ECO:0000269|PubMed:11788822, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:22308388}.Q13107UBP4'Ubiquitin carboxyl-terminal hydrolase 4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:20595234}. Nucleus {ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:20595234}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type. {ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:20595234}.negative regulation of protein ubiquitination [GO:0031397]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein localization to cell surface [GO:0034394]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein stability [GO:0031647]; spliceosomal tri-snRNP complex assembly [GO:0000244]adenosine receptor binding [GO:0031685]; cysteine-type endopeptidase activity [GO:0004197]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin-specific protease activity [GO:0004843]acytoplasm [GO:0005737]; lysosome [GO:0005764]; nucleus [GO:0005634]; plasma membrane [GO:0005886]oFUNCTION: Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:7784062}.Q9UJW0DCTN4Dynactin subunit 4nSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10671518}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10671518}. Note=In skeletal muscles, demonstrates a punctate distribution along costameres (By similarity). Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin. Overexpression does not disrupt microtubule organization or the integrity of the Golgi but does cause both cytosolic and nuclear distribution, suggesting that this polypeptide may be targeted to the nucleus at very high expression levels. {ECO:0000250}.~antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; nuclear migration [GO:0007097]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; nucleus [GO:0005634]FUNCTION: Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.Q9BV20MTNA&Methylthioribose-1-phosphate isomeraseaSUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:19620624}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:19620624}. Cell projection {ECO:0000269|PubMed:19620624}. Note=Primarily nuclear, but cytoplasmic in cancer cells, with enrichment at leading edge of the plasma membrane in late stage tumor cells.Wcellular nitrogen compound metabolic process [GO:0034641]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; L-methionine biosynthetic process from S-adenosylmethionine [GO:0019284]; polyamine metabolic process [GO:0006595]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]iidentical protein binding [GO:0042802]; S-methyl-5-thioribose-1-phosphate isomerase activity [GO:0046523]bcell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]pFUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:19620624}.Q9H832UBE2Z!Ubiquitin-conjugating enzyme E2 ZeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17160626}. Nucleus {ECO:0000269|PubMed:17160626}.apoptotic process [GO:0006915]; protein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]ATP binding [GO:0005524]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]'FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:17464193, ECO:0000269|PubMed:17597759}.Q13614MTMR2Myotubularin-related protein 2=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758}. Early endosome membrane {ECO:0000269|PubMed:21372139}; Peripheral membrane protein {ECO:0000269|PubMed:21372139}. Note=Partly associated with membranes. {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:21372139, ECO:0000305}.0dendritic spine maintenance [GO:0097062]; inositol phosphate dephosphorylation [GO:0046855]; myelin assembly [GO:0032288]; negative regulation of endocytosis [GO:0045806]; negative regulation of excitatory postsynaptic membrane potential [GO:0090394]; negative regulation of myelination [GO:0031642]; negative regulation of receptor catabolic process [GO:2000645]; negative regulation of receptor internalization [GO:0002091]; neuron development [GO:0048666]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; positive regulation of early endosome to late endosome transport [GO:2000643]; protein dephosphorylation [GO:0006470]; protein tetramerization [GO:0051262]; small molecule metabolic process [GO:0044281]phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]_axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; neuronal postsynaptic density [GO:0097481]; nucleus [GO:0005634]; synaptic membrane [GO:0097060]; synaptic vesicle [GO:0008021]; vacuolar membrane [GO:0005774]FUNCTION: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:21372139}.P47756CAPZB$F-actin-capping protein subunit betakSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; barbed-end actin filament capping [GO:0051016]; blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; cytoskeleton organiz< ation [GO:0007010]; movement of cell or subcellular component [GO:0006928]; negative regulation of filopodium assembly [GO:0051490]; regulation of cell morphogenesis [GO:0022604]; regulation of lamellipodium assembly [GO:0010591]actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; F-actin capping protein complex [GO:0008290]; sarcomere [GO:0030017]; WASH complex [GO:0071203]FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.O43822CU002Protein C21orf2cilium morphogenesis [GO:0060271]; cytoskeleton organization [GO:0007010]; regulation of cell shape [GO:0008360]; smoothened signaling pathway [GO:0007224]FUNCTION: May play roles in cilia formation and/or maintenance (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000250, ECO:0000269|PubMed:21834987}.P46940IQGA1)Ras GTPase-activating-like protein IQGAP1BSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15355962}.1cellular response to calcium ion [GO:0071277]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glomerular visceral epithelial cell development [GO:0072015]; negative regulation of dephosphorylation [GO:0035305]; negative regulation of GTPase activity [GO:0034260]; neuron projection extension [GO:1990138]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; regulation of cytokine production [GO:0001817]; regulation of insulin secretion [GO:0050796]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; GTPase inhibitor activity [GO:0005095]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activator activity [GO:0043539]; S100 protein binding [GO:0044548]0actin filament [GO:0005884]; axon [GO:0030424]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; lateral plasma membrane [GO:0016328]; microtubule [GO:0005874]; midbody [GO:0030496]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; slit diaphragm [GO:0036057]nFUNCTION: Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth. {ECO:0000269|PubMed:15695813}.O14980XPO1 Exportin-1SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.gene expression [GO:0010467]; intracellular transport of virus [GO:0075733]; mitotic cell cycle [GO:0000278]; mRNA transport [GO:0051028]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; protein export from nucleus [GO:0006611]; protein localization to nucleus [GO:0034504]; regulation of centrosome duplication [GO:0010824]; regulation of protein catabolic process [GO:0042176]; regulation of protein export from nucleus [GO:0046825]; response to drug [GO:0042493]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from nucleus [GO:0000056]; small GTPase mediated signal transduction [GO:0007264]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral life cycle [GO:0019058]; viral process [GO:0016032]nucleocytoplasmic transporter activity [GO:0005487]; protein transporter activity [GO:0008565]; RNA binding [GO:0003723]; transporter activity [GO:0005215]{annulate lamellae [GO:0005642]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; kinetochore [GO:0000776]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]>FUNCTION: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization. {ECO:0000269|PubMed:14612415, ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:9311922, ECO:0000269|PubMed:9323133, ECO:0000269|PubMed:9837918}.O00471EXOC5Exocyst complex component 5=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119050}.cellular protein metabolic process [GO:0044267]; exocytosis [GO:0006887]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; vesicle docking [GO:0048278]Ral GTPase binding [GO:0017160]FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.Q16513PKN2"Serine/threonine-protein kinase N2kinaseSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000250}. Cell projection, lamellipodium. Cytoplasm, cytoskeleton. Cleavage furrow. Midbody. Cell junction. Note=Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. In the course of viral infection, colocalizes with HCV NS5B at perinuclear region in the cytoplasm.sapical junction assembly [GO:0043297]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; epithelial cell migration [GO:00106< 31]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of cell motility [GO:2000145]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351],ATP binding [GO:0005524]; histone deacetylase binding [GO:0042826]; kinase activity [GO:0016301]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase binding [GO:0070063]apical junction complex [GO:0043296]; cell junction [GO:0030054]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. {ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:15364941, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:9121475}.O43633CHM2A&Charged multivesicular body protein 2aSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral membrane protein {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Cytoplasmic side {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; establishment of protein localization [GO:0045184]; membrane invagination [GO:0010324]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; negative regulation of cell death [GO:0060548]; negative regulation of centriole elongation [GO:1903723]; nucleus organization [GO:0006997]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of viral release from host cell [GO:1902188]; post-Golgi vesicle-mediated transport [GO:0006892]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein polymerization [GO:0051258]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; regulation of viral process [GO:0050792]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]Vphosphatidylcholine binding [GO:0031210]; protein domain specific binding [GO:0019904]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; membrane coat [GO:0030117]FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844}.Q9NZN5ARHGC)Rho guanine nucleotide exchange factor 12SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}. Note=Translocated to the membrane upon stimulation. {ECO:0000305}.apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; G-protein coupled receptor signaling pathway [GO:0007186]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; termination of G-protein coupled receptor signaling pathway [GO:0038032]G-protein coupled receptor binding [GO:0001664]; GTPase activator activity [GO:0005096]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]#FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. {ECO:0000269|PubMed:11094164}.Q9UPM8AP4E1AP-4 complex subunit epsilon-1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Membrane, coated pit {ECO:0000250}. Note=Associated with the trans-Golgi network. Found in soma and dendritic shafts of neuronal cells.intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]{coated pit [GO:0005905]; endosome lumen [GO:0031904]; membrane coat [GO:0030117]; trans-Golgi network membrane [GO:0032588]FUNCTION: Subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.Q9H6S0YTDC2*Probable ATP-dependent RNA helicase YTHDC2positive regulation by host of viral genome replication [GO:0044829]; response to interleukin-1 [GO:0070555]; response to tumor necrosis factor [GO:0034612]; RNA processing [GO:0006396]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]; RNA-dependent ATPase activity [GO:0008186]; RNA polymerase binding [GO:0070063]:cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. {ECO:0000250|UniProtKB:Q9QY02}< .O43747AP1G1AP-1 complex subunit gamma-1qSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:12773381}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:12773381}; Peripheral membrane protein {ECO:0000269|PubMed:12773381}; Cytoplasmic side {ECO:0000269|PubMed:12773381}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.Tantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; endosome to melanosome transport [GO:0035646]; Golgi to lysosome transport [GO:0090160]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; membrane organization [GO:0061024]; positive regulation of natural killer cell degranulation [GO:0043323]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of defense response to virus by virus [GO:0050690]; viral process [GO:0016032]GTP-dependent protein binding [GO:0030742]; kinesin binding [GO:0019894]; protein transporter activity [GO:0008565]; Rab GTPase binding [GO:0017137]; transporter activity [GO:0005215]dAP-type membrane coat adaptor complex [GO:0030119]; clathrin adaptor complex [GO:0030131]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; trans-Golgi network membrane [GO:0032588]Q13200PSMD2.26S proteasome non-ATPase regulatory subunit 2 proteasomecytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]1FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.; FUNCTION: Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.O60841IF2P+Eukaryotic translation initiation factor 5Bcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; translation initiation factor activity [GO:0003743]FUNCTION: Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity). {ECO:0000250}.Q9HAU5RENT2#Regulator of nonsense transcripts 2SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187}.gene expression [GO:0010467]; liver development [GO:0001889]; mRNA export from nucleus [GO:0006406]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; organ regeneration [GO:0031100]cytoplasm [GO:0005737]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]cFUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:18066079}.Q99571P2RX4P2X purinoceptor 4 Ca-SignalingROCxSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10515189}; Multi-pass membrane protein {ECO:0000269|PubMed:10515189}.Capoptotic signaling pathway [GO:0097190]; calcium ion transport [GO:0006816]; cation transport [GO:0006812]; cellular response to ATP [GO:0071318]; endothelial cell activation [GO:0042118]; ion transmembrane transport [GO:0034220]; membrane depolarization [GO:0051899]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; neuronal action potential [GO:0019228]; nitric oxide biosynthetic process [GO:0006809]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of prostaglandin secretion [GO:0032308]; protein homooligomerization [GO:0051260]; purinergic nucleotide receptor signaling pathway [GO:0035590]; regulation of blood pressure [GO:0008217]; regulation of cardiac muscle contraction [GO:0055117]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of sodium ion transport [GO:0002028]; relaxation of cardiac muscle [GO:0055119]; response to ATP [GO:0033198]; response to fluid shear stress [GO:0034405]; sensory perception of pain [GO:0019233]; signal transduction [GO:0007165]; tissue homeostasis [GO:0001894]; transport [GO:0006810]; vasodilation [GO:0042311]UATP binding [GO:0005524]; cadherin binding [GO:0045296]; copper ion binding [GO:0005507]; drug binding [GO:0008144]; extracellular ATP-gated cation channel activity [GO:0004931]; protein homodimerization activity [GO:0042803]; purinergic nucleotide receptor activity [GO:0001614]; receptor binding [GO:0005102]; zinc ion binding [GO:0008270]apical part of cell [GO:0045177]; cell junction [GO:0030054]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; integral component of nuclear inner membrane [GO:0005639]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; terminal bouton [GO:0043195]FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel. This receptor is insensitive to the antagonists PPADS and suramin. {ECO:0000269|PubMed:10515189}.Q9Y262EIF3L4Eukaryotic translation initiation factor 3 subunit LBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.formation of translation preinitiation complex [GO:0001731]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413]Upoly(A) RNA binding [GO:0044822]; translation initiation factor activity [GO:0003743]eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; fibrillar center [GO:0001650]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.Q9NZ32ARP10Actin-related protein 10'microtubule-based movement [GO:0007018]5cytoplasm [GO:0005737]; dynactin complex [GO:0005869]P11142HSP7C!Heat shock cognate 71 kDa protein< SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.ATP metabolic process [GO:0046034]; axon guidance [GO:0007411]; cellular response to heat [GO:0034605]; chaperone mediated protein folding requiring cofactor [GO:0051085]; clathrin coat disassembly [GO:0072318]; gene expression [GO:0010467]; membrane organization [GO:0061024]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of fibril organization [GO:1902904]; negative regulation of transcription, DNA-templated [GO:0045892]; neurotransmitter secretion [GO:0007269]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; post-Golgi vesicle-mediated transport [GO:0006892]; protein folding [GO:0006457]; protein refolding [GO:0042026]; regulation of cell cycle [GO:0051726]; regulation of cellular response to heat [GO:1900034]; response to unfolded protein [GO:0006986]; RNA splicing [GO:0008380]; synaptic transmission [GO:0007268]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; C3HC4-type RING finger domain binding [GO:0055131]; enzyme binding [GO:0019899]; G-protein coupled receptor binding [GO:0001664]; heat shock protein binding [GO:0031072]; MHC class II protein complex binding [GO:0023026]; poly(A) RNA binding [GO:0044822]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]!blood microparticle [GO:0072562]; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; melanosome [GO:0042470]; membrane [GO:0016020]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Prp19 complex [GO:0000974]; ribonucleoprotein complex [GO:0030529]; spliceosomal complex [GO:0005681] FUNCTION: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:23990462}.Q86VX2COMD7 COMM domain-containing protein 7HSUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:21778237}.negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]; tumor necrosis factor-mediated signaling pathway [GO:0033209]NF-kappaB binding [GO:0051059]Ucytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Associates with the NF-kappa-B complex and suppresses its transcriptional activity (PubMed:15799966). {ECO:0000269|PubMed:15799966, ECO:0000305|PubMed:21778237}.Q01970PLCB3@1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 Gap junction<SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.G-protein coupled receptor signaling pathway [GO:0007186]; inositol phosphate metabolic process [GO:0043647]; intracellular signal transduction [GO:0035556]; lipid catabolic process [GO:0016042]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of systemic arterial blood pressure [GO:0003073]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; signal transducer activity [GO:0004871]ecytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]; sarcolemma [GO:0042383]FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.P62191PRS4!26S protease regulatory subunit 45anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; proteasome-activating ATPase activity [GO:0036402]; TBP-class protein binding [GO:0017025]mcell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.O00410IPO5 Importin-5SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus.1cellular response to amino acid stimulus [GO:0071230]; negative regulation of GTPase activity [GO:0034260]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of protein import into nucleus [GO:0042307]; ribosomal protein import into nucleus [GO:0006610]; viral process [GO:0016032]GTPase inhibitor activity [GO:0005095]; poly(A) RNA binding [GO:0044822]; protein transporter activity [GO:0008565]; Ran GTPase binding [GO:0008536]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020];< nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]\FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000250, ECO:0000269|PubMed:9687515}.P26640SYVCValine--tRNA ligase~gene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]; valyl-tRNA aminoacylation [GO:0006438]paminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; valine-tRNA ligase activity [GO:0004832]Q96F86EDC3$Enhancer of mRNA-decapping protein 3cSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16364915}. Note=Processing bodies (PB).exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]@identical protein binding [GO:0042802]; RNA binding [GO:0003723]Zcytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; membrane [GO:0016020]FUNCTION: Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis. {ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:17533573, ECO:0000269|PubMed:18678652}.Q7KZF4SND13Staphylococcal nuclease domain-containing protein 1&SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.osteoblast differentiation [GO:0001649]; posttranscriptional gene silencing by RNA [GO:0035194]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]nnuclease activity [GO:0004518]; poly(A) RNA binding [GO:0044822]; transcription cofactor activity [GO:0003712]cytoplasm [GO:0005737]; dense body [GO:0097433]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; RISC complex [GO:0016442] FUNCTION: Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). {ECO:0000269|PubMed:7651391}.Q8WXA3RUFY2(RUN and FYVE domain-containing protein 2Q96F24NRBF2!Nuclear receptor-binding factor 2SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasmic vesicle {ECO:0000269|PubMed:25086043}. Cytoplasmic vesicle, autophagosome {ECO:0000305}.autophagy [GO:0006914]; gene expression [GO:0010467]; regulation of autophagy [GO:0010506]; regulation of transcription, DNA-templated [GO:0006355]; transcription initiation from RNA polymerase II promoter [GO:0006367]autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; nucleoplasm [GO:0005654]FUNCTION: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro). {ECO:0000269|PubMed:15610520}.; FUNCTION: Involved in starvation-induced autophagy probably by its association with PI3K complex I (PI3KC3-C1). However, effects has been described variably. Involved in the induction of starvation-induced autophagy (PubMed:24785657). Stabilzes PI3KC3-C1 assembly and enhances ATG14-linked lipid kinase activity of PIK3C3 (By similarity). Proposed to negatively regulate basal and starvation-induced autophagy and to inhibit PIK3C3 activity by modulating interactions in PI3KC3-C1 (PubMed:25086043). May be involved in autophagosome biogenesis (PubMed:25086043). May play a role in neural progenitor cell survival during differentiation (By similarity). {ECO:0000250|UniProtKB:Q8VCQ3, ECO:0000269|PubMed:24785657, ECO:0000269|PubMed:25086043}.P07814SYEP+Bifunctional glutamate/proline--tRNA ligase6cellular response to interferon-gamma [GO:0071346]; gene expression [GO:0010467]; glutamyl-tRNA aminoacylation [GO:0006424]; negative regulation of translation [GO:0017148]; prolyl-tRNA aminoacylation [GO:0006433]; protein complex assembly [GO:0006461]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; glutamate-tRNA ligase activity [GO:0004818]; GTPase binding [GO:0051020]; proline-tRNA ligase activity [GO:0004827]; RNA stem-loop binding [GO:0035613]aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; membrane [GO:0016020]; ribonucleoprotein complex [GO:0030529]CFUNCTION: Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. {ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:1756734, ECO:0000269|PubMed:23071094}.Q9NZB2F120A5Constitutive coactivator of PPAR-gamma-like protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19015244}. Cell membrane {ECO:0000269|PubMed:19015244}; Peripheral membrane protein {ECO:0000269|PubMed:19015244}; Cytoplasmic side {ECO:0000269|PubMed:19015244}. Note=Translocates to plasma membrane upon ultraviolet exposure.Kcytoplasm [GO:0005737]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: May participate in mRNA transport in the cytoplasm (By similarity). Critical component of the oxidative stress-induced survival signaling. Activates src family kinases and acts as a scaffolding protein enabling src family kinases to phosphorylate and activate PI3-kinase. Binds RNA and promotes the secretion of IGF-II. May play a pivotal role in the progression of scirrhous-type gastric cancer by supporting cancer cell survival in environments with various oxidative stresses. {ECO:0000250, ECO:0000269|PubMed:19015244}.Q00610CLH1Clathrin heavy chain 1 SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17081065}; Peripheral membrane protein {ECO:0000269|PubMed:17081065}; Cytoplasmic side {ECO:0000269|PubMed:17081065}. Membrane, coated pit {ECO:0000269|PubMed:17081065}; Peripheral membrane protein {ECO:0000269|PubMed:17081065}; Cytoplasmic side {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Cytoplasmic face of coated pits and vesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.< =antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; mitotic nuclear division [GO:0007067]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of protein localization to plasma membrane [GO:1903077]; osteoblast differentiation [GO:0001649]; post-Golgi vesicle-mediated transport [GO:0006892]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; transferrin transport [GO:0033572]clathrin light chain binding [GO:0032051]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; structural molecule activity [GO:0005198]tclathrin coat [GO:0030118]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated vesicle [GO:0030136]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin complex [GO:0071439]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; spindle [GO:0005819]; trans-Golgi network membrane [GO:0032588]FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.Q9Y2A7NCKP1Nck-associated protein 1aSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}.=apical protein localization [GO:0045176]; apoptotic process [GO:0006915]; basal protein localization [GO:0045175]; cell migration involved in gastrulation [GO:0042074]; central nervous system development [GO:0007417]; embryonic body morphogenesis [GO:0010172]; embryonic foregut morphogenesis [GO:0048617]; embryonic heart tube development [GO:0035050]; endoderm development [GO:0007492]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; in utero embryonic development [GO:0001701]; lamellipodium assembly [GO:0030032]; mesodermal cell migration [GO:0008078]; neural tube closure [GO:0001843]; notochord morphogenesis [GO:0048570]; paraxial mesoderm morphogenesis [GO:0048340]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; positive regulation of lamellipodium assembly [GO:0010592]; protein stabilization [GO:0050821]; Rac protein signal transduction [GO:0016601]; regulation of protein localization [GO:0032880]; small GTPase mediated signal transduction [GO:0007264]; somitogenesis [GO:0001756]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]; zygotic determination of anterior/posterior axis, embryo [GO:0007354]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lamellipodium membrane [GO:0031258]; SCAR complex [GO:0031209]FUNCTION: Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1.Q9Y6W5WASF20Wiskott-Aldrich syndrome protein family member 2Arp2/3 activators(6)SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=At the interface between the lamellipodial actin meshwork and the membrane. {ECO:0000250}.#actin cytoskeleton organization [GO:0030036]; actin filament-based movement [GO:0030048]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; ameboidal-type cell migration [GO:0001667]; angiogenesis [GO:0001525]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; lamellipodium assembly [GO:0030032]; lamellipodium morphogenesis [GO:0072673]; megakaryocyte development [GO:0035855]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of lamellipodium assembly [GO:0010592]; Rac protein signal transduction [GO:0016601]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]@actin binding [GO:0003779]; protein complex binding [GO:0032403]actin cytoskeleton [GO:0015629]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; lamellipodium [GO:0030027]; ruffle [GO:0001726]; SCAR complex [GO:0031209]FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. {ECO:0000269|PubMed:10381382, ECO:0000269|PubMed:16275905}.Q92614MY18AUnconventional myosin-XVIIIaSUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Cytoplasm, cytoskeleton. Note=Colocalizes with actin.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks the PDZ domain. Diffusely localized in the cytoplasm.; SUBCELLULAR LOCATION: Golgi apparatus. Golgi apparatus, trans-Golgi network. Note=Recruited to the Golgi apparatus by GOLPH3.wactomyosin structure organization [GO:0031032]; asymmetric Golgi ribbon formation [GO:0090164]; cell migration [GO:0016477]; DNA metabolic process [GO:0006259]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; Golgi vesicle budding [GO:0048194]; negative regulation of apoptotic process [GO:0043066]; positive regulation of protein secretion [GO:0050714]actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]actomyosin [GO:0042641]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; myosin complex [GO:0016459]; trans-Golgi network [GO:0005802]yFUNCTION: May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. May be involved in the maintenance of the stromal cell architectures required for cell to cell contact. {ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:23345592}.Q86V48LUZP1Leucine zipper protein 1bSUBCELLULAR LOCATION: Nucleus. Note=Also detected in soma and dendrites of neurons. {ECO:0000250}.nartery development [GO:0060840]; neural fold bending [GO:0021503]; ventricular septum development [GO:0003281]Oextracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]P63279UBC9SUMO-conjugating enzyme UBC9SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body (By similarity). {ECO:0000250}.cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; chromosome segregation [GO:0007059]; mitotic nuclear < division [GO:0007067]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of intracellular steroid hormone receptor signaling pathway [GO:0033145]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of SUMO transferase activity [GO:1903755]; post-translational protein modification [GO:0043687]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein sumoylation [GO:0016925]; protein ubiquitination [GO:0016567]; regulation of receptor activity [GO:0010469]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]_ATP binding [GO:0005524]; enzyme binding [GO:0019899]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; RING-like zinc finger domain binding [GO:0071535]; SUMO conjugating enzyme activity [GO:0061656]; SUMO transferase activity [GO:0019789]; transcription factor binding [GO:0008134]; ubiquitin-protein transferase activity [GO:0004842]8cytoplasm [GO:0005737]; dendrite [GO:0030425]; fibrillar center [GO:0001650]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; sumoylated E2 ligase complex [GO:1990356]; synapse [GO:0045202]; synaptonemal complex [GO:0000795]; transferase complex [GO:1990234]gFUNCTION: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:8668529}.O00303EIF3F4Eukaryotic translation initiation factor 3 subunit FBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.'cellular protein metabolic process [GO:0044267]; formation of translation preinitiation complex [GO:0001731]; gene expression [GO:0010467]; protein deubiquitination [GO:0016579]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]ftranslation initiation factor activity [GO:0003743]; ubiquitin-specific protease activity [GO:0004843]cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; membrane [GO:0016020]|FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:21124883}.; FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling. {ECO:0000269|PubMed:21124883}.P09525ANXA4 Annexin A4epithelial cell differentiation [GO:0030855]; negative regulation of apoptotic process [GO:0043066]; negative regulation of catalytic activity [GO:0043086]; negative regulation of interleukin-8 secretion [GO:2000483]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; NF-kappaB binding [GO:0051059]; phospholipase inhibitor activity [GO:0004859]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506]{FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. {ECO:0000250}.P35611ADDA Alpha-adducinlSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.Uactin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; apoptotic process [GO:0006915]; barbed-end actin filament capping [GO:0051016]; cell morphogenesis [GO:0000902]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular protein metabolic process [GO:0044267]; cell volume homeostasis [GO:0006884]; endoplasmic reticulum unfolded protein response [GO:0030968]; erythrocyte differentiation [GO:0030218]; hemoglobin metabolic process [GO:0020027]; homeostasis of number of cells within a tissue [GO:0048873]; in utero embryonic development [GO:0001701]; IRE1-mediated unfolded protein response [GO:0036498]; multicellular organism growth [GO:0035264]; positive regulation of protein binding [GO:0032092]; programmed cell death [GO:0012501]; transmembrane transport [GO:0055085]8actin binding [GO:0003779]; actin filament binding [GO:0051015]; poly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; spectrin binding [GO:0030507]; structural molecule activity [GO:0005198]; transcription factor binding [GO:0008134]cytosol [GO:0005829]; F-actin capping protein complex [GO:0008290]; focal adhesion [GO:0005925]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.Q6R327RICTR'Rapamycin-insensitive companion of mTOR actin cytoskeleton reorganization [GO:0031532]; embryo development [GO:0009790]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of TOR signaling [GO:0032008]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of establishment of cell polarity [GO:2000114]; regulation of gene expression [GO:0010468]; regulation of GTPase activity [GO:0043087]; regulation of inflammatory response [GO:0050727]; regulation of peptidyl-serine phosphorylation [GO:0033135]; regulation of protein kinase B signaling [GO:0051896]; T cell costimulation [GO:0031295]; TOR signaling [GO:0031929]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]Bprotein kinase binding [GO:0019901]; ribosome binding [GO:0043022]0cytosol [GO:0005829]; TORC2 complex [GO:0031932]FUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of< Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development. {ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470}.Q14653IRF3Interferon regulatory factor 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10805757}. Nucleus {ECO:0000269|PubMed:10805757}. Note=Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm.apoptotic process [GO:0006915]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to dsRNA [GO:0071359]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; macrophage apoptotic process [GO:0071888]; MDA-5 signaling pathway [GO:0039530]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of type I interferon production [GO:0032480]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; positive regulation of type I interferon production [GO:0032481]; programmed necrotic cell death [GO:0097300]; response to exogenous dsRNA [GO:0043330]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; type I interferon biosynthetic process [GO:0045351]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]DNA binding [GO:0003677]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; regulatory region DNA binding [GO:0000975]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription cofactor activity [GO:0003712]sFUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.Q9H0B6KLC2Kinesin light chain 2antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon cargo transport [GO:0008088]; blood coagulation [GO:0007596]; microtubule-based movement [GO:0007018]; small GTPase mediated signal transduction [GO:0007264]Ekinesin binding [GO:0019894]; microtubule motor activity [GO:0003777]ciliary rootlet [GO:0035253]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinesin I complex [GO:0016938]; membrane [GO:0016020]; microtubule [GO:0005874]; neuron projection [GO:0043005]; protein complex [GO:0043234]FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.Q8N3C0ASCC32Activating signal cointegrator 1 complex subunit 3cell proliferation [GO:0008283]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]rATP binding [GO:0005524]; ATP-dependent 3'-5' DNA helicase activity [GO:0043140]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]?FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3, enabling ALKHB3 to process alkylated N3-methylcytosine (3mC) within double-stranded regions. Enhances NF-kappa-B, SRF and AP1 transactivation. {ECO:0000269|PubMed:22055184}.O60232SSA27+Sjoegren syndrome/scleroderma autoantigen 1Acell division [GO:0051301]; mitotic nuclear division [GO:0007067]FUNCTION: Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies.P53367ARFP1 Arfaptin-1intracellular protein transport [GO:0006886]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; regulation of protein secretion [GO:0050708]5phosphatidylinositol-4-phosphate binding [GO:0070273]tcytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; trans-Golgi network membrane [GO:0032588]=FUNCTION: Putative target protein of ADP-ribosylation factor.Q15008PSMD6.26S proteasome non-ATPase regulatory subunit 6anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]ATPase activity [GO:0016887]cytosol [G< O:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.Q96MX6WDR92WD repeat-containing protein 92Gapoptotic process [GO:0006915]; histone lysine methylation [GO:0034968]'methylated histone binding [GO:0035064]RFUNCTION: Seems to act as a modulator of apoptosis. {ECO:0000269|PubMed:16487927}.P11172UMPS!Uridine 5'-monophosphate synthase Pyrimidine metabolismde novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; cellular response to drug [GO:0035690]; female pregnancy [GO:0007565]; lactation [GO:0007595]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; small molecule metabolic process [GO:0044281]; UMP biosynthetic process [GO:0006222]sorotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590]Q7Z5L2R3HCL-Coiled-coil domain-containing protein R3HCC1Lnucleotide binding [GO:0000166]P42566EPS15-Epidermal growth factor receptor substrate 15SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Recruited to the plasma membrane upon EGFR activation and localizes to coated pits. Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and in cytoplasmic juxtanuclear structures called aggresomes. {ECO:0000269|PubMed:16159959}.; SUBCELLULAR LOCATION: Isoform 2: Early endosome membrane {ECO:0000269|PubMed:18362181}; Peripheral membrane protein {ECO:0000269|PubMed:18362181}; Cytoplasmic side {ECO:0000269|PubMed:18362181}. Note=Colocalizes with HGS on bilayered clathrin coats on endosomes.cell proliferation [GO:0008283]; clathrin coat assembly [GO:0048268]; endocytic recycling [GO:0032456]; epidermal growth factor receptor signaling pathway [GO:0007173]; Golgi to endosome transport [GO:0006895]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; protein transport [GO:0015031]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; vesicle organization [GO:0016050]; viral entry into host cell [GO:0046718]Dcalcium ion binding [GO:0005509]; polyubiquitin binding [GO:0031593]1aggresome [GO:0016235]; AP-2 adaptor complex [GO:0030122]; ciliary membrane [GO:0060170]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. {ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:18362181, ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}.Q7Z3U7MON2Protein MON2 homologGolgi to endosome transport [GO:0006895]; positive regulation of GTPase activity [GO:0043547]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192];ARF guanyl-nucleotide exchange factor activity [GO:0005086]Dextracellular exosome [GO:0070062]; trans-Golgi network [GO:0005802]\FUNCTION: May be required for traffic between late Golgi and early endosomes. {ECO:0000250}.Q13492PICAL6Phosphatidylinositol-binding clathrin assembly proteinSUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus. Note=Colocalized with clathrin in the Golgi area. Interaction with FAM64A may target PICALM to the nucleus in some cells.$axonogenesis [GO:0007409]; cargo loading into vesicle [GO:0035459]; cell proliferation [GO:0008283]; clathrin coat assembly [GO:0048268]; clathrin-mediated endocytosis [GO:0072583]; dendrite morphogenesis [GO:0048813]; endosomal transport [GO:0016197]; hemopoiesis [GO:0030097]; iron ion homeostasis [GO:0055072]; iron ion import into cell [GO:0097459]; negative regulation of gene expression [GO:0010629]; negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902963]; negative regulation of receptor-mediated endocytosis [GO:0048261]; positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902961]; positive regulation of beta-amyloid formation [GO:1902004]; positive regulation of neuron death [GO:1901216]; positive regulation of transcription, DNA-templated [GO:0045893]; protein complex assembly [GO:0006461]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902959]; regulation of endocytosis [GO:0030100]; regulation of protein localization [GO:0032880]; synaptic vesicle maturation [GO:0016188]; vesicle-mediated transport [GO:0016192]1-phosphatidylinositol binding [GO:0005545]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neurofibrillary tangle [GO:0097418]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; vesicle [GO:0031982]FUNCTION: Assembly protein recruiting clathrin and adapter protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. {ECO:0000269|PubMed:10436022}.Q9H7D7WDR26WD repeat-containing protein 26>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378603}.JFUNCTION: May be involved in MAPK pathways. {ECO:0000269|PubMed:15378603}.P23258TBG1Tubulin gamma-1 chainvSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9566969}./cytoplasmic microtubule organization [GO:0031122]; G2/M transition of mitotic cell cycle [GO:0000086]; meiotic spindle organization [GO:0000212]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]apical part of cell [GO:0045177]; cell leading edge [GO:0031252]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; gamma-tubulin complex [GO:0000930]; nonmotile primary cilium [GO:0031513]; pericentriolar material [GO:0000242]; polar microtubule [GO:0005827]; recycling endosome [GO:0055037].FUNCTION: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.P62333PRS10#26S protease regulat< ory subunit 10Bqanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; proteasome-activating ATPase activity [GO:0036402]; protein binding, bridging [GO:0030674]; TBP-class protein binding [GO:0017025]]cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]O43324MCA34Eukaryotic translation elongation factor 1 epsilon-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15680327}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.)gene expression [GO:0010467]; negative regulation of cell proliferation [GO:0008285]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; tRNA aminoacylation for protein translation [GO:0006418];FUNCTION: Positive modulator of ATM response to DNA damage.P41252SYIC$Isoleucine--tRNA ligase, cytoplasmic=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7721108}.gene expression [GO:0010467]; isoleucyl-tRNA aminoacylation [GO:0006428]; osteoblast differentiation [GO:0001649]; tRNA aminoacylation for protein translation [GO:0006418]aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; GTPase binding [GO:0051020]; isoleucine-tRNA ligase activity [GO:0004822]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]A0JNW5UH1BLUHRF1-binding protein 1-likeQ69YQ0CYTSA Cytospin-ASUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21703590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21703590}. Cell junction, gap junction {ECO:0000269|PubMed:21703590}. Note=Colocalizes with acetylated alpha-tubulin, gamma-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microtubule organizing center.Ocell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]Gcytoplasm [GO:0005737]; gap junction [GO:0005921]; spindle [GO:0005819]FUNCTION: Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration. {ECO:0000269|PubMed:21703590}.A1A4S6RHG10 Rho GTPase-activating protein 10SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to cell membrane is dependent on PH domain. {ECO:0000250}.Mapoptotic process [GO:0006915]; cytoskeleton organization [GO:0007010]; negative regulation of apoptotic process [GO:0043066]; programmed cell death [GO:0012501]; regulation of apoptotic process [GO:0042981]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]`cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). {ECO:0000250}.Q9H1C3GL8D21Glycosyltransferase 8 domain-containing protein 2?transferase activity, transferring glycosyl groups [GO:0016757]+integral component of membrane [GO:0016021]P06756ITAVIntegrin alpha-VreceptorDSUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.Dangiogenesis [GO:0001525]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; calcium ion transmembrane transport [GO:0070588]; cell adhesion [GO:0007155]; cell growth [GO:0016049]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cell-substrate adhesion [GO:0031589]; endodermal cell differentiation [GO:0035987]; entry of symbiont into host cell by promotion of host phagocytosis [GO:0052066]; ERK1 and ERK2 cascade [GO:0070371]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; negative chemotaxis [GO:0050919]; negative regulation of entry of bacterium into host cell [GO:2000536]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of lipid storage [GO:0010888]; negative regulation of lipid transport [GO:0032369]; negative regulation of lipoprotein metabolic process [GO:0050748]; negative regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045715]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of osteoblast proliferation [GO:0033690]; regulation of apoptotic cell clearance [GO:2000425]; regulation of phagocytosis [GO:0050764]; substrate adhesion-dependent cell spreading [GO:0034446]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral entry into host cell [GO:0046718]Nextracellular matrix binding [GO:0050840]; extracellular matrix protein binding [GO:1990430]; fibronectin binding [GO:0< 001968]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; transforming growth factor beta binding [GO:0050431]; virus receptor activity [GO:0001618]; voltage-gated calcium channel activity [GO:0005245]valphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; integrin alphav-beta3 complex [GO:0034683]; integrin alphav-beta5 complex [GO:0034684]; integrin alphav-beta8 complex [GO:0034686]; integrin complex [GO:0008305]; lamellipodium membrane [GO:0031258]; membrane [GO:0016020]; microvillus membrane [GO:0031528]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.Q9BW92SYTM%Threonine--tRNA ligase, mitochondrial9SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.gene expression [GO:0010467]; mitochondrial threonyl-tRNA aminoacylation [GO:0070159]; tRNA aminoacylation for protein translation [GO:0006418]EATP binding [GO:0005524]; threonine-tRNA ligase activity [GO:0004829]!mitochondrial matrix [GO:0005759]P51648AL3A2Fatty aldehyde dehydrogenaseeSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side.:cellular aldehyde metabolic process [GO:0006081]; central nervous system development [GO:0007417]; epidermis development [GO:0008544]; oxidation-reduction process [GO:0055114]; peripheral nervous system development [GO:0007422]; phytol metabolic process [GO:0033306]; sesquiterpenoid metabolic process [GO:0006714]L3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD) activity [GO:0004029]; aldehyde dehydrogenase [NAD(P)+] activity [GO:0004030]; long-chain-alcohol oxidase activity [GO:0046577]; long-chain-aldehyde dehydrogenase activity [GO:0050061]; medium-chain-aldehyde dehydrogenase activity [GO:0052814]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; peroxisome [GO:0005777]QFUNCTION: Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. {ECO:0000269|PubMed:22633490}.O15160RPAC14DNA-directed RNA polymerases I and III subunit RPAC1RNA polymerasegene expression [GO:0010467]; innate immune response [GO:0045087]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of type I interferon production [GO:0032481]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase III transcription [GO:0006386]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase III promoter [GO:0006383]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]KDNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]cytosol [GO:0005829]; DNA-directed RNA polymerase I complex [GO:0005736]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleoplasm [GO:0005654]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}.Q12846STX4 Syntaxin-4fSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.:blood coagulation [GO:0007596]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; long-term synaptic potentiation [GO:0060291]; membrane organization [GO:0061024]; organelle fusion [GO:0048284]; platelet activation [GO:0030168]; positive regulation of catalytic activity [GO:0043085]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of eosinophil degranulation [GO:0043311]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of immunoglobulin secretion [GO:0051024]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of exocytosis [GO:0017157]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; response to hydroperoxide [GO:0033194]; SNARE complex assembly [GO:0035493]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; vesicle docking [GO:0048278]SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; sphingomyelin phosphodiesterase activator activity [GO:0016230]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; endomembrane system [GO:0012505]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; lamellipodium [GO:0030027]; lateral loop [GO:0043219]; membrane [GO:0016020]; myelin sheath adaxonal region [GO:0035749]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; somatodendritic compartment [GO:0036477]; specific granule [GO:0042581]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; trans-Golgi network [GO:0005802]; vacuole [GO:0005773]FUNCTION: Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes (By similarity). May also play a role in docking of synaptic vesicles at presynaptic active zones. {ECO:0000250}.Q7L014DDX46)Probable ATP-dependent RNA helicase DDX46 Complex CSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12234937}. Nucleus, Cajal body {ECO:0000269|PubMed:12234937}. Note=Present in Cajal bodies (CBs) and nuclear speckles.mRNA splicing, via spliceosome [GO:0000398]; regulation of gene expression [GO:0010468]; RNA secondary structure unwinding [GO:0010501]lATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]ICajal body [GO:0015030]; nuclear speck [GO:0016607]; nucleus [GO:0005634]FUNCTION: Plays an essential role in splicing, either prior to, or during splicing A complex formation. {ECO:0000269|PubMed:12234937}.Q7L2J0MEPCE(7SK snRNA methylphosphate capping enzyme8negative regulation of chromatin binding [GO:0035562]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of< G1/S transition of mitotic cell cycle [GO:1900087]; RNA methylation [GO:0001510]; snRNA metabolic process [GO:0016073]; snRNA modification [GO:0040031]poly(A) RNA binding [GO:0044822]; RNA methyltransferase activity [GO:0008173]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it. {ECO:0000269|PubMed:17643375}.Q9NYV4CDK12Cyclin-dependent kinase 12mSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Colocalized with nuclear speckles throughout interphase.mRNA processing [GO:0006397]; phosphorylation of RNA polymerase II C-terminal domain [GO:0070816]; protein autophosphorylation [GO:0046777]; regulation of MAP kinase activity [GO:0043405]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]cyclin K-CDK12 complex [GO:0002944]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors. {ECO:0000269|PubMed:11683387, ECO:0000269|PubMed:19651820, ECO:0000269|PubMed:20952539, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:24662513}.Q7Z4Q2HEAT3 HEAT repeat-containing protein 3Q8NC56LEMD2LEM domain-containing protein 2dSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM). Localized exclusively to the nuclear envelope, giving rise to a typical rim-like staining of the nuclear periphery.negative regulation of MAPK cascade [GO:0043409]; nuclear envelope organization [GO:0006998]; skeletal muscle cell differentiation [GO:0035914]ointegral component of nuclear inner membrane [GO:0005639]; membrane [GO:0016020]; nuclear membrane [GO:0031965]FUNCTION: Involved in nuclear structure organization (PubMed:16339967). Required for maintaining the integrity of the nuclear envelope (PubMed:17097643). {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643}.; FUNCTION: Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT. Required for myoblast differentiation involving regulation of ERK signaling (By similarity). {ECO:0000250|UniProtKB:Q6DVA0}.Q96DM3MIC1Uncharacterized protein C18orf8lysosomal membrane [GO:0005765]P23142FBLN1 Fibulin-1blood coagulation, fibrin clot formation [GO:0072378]; embryo implantation [GO:0007566]; extracellular matrix organization [GO:0030198]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell motility [GO:2000146]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; negative regulation of transformation of host cell by virus [GO:1904188]; negative regulation of transforming growth factor-beta secretion [GO:2001202]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of substrate-dependent cell migration, cell attachment to substrate [GO:1904237]; viral process [GO:0016032]^calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]; fibrinogen binding [GO:0070051]; fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; peptidase activator activity [GO:0016504]; protein complex binding [GO:0032403]; protein C-terminus binding [GO:0008022]basement membrane [GO:0005604]; elastic fiber [GO:0071953]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP. {ECO:0000269|PubMed:11792823, ECO:0000269|PubMed:9393974, ECO:0000269|PubMed:9466671}.Q9UL26RB22ARas-related protein Rab-22ASUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Early endosome. Cell projection, ruffle. Cytoplasmic vesicle. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.endocytosis [GO:0006897]; endosome organization [GO:0007032]; intracellular protein transport [GO:0006886]; Rab protein signal transduction [GO:0032482]; regulation of vesicle size [GO:0097494]PGDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]actin cytoskeleton [GO:0015629]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form. {ECO:0000269|PubMed:16537905, ECO:0000269|PubMed:21849477}.Q9BTD8RBM42RNA-binding protein 42SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Upon stress response, localizes with HNRNPK in cytoplasmic aggregates of stalled translational preinitiation complexes called stress granules. {ECO:0000250}.Bnegative regulation of mRNA splicing, via spliceosome [GO:0048025]gFUNCTION: Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA. {ECO:0000250}.O00567NOP56Nucleolar protein 56fSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000305}.<rRNA modification [GO:0000154]; rRNA processing [GO:0006364]Wpoly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; snoRNA binding [GO:0030515]box C/D snoRNP complex [GO:0031428]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; pre-snoRNP complex [GO:0070761]; small nucleolar ribonucleoprotein complex [GO:0005732]; small-subunit processome [GO:0032040]-FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribon< ucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs. {ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:15574333}.O94776MTA2"Metastasis-associated protein MTA2 Mi-2_NuRDkSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}.yATP-dependent chromatin remodeling [GO:0043044]; chromatin assembly or disassembly [GO:0006333]; chromatin organization [GO:0006325]; DNA methylation [GO:0006306]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of fibroblast migration [GO:0010762]chromatin binding [GO:0003682]; histone deacetylase activity [GO:0004407]; RNA polymerase II repressing transcription factor binding [GO:0001103]; RNA polymerase II transcription factor binding [GO:0001085]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding transcription factor activity [GO:0000989]; transcription regulatory region DNA binding [GO:0044212]; zinc ion binding [GO:0008270]histone deacetylase complex [GO:0000118]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; NuRD complex [GO:0016581]; protein complex [GO:0043234]; transcription factor complex [GO:0005667]FUNCTION: May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.Q05048CSTF1%Cleavage stimulation factor subunit 1^gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA cleavage [GO:0006379]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]}cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA.P16435NCPR NADPH--cytochrome P450 reductaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Anchored to the ER membrane by its N-terminal hydrophobic region.{carnitine metabolic process [GO:0009437]; cellular organofluorine metabolic process [GO:0090346]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to peptide hormone stimulus [GO:0071375]; demethylation [GO:0070988]; fatty acid oxidation [GO:0019395]; flavonoid metabolic process [GO:0009812]; internal peptidyl-lysine acetylation [GO:0018393]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of lipase activity [GO:0060192]; nitrate catabolic process [GO:0043602]; nitric oxide catabolic process [GO:0046210]; oxidation-reduction process [GO:0055114]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of monooxygenase activity [GO:0032770]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; regulation of growth plate cartilage chondrocyte proliferation [GO:0003420]; response to drug [GO:0042493]; response to nutrient [GO:0007584]Xcytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; electron carrier activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; hydrolase activity [GO:0016787]; iron-cytochrome-c reductase activity [GO:0047726]; iron ion binding [GO:0005506]; NADP binding [GO:0050661]; NADPH-hemoprotein reductase activity [GO:0003958]; nitric oxide dioxygenase activity [GO:0008941]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.Q9Y4K0LOXL2Lysyl oxidase homolog 2SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}. Nucleus. Chromosome. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, different reports confirmed the intracellular location and its key role in transcription regulation.aging [GO:0007568]; cell adhesion [GO:0007155]; cellular protein modification process [GO:0006464]; collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; histone modification [GO:0016570]; negative regulation of transcription, DNA-templated [GO:0045892]; oxidation-reduction process [GO:0055114]; positive regulation of chondrocyte differentiation [GO:0032332]; protein deamination [GO:0018277]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]; transcription, DNA-templated [GO:0006351]Achromatin binding [GO:0003682]; copper ion binding [GO:0005507]; electron carrier activity [GO:0009055]; methylated histone binding [GO:0035064]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720]; scavenger receptor activity [GO:0005044]; transcription corepressor activity [GO:0003714]basement membrane [GO:0005604]; chromosome [GO:0005694]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]AFUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3. Also involved in E-cadherin repression following hypoxia, a hallmark of epithelial to mesenchymal transition believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20026874, ECO:0000269|PubMed:21233336, ECO:0000269|PubMed:21732535, ECO:0000269|PubMed:21835952, ECO:0000269|PubMed:22483618}.O60306AQRIntron-binding protein aquarius Prp19(24)SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16949364}. Note=Localizes to speckle-like regions of the nucleoplasm. {ECO:0000269|PubMed:16949364}.+mRNA splicing, via spliceosome [GO:0000398]pcatalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]:FUNCTION: Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis. Plays a key role in position-dependent assembly of intron-encoded box C/D< small snoRNP, splicing being required for snoRNP assembly. May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing. {ECO:0000269|PubMed:16949364}.P26368U2AF2#Splicing factor U2AF 65 kDa subunitU2;gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of RNA splicing [GO:0033120]; regulation of mitochondrion degradation [GO:1903146]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]^enzyme binding [GO:0019899]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]Wnuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]FUNCTION: Necessary for the splicing of pre-mRNA. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:19470458, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:21536736}.O14578CTROCitron Rho-interacting kinasecytokinesis [GO:0000910]; dendrite development [GO:0016358]; generation of neurons [GO:0048699]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of dendrite morphogenesis [GO:0050774]; positive regulation of cytokinesis [GO:0032467]; small GTPase mediated signal transduction [GO:0007264]; spermatogenesis [GO:0007283]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]wactin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; membrane [GO:0016020]; ruffle [GO:0001726]; vacuole [GO:0005773]FUNCTION: Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:21457715}.O00267SPT5H$Transcription elongation factor SPT5<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10075709}.7-methylguanosine mRNA capping [GO:0006370]; cell cycle [GO:0007049]; chromatin remodeling [GO:0006338]; DNA-templated transcription, elongation [GO:0006354]; gene expression [GO:0010467]; negative regulation of DNA-templated transcription, elongation [GO:0032785]; negative regulation of mRNA polyadenylation [GO:1900364]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; response to organic substance [GO:0010033]; single stranded viral RNA replication via double stranded DNA intermediate [GO:0039692]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]IDSIF complex [GO:0032044]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]IFUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9514752, ECO:0000269|PubMed:9857195}.Q9Y2R4DDX52)Probable ATP-dependent RNA helicase DDX52GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.ZATP binding [GO:0005524]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]Cmembrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]Q86UE4LYRIC Protein LYRIC:SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain (By similarity). TNF-alpha causes translocation from the cytoplasm to the nucleus. {ECO:0000250}.,bicellular tight junction assembly [GO:0070830]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of angiogenesis [GO:0045766]; positive regulation of autophagy [GO:0010508]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein kinase B signaling [GO:0051897]double-stranded RNA binding [GO:0003725]; NF-kappaB binding [GO:0051059]; poly(A) RNA binding [GO:0044822]; RNA polymerase II transcription factor binding [GO:0001085]; transcription coactivator activity [GO:0003713]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:00059< 23]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intercellular canaliculus [GO:0046581]; nuclear body [GO:0016604]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]LFUNCTION: Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}.Q8N128F177AProtein FAM177A1Q9Y383LC7L2(Putative RNA-binding protein Luc7-like 2SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Colocalizes with SCNM1 and SNRNP70 in nuclear speckles. {ECO:0000250}.'mRNA splice site selection [GO:0006376]Xenzyme binding [GO:0019899]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]1nuclear speck [GO:0016607]; U1 snRNP [GO:0005685]6FUNCTION: May bind to RNA via its Arg/Ser-rich domain.Q9BTC0DIDO1Death-inducer obliterator 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00651}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23831028}. Note=Translocates to the nucleus after pro-apoptotic stimuli (By similarity). Translocates to the mitotic spindle upon loss of interaction with H3K4me3 during early mitosis. {ECO:0000250}.Sapoptotic signaling pathway [GO:0097190]; transcription, DNA-templated [GO:0006351]Bcytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle [GO:0005819]hFUNCTION: Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. Required for early embryonic stem cell development. {ECO:0000250, ECO:0000269|PubMed:16127461}.; FUNCTION: Isoform 2: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes. {ECO:0000269|PubMed:16127461}.O00462MANBABeta-mannosidaseglycosidases(16) Glycan metabolismSUBCELLULAR LOCATION: Lysosome.carbohydrate metabolic process [GO:0005975]; cellular protein modification process [GO:0006464]; mannan catabolic process [GO:0046355]Dbeta-mannosidase activity [GO:0004567]; mannose binding [GO:0005537]Lintracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides.Q9H8Y8GORS2#Golgi reassembly-stacking protein 2dSUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor. Membrane; Peripheral membrane protein.Dmitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]PGolgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020][FUNCTION: Plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after mitotic breakdown. May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA. {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:21515684}.P50402EMDEmerinSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.5cellular response to growth factor stimulus [GO:0071363]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mitotic nuclear envelope reassembly [GO:0007084]; muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; negative regulation of catenin import into nucleus [GO:0035414]; negative regulation of fibroblast proliferation [GO:0048147]; positive regulation of protein export from nucleus [GO:0046827]; regulation of canonical Wnt signaling pathway [GO:0060828]; skeletal muscle cell differentiation [GO:0035914]=actin binding [GO:0003779]; beta-tubulin binding [GO:0048487]endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; microtubule [GO:0005874]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]uFUNCTION: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}.A2RRP1NBAS Neuroblastoma-amplified sequenceSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20577004}. Endoplasmic reticulum {ECO:0000269|PubMed:19369418}. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000305}.negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; nuclear-transcribed mRNA catabolic process [GO:0000956]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]cytoplasm [GO:0005737]; Dsl1p complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]FUNCTION: Involved in Golgi-to-endoplasmic reticulum (ER) retrograde tranport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). {ECO:0000269|PubMed:19369418, ECO:0000305}.P61289PSME3&Proteasome activator complex subunit 3/SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10657252, ECO:0000269|PubMed:12629132}. Cytoplasm {ECO:0000250}. Note=Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase. {ECO:0000250}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of ubiquitin< -protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of endopeptidase activity [GO:0010950]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]endopeptidase activator activity [GO:0061133]; identical protein binding [GO:0042802]; MDM2/MDM4 family protein binding [GO:0097371]; p53 binding [GO:0002039]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome activator complex [GO:0008537]; proteasome complex [GO:0000502]KFUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (PubMed:25361978). {ECO:0000269|PubMed:10835274, ECO:0000269|PubMed:11185562, ECO:0000269|PubMed:11432824, ECO:0000269|PubMed:15111123, ECO:0000269|PubMed:18309296, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:9325261}.O15439MRP4)Multidrug resistance-associated protein 4Bile secretion<SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.blood coagulation [GO:0007596]; oxidation-reduction process [GO:0055114]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; transmembrane transport [GO:0055085]15-hydroxyprostaglandin dehydrogenase (NAD+) activity [GO:0016404]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]basolateral plasma membrane [GO:0016323]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088]KFUNCTION: May be an organic anion pump relevant to cellular detoxification.Q96AE7TTC17#Tetratricopeptide repeat protein 17SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24475127}. Cell membrane {ECO:0000269|PubMed:24475127}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24475127}. Note=Colocalized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions.Lactin filament polymerization [GO:0030041]; cilium organization [GO:0044782]Uactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]qFUNCTION: Plays a role in primary ciliogenesis by modulating actin polymerization. {ECO:0000269|PubMed:24475127}.P50613CDK7Cyclin-dependent kinase 7SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides.7-methylguanosine mRNA capping [GO:0006370]; androgen receptor signaling pathway [GO:0030521]; cell cycle arrest [GO:0007050]; cell division [GO:0051301]; cell proliferation [GO:0008283]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]|androgen receptor binding [GO:0050681]; ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; DNA-dependent ATPase activity [GO:0008094]; protein C-terminus binding [GO:0008022]; protein kinase activity [GO:0004672]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; holo TFIIH complex [GO:0005675]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261, ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234, ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461, ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:9372954, ECO:0000269|PubMed:9840937}.O00422SAP18)Histone deacetylase complex subunit SAP18Sin3SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus speckle. Note=Shuttles between the nucleus and the cytoplasm. Colocalizes with ACIN1 and SRSF2 in nuclear speckles.tchromatin organization [GO:0006325]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of nucleic acid-templated transcription [GO:1903507]; positive< regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]Qpoly(A) RNA binding [GO:0044822]; transcription corepressor activity [GO:0003714]ASAP complex [GO:0061574]; cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]WFUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. {ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:9150135}.Q5SY16NOL9&Polynucleotide 5'-hydroxyl-kinase NOL9SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:21063389}. Note=Colocalizes with pre-60S rRNP particles.cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; maturation of 5.8S rRNA [GO:0000460]; RNA processing [GO:0006396]kATP binding [GO:0005524]; polynucleotide 5'-hydroxyl-kinase activity [GO:0051731]; RNA binding [GO:0003723]HFUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA. {ECO:0000269|PubMed:21063389}.Q86SQ7SDCG8,Serologically defined colon cancer antigen 8 SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cell junction. Note=Located at the distal ends of both centrioles and colocalizes to centrosomes throughout the cell cycle.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.establishment of cell polarity [GO:0030010]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule organizing center organization [GO:0031023]; mitotic cell cycle [GO:0000278]; neuron migration [GO:0001764]; organelle organization [GO:0006996]; tube formation [GO:0035148]cell-cell junction [GO:0005911]; centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]FUNCTION: Plays a role in the establishment of cell polarity and epithelial lumen formation (By similarity). May play a role in ciliogenesis. {ECO:0000250|UniProtKB:Q80UF4}.Q9UK61F208AProtein FAM208ASUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26022416}. Chromosome {ECO:0000269|PubMed:26022416}. Note=Localizes to chromatin. {ECO:0000269|PubMed:26022416}.mFUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. {ECO:0000269|PubMed:26022416}.O15031PLXB2 Plexin-B2 Development Axon guidanceSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12533544}; Single-pass type I membrane protein {ECO:0000269|PubMed:12533544}.brain development [GO:0007420]; neural tube closure [GO:0001843]; neuroblast proliferation [GO:0007405]; positive regulation of axonogenesis [GO:0050772]; regulation of cell shape [GO:0008360]; regulation of GTPase activity [GO:0043087]; regulation of neuron migration [GO:2001222]; regulation of protein phosphorylation [GO:0001932]; semaphorin-plexin signaling pathway [GO:0071526])semaphorin receptor activity [GO:0017154]qcell surface [GO:0009986]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling. Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development. Regulates the migration of cerebellar granule cells in the developing brain. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May modulate the activity of RAC1 and CDC42. Down-regulates macrophage migration in wound-healing assays (in vitro) (By similarity). {ECO:0000250}.Q03252LMNB2Lamin-B2OSUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor; Nucleoplasmic side.@lamin filament [GO:0005638]; nuclear inner membrane [GO:0005637]FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.O95573ACSL3#Long-chain-fatty-acid--CoA ligase 3SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.brain development [GO:0007420]; cellular lipid metabolic process [GO:0044255]; fatty acid biosynthetic process [GO:0006633]; long-chain fatty acid import [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of Golgi to plasma membrane protein transport [GO:0042998]; positive regulation of phosphatidylcholine biosynthetic process [GO:2001247]; positive regulation of secretion [GO:0051047]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; very-low-density lipoprotein particle assembly [GO:0034379]ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]Jendoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778],FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). Has mainly an anabolic role in energy metabolism. Requ< ired for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). {ECO:0000250, ECO:0000269|PubMed:18003621}.Q13868EXOS2Exosome complex component RRP4=SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus.CUT catabolic process [GO:0071034]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; gene expression [GO:0010467]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription [GO:0071049]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; positive regulation of cell growth [GO:0030307]; rRNA processing [GO:0006364]; U4 snRNA 3'-end processing [GO:0034475]H3'-5'-exoribonuclease activity [GO:0000175]; 7S RNA binding [GO:0008312]cytoplasm [GO:0005737]; cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7. {ECO:0000269|PubMed:17545563}.Q9NWH9SLTM!SAFB-like transcription modulatoraSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Detected in punctate structures. {ECO:0000250}.apoptotic process [GO:0006915]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]nucleoplasm [GO:0005654]}FUNCTION: When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis. {ECO:0000250}.Q9BUJ2HNRL18Heterogeneous nuclear ribonucleoprotein U-like protein 1uSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11513728, ECO:0000269|PubMed:12489984, ECO:0000269|PubMed:9733834}.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; regulation of transcription, DNA-templated [GO:0006355]; response to virus [GO:0009615]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]Wenzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]Vnucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro. {ECO:0000269|PubMed:12489984, ECO:0000269|PubMed:9733834}.Q96HD1CREL1,Cysteine-rich with EGF-like domain protein 1 GlycoproteinXSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.Ucardiac septum development [GO:0003279]; endocardial cushion development [GO:0003197]Q9NXH9TRM1+tRNA (guanine(26)-N(2))-dimethyltransferase(tRNA N2-guanine methylation [GO:0002940]metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; tRNA (guanine-N2-)-methyltransferase activity [GO:0004809]; tRNA binding [GO:0000049]0mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.Q9BY50SC11C1Signal peptidase complex catalytic subunit SEC11CProtein exprotSUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; regulation of insulin secretion [GO:0050796]; signal peptide processing [GO:0006465]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]+serine-type peptidase activity [GO:0008236]FUNCTION: Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. {ECO:0000250}.Q9P0M6H2AWCore histone macro-H2A.2SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin.brain development [GO:0007420]; chromatin modification [GO:0016568]; dosage compensation [GO:0007549]; establishment of protein localization to chromatin [GO:0071169]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter [GO:1901837]; nucleosome assembly [GO:0006334]; positive regulation of keratinocyte differentiation [GO:0045618]chromatin DNA binding [GO:0031490]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; transcription regulatory region DNA binding [GO:0044212]Barr body [GO:0001740]; extracellular exosome [GO:0070062]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]gFUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in stable X chromosome inactivation. {ECO:0000269|PubMed:15621527}.Q8IYB8SUV31ATP-dependent RNA helicase SUPV3L1, mitochondrialbSUBCELLULAR LOCATION: Nucleus. Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.Schromatin maintenance [GO:0070827]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; mitochondrial mRNA catabolic process [GO:0000958]; mitochondrial mRNA surveillance [GO:0035946]; mitochondrial ncRNA surveillance [GO:0035945]; mitochondri< al RNA 3'-end processing [GO:0000965]; mitochondrial RNA surveillance [GO:2000827]; mitochondrion morphogenesis [GO:0070584]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell growth [GO:0030307]; positive regulation of mitochondrial RNA catabolic process [GO:0000962]; RNA catabolic process [GO:0006401]h3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]mitochondrial degradosome [GO:0045025]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA. {ECO:0000269|PubMed:12466530, ECO:0000269|PubMed:15096047, ECO:0000269|PubMed:17352692, ECO:0000269|PubMed:17961633, ECO:0000269|PubMed:18678873, ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:19864255}.Q12996CSTF3%Cleavage stimulation factor subunit 3Agene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA cleavage [GO:0006379]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]UmRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]nFUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs.Q86T03TM55B:Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphataseSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16365287}; Multi-pass membrane protein {ECO:0000269|PubMed:16365287}. Lysosome membrane {ECO:0000269|PubMed:16365287}; Multi-pass membrane protein {ECO:0000269|PubMed:16365287}.3phosphatidylinositol dephosphorylation [GO:0046856]Iphosphatidylinositol-4,5-bisphosphate 4-phosphatase activity [GO:0034597]qintegral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate. {ECO:0000269|PubMed:16365287}.Q9Y276BCS1Mitochondrial chaperone BCS1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:9878253}; Single-pass membrane protein {ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:9878253}.mitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrial respiratory chain complex III assembly [GO:0034551]; mitochondrial respiratory chain complex IV assembly [GO:0033617]; mitochondrion organization [GO:0007005]Tmitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] FUNCTION: Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. {ECO:0000269|PubMed:18628306}.O14828SCAM3/Secretory carrier-associated membrane protein 3zpost-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; response to retinoic acid [GO:0032526]lextracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]fFUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.Q9Y2S7PDIP2&Polymerase delta-interacting protein 2(mitochondrion morphogenesis [GO:0070584]Umitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]Q9BV10ALG12>Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferasenSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.Kcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]alpha-1,6-mannosyltransferase activity [GO:0000009]; dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity [GO:0052917]; mannosyltransferase activity [GO:0000030]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.Q08380LG3BPGalectin-3-binding proteinTSUBCELLULAR LOCATION: Secreted. Secreted, extracellular space, extracellular matrix.cell adhesion [GO:0007155]; cellular defense response [GO:0006968]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165](scavenger receptor activity [GO:0005044]blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Promotes intergrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells. {ECO:0000269|PubMed:11146440, ECO:0000269|PubMed:8034587, ECO:0000269|PubMed:9501082}.Q7Z388D19L4&Probable C-mannosyltransferase DPY19L4Nprotein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan [GO:0018406])mannosyltransferase activity [GO:0000030]Pintegral component of membrane [GO:0016021]; nuclear inner membrane [GO:0005637]FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. {ECO:0000250}.Q9GZP9DERL2Derlin-2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}; Multi-pass membrane protein {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}.endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; positive regulation of cell growth [GO:0030307]; positive regulation of cell proliferation [GO:0008284]; retrograde protein transport, ER to cytosol [GO:0030970]; suckling behavior [GO:0001967]early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; late endosome [GO:0005770]; membrane [GO:0016020]FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. < In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}.P55265DSRAD0Double-stranded RNA-specific adenosine deaminaseKSUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and nucleus.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Predominantly nuclear but can shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear import whereas XPO1 can mediate its nuclear export.{adenosine to inosine editing [GO:0006382]; base conversion or substitution editing [GO:0016553]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; definitive hemopoiesis [GO:0060216]; erythrocyte differentiation [GO:0030218]; gene expression [GO:0010467]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell homeostasis [GO:0061484]; innate immune response [GO:0045087]; in utero embryonic development [GO:0001701]; miRNA loading onto RISC involved in gene silencing by miRNA [GO:0035280]; mRNA modification [GO:0016556]; mRNA processing [GO:0006397]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein kinase activity by regulation of protein phosphorylation [GO:0044387]; negative regulation of RNA interference [GO:1900369]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; negative regulation of viral genome replication [GO:0045071]; osteoblast differentiation [GO:0001649]; positive regulation of viral genome replication [GO:0045070]; pre-miRNA processing [GO:0031054]; protein export from nucleus [GO:0006611]; protein import into nucleus [GO:0006606]; response to interferon-alpha [GO:0035455]; response to virus [GO:0009615]; somatic diversification of immune receptors via somatic mutation [GO:0002566]; type I interferon signaling pathway [GO:0060337]DNA binding [GO:0003677]; double-stranded RNA adenosine deaminase activity [GO:0003726]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supraspliceosomal complex [GO:0044530]@ FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874, ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222}.Q12849GRSF1G-rich sequence factor 1SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion matrix, mitochondrion nucleoid. Note=Forms granules that colocalize with foci of newly synthesized mtRNA next to mitochondrial nucleoids.anterior/posterior pattern specification [GO:0009952]; morphogenesis of embryonic epithelium [GO:0016331]; mRNA polyadenylation [GO:0006378]; tRNA processing [GO:0008033]vmRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]Wcytoplasm [GO:0005737]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences. {ECO:0000269|PubMed:23473033, ECO:0000269|PubMed:23473034}.P61006RAB8ARas-related protein Rab-8APancreatic secretionSSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus. Recycling endosome membrane. Cell projection, cilium. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis.axonogenesis [GO:0007409]; cellular response to insulin stimulus [GO:0032869]; cilium assembly [GO:0042384]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi vesicle fusion to target membrane [GO:0048210]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0017157]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of protein transport [GO:0051223]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking involved in exocytosis [GO:0006904]GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin V binding [GO:0031489]; Rab GTPase binding [GO:0017137]centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; neuronal cell body [GO:< 0043025]; nonmotile primary cilium [GO:0031513]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; primary cilium [GO:0072372]; recycling endosome membrane [GO:0055038]; secretory granule membrane [GO:0030667]; synaptic vesicle [GO:0008021]; trans-Golgi network transport vesicle [GO:0030140]YFUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. Plays an important role in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis. {ECO:0000269|PubMed:20890297, ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:21844891}.Q9NXG6P4HTM"Transmembrane prolyl 4-hydroxylaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031}; Single-pass type II membrane protein {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031}.6regulation of erythrocyte differentiation [GO:0045646]5calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. {ECO:0000269|PubMed:17726031}.P21964COMTCatechol O-methyltransferaseSteroid hormone biosynthesisSUBCELLULAR LOCATION: Isoform Soluble: Cytoplasm.; SUBCELLULAR LOCATION: Isoform Membrane-bound: Cell membrane; Single-pass type II membrane protein; Extracellular side {ECO:0000269|PubMed:21846718}.cellular response to phosphate starvation [GO:0016036]; developmental process [GO:0032502]; dopamine catabolic process [GO:0042420]; estrogen metabolic process [GO:0008210]; female pregnancy [GO:0007565]; learning [GO:0007612]; methylation [GO:0032259]; multicellular organismal reproductive process [GO:0048609]; negative regulation of dopamine metabolic process [GO:0045963]; negative regulation of renal sodium excretion [GO:0035814]; negative regulation of smooth muscle cell proliferation [GO:0048662]; neurotransmitter biosynthetic process [GO:0042136]; neurotransmitter catabolic process [GO:0042135]; positive regulation of homocysteine metabolic process [GO:0050668]; regulation of sensory perception of pain [GO:0051930]; response to drug [GO:0042493]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to pain [GO:0048265]; short-term memory [GO:0007614]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; xenobiotic metabolic process [GO:0006805]catechol O-methyltransferase activity [GO:0016206]; magnesium ion binding [GO:0000287]; O-methyltransferase activity [GO:0008171]#axon [GO:0030424]; cell body [GO:0044297]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.O14672ADA10>Disintegrin and metalloproteinase domain-containing protein 10NotchSecretase Complex(6)/ADAMs(4)#SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Note=Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi.axon guidance [GO:0007411]; cell-cell signaling [GO:0007267]; collagen catabolic process [GO:0030574]; constitutive protein ectodomain proteolysis [GO:0051089]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; in utero embryonic development [GO:0001701]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte activation [GO:0042117]; negative regulation of cell adhesion [GO:0007162]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; PMA-inducible membrane protein ectodomain proteolysis [GO:0051088]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of T cell chemotaxis [GO:0010820]; protein phosphorylation [GO:0006468]; response to tumor necrosis factor [GO:0034612])endopeptidase activity [GO:0004175]; integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; receptor binding [GO:0005102]; zinc ion binding [GO:0008270]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; tetraspanin-enriched microdomain [GO:0097197]FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling. {ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905, ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900}.O43660PLRG1Pleiotropic regulator 1Igene expression [GO:0010467]; mRNA splicing, via spliceosome [GO< :0000398]; negative regulation of nucleic acid-templated transcription [GO:1903507]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; protein localization to nucleus [GO:0034504]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]ucatalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000250}.Q8NCH0CHSTE Carbohydrate sulfotransferase 14qSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.bcarbohydrate biosynthetic process [GO:0016051]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; dermatan sulfate proteoglycan metabolic process [GO:0050655]; glycosaminoglycan metabolic process [GO:0030203]; small molecule metabolic process [GO:0044281]dN-acetylgalactosamine 4-O-sulfotransferase activity [GO:0001537]; phosphate ion binding [GO:0042301]FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. GlcUA to IdoUA. Appears to have an important role in the formation of the cerbellar neural network during postnatal brain development. {ECO:0000269|PubMed:19661164}.Q8TCT7SPP2B Signal peptide peptidase-like 2BSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829952}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:17965014}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}. Note=targeted through the entire secretory pathway to endosomes/lysosomes (PubMed:15998642). {ECO:0000269|PubMed:15998642}.membrane protein ectodomain proteolysis [GO:0006509]; membrane protein intracellular domain proteolysis [GO:0031293]; membrane protein proteolysis [GO:0033619]; regulation of immune response [GO:0050776]taspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; protein homodimerization activity [GO:0042803]Nendosome membrane [GO:0010008]; Golgi-associated vesicle membrane [GO:0030660]; integral component of cytoplasmic side of endoplasmic reticulum membrane [GO:0071458]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17965014, PubMed:19114711, PubMed:22194595). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952, PubMed:16829951). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus processed leader peptide gp18 of the envelope glycoprotein gp130 dependently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:17965014, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:22194595, ECO:0000269|PubMed:23132852}.P40692MLH1 DNA mismatch repair protein Mlh1Mismatch excision repair (MMR)YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842}.DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; female meiosis chromosome segregation [GO:0016321]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; isotype switching [GO:0045190]; male meiosis chromosome segregation [GO:0007060]; meiotic metaphase I plate congression [GO:0043060]; meiotic spindle midzone assembly [GO:0051257]; mismatch repair [GO:0006298]; negative regulation of mitotic recombination [GO:0045950]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; oogenesis [GO:0048477]; resolution of meiotic recombination intermediates [GO:0000712]; somatic hypermutation of immunoglobulin genes [GO:0016446]; spermatogenesis [GO:0007283]; synapsis [GO:0007129][ATPase activity [GO:0016887]; ATP binding [GO:0005524]; mismatched DNA binding [GO:0030983]chiasma [GO:0005712]; male germ cell nucleus [GO:0001673]; membrane [GO:0016020]; MutLalpha complex [GO:0032389]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]FUNCTION: Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis. {ECO:0000269|PubMed:16873062, ECO:0000269|PubMed:18206974}.Q7L1W4LRC8D-Volume-regulated anion channel subunit LRRC8DISUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24782309}; Multi-pass membrane protein {ECO:0000269|PubMed:24782309}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24782309}; Multi-pass membrane protein {ECO:0000269|PubMed:24782309}. Note=Mainly localizes in the endoplasmic reticulum. {ECO:0000269|PubMed:24782309}.ion transport [GO:0006811]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]BFUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8D constitutes a pore-forming subunit or whether it is closely associated with the pore (By similarity). Mediates the import of the antibiotic blasticidin-S into cell (PubMed:24782309). {ECO:0000250, ECO:0000269|PubMed:24782309}.Q8TED1GPX8!Probable glutathione peroxidase 8YSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.0response to reactive oxygen species [GO:0000302]Nglutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]Uendoplasmic reticulum lumen [GO:0005788]; inte< gral component of membrane [GO:0016021]Q92805GOGA1Golgin subfamily A member 1SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:9324025}; Peripheral membrane protein {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:9324025}.'protein targeting to Golgi [GO:0000042]Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; trans-Golgi network [GO:0005802]YFUNCTION: Probably involved in maintaining Golgi structure. {ECO:0000269|PubMed:9324025}.Q969N2PIGT GPI transamidase component PIG-T Glycolipid biosynthesisSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Single-pass type I membrane protein {ECO:0000269|PubMed:11483512}.attachment of GPI anchor to protein [GO:0016255]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; post-translational protein modification [GO:0043687]-GPI-anchor transamidase activity [GO:0003923]cytoplasmic membrane-bounded vesicle [GO:0016023]; endoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]FUNCTION: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates. {ECO:0000269|PubMed:11483512}.Q9BV81EMC6%ER membrane protein complex subunit 6xSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22119785}; Multi-pass membrane protein {ECO:0000269|PubMed:22119785}.Zautophagosome assembly [GO:0000045]; protein folding in endoplasmic reticulum [GO:0034975]ER membrane protein complex [GO:0072546]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; integral component of omegasome membrane [GO:0097631]Q7KYR7BT2A1"Butyrophilin subfamily 2 member A1`SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.$lipid metabolic process [GO:0006629]Vextracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]O14653GOSR2$Golgi SNAP receptor complex member 2SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus (By similarity). {ECO:0000250}.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi to vacuole transport [GO:0006896]; intra-Golgi vesicle-mediated transport [GO:0006891]; IRE1-mediated unfolded protein response [GO:0036498]; membrane fusion [GO:0061025]; protein targeting to vacuole [GO:0006623]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion with Golgi apparatus [GO:0048280]bSNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; transporter activity [GO:0005215] endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; SNARE complex [GO:0031201]aFUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.P50336PPOXProtoporphyrinogen oxidaseSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.Vheme biosynthetic process [GO:0006783]; oxidation-reduction process [GO:0055114]; porphyrin-containing compound biosynthetic process [GO:0006779]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to drug [GO:0042493]; small molecule metabolic process [GO:0044281]sflavin adenine dinucleotide binding [GO:0050660]; oxygen-dependent protoporphyrinogen oxidase activity [GO:0004729]integral component of mitochondrial inner membrane [GO:0031305]; intrinsic component of mitochondrial inner membrane [GO:0031304]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000269|PubMed:21048046, ECO:0000269|PubMed:23467411, ECO:0000269|PubMed:7713909}.O94808GFPT2@Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; energy reserve metabolic process [GO:0006112]; fructose 6-phosphate metabolic process [GO:0006002]; glutamine metabolic process [GO:0006541]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047]FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.Q15853USF2Upstream stimulatory factor 2lactation [GO:0007595]; late viral transcription [GO:0019086]; lipid homeostasis [GO:0055088]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]; regulation of transcription from RNA polymerase II promoter by glucose [GO:0000430]; transcription from RNA polymerase II promoter [GO:0006366]rbHLH transcription factor binding [GO:0043425]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.Q6P1Q0LTMD1!LETM1 domain-containing protein 1SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17943721, ECO:0000269|PubMed:18045496}; Single-pass membrane protein {ECO:0000269|PubMed:17943721, ECO:0000269|PubMed:18045496}.Vintegral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]|FUNCTION: Involved in tumorigenesis and may function as a negative regulator of the p53/TP53. {ECO:0000269|PubMed:12879013}.Q6UXV4MIC27MICOS complex subunit MIC27SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979}; Multi-pass membrane protein {ECO:0000269|PubMed:23704930}. Mitochondrion {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.6MICOS complex [GO:0061617]; mitochondrion [GO:0005739] FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol. Plays a crucial role in crista junction formation and mitochondrial function (PubMed:23704930), (PubMed:25764979). {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979}.Q8NHQ8RASF8+Ras association domain-containing protein 8Q09666AHNK3Neuroblast differentiation-associated protein AHNAKprotein oligomerization [GO:0051259]; regulation of RNA splicing [GO:0043484]; regulation of v< oltage-gated calcium channel activity [GO:1901385]poly(A) RNA binding [GO:0044822]; S100 protein binding [GO:0044548]; structural molecule activity conferring elasticity [GO:0097493]}actin cytoskeleton [GO:0015629]; cell-cell contact zone [GO:0044291]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]; vesicle [GO:0031982]<FUNCTION: May be required for neuronal cell differentiation.Q14151SAFB2Scaffold attachment factor B2DNA binding [GO:0003677]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.Q9Y6Y9LY96Lymphocyte antigen 96LPS(G-)4SUBCELLULAR LOCATION: Secreted, extracellular space.activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular defense response [GO:0006968]; detection of lipopolysaccharide [GO:0032497]; extrinsic apoptotic signaling pathway [GO:0097191]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; programmed cell death [GO:0012501]; response to lipopolysaccharide [GO:0032496]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]Scoreceptor activity [GO:0015026]; lipopolysaccharide receptor activity [GO:0001875]endosome membrane [GO:0010008]; extracellular space [GO:0005615]; lipopolysaccharide receptor complex [GO:0046696]; plasma membrane [GO:0005886]BFUNCTION: Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both MD2 and TLR4, but not TLR4 alone, respond to LPS.Q9UQ88CD11ACyclin-dependent kinase 11Aapoptotic process [GO:0006915]; mitotic nuclear division [GO:0007067]; protein phosphorylation [GO:0006468]; regulation of cell growth [GO:0001558]; regulation of mRNA processing [GO:0050684]; regulation of transcription, DNA-templated [GO:0006355]ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]rFUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression. {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}.Q9NZJ7MTCH1Mitochondrial carrier homolog 1lSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; neuronal ion channel clustering [GO:0045161]; positive regulation of apoptotic process [GO:0043065]; regulation of signal transduction [GO:0009966]; transport [GO:0006810]integral component of membrane [GO:0016021]; intracellular [GO:0005622]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]kFUNCTION: Potential mitochondrial transporter. May play a role in apoptosis. {ECO:0000269|PubMed:12377771}.P98179RBM3Putative RNA-binding protein 3SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA granules in dentrites. {ECO:0000250}.positive regulation of translation [GO:0045727]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; regulation of translation [GO:0006417]; response to cold [GO:0009409]; RNA processing [GO:0006396]; translation [GO:0006412]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; ribosomal large subunit binding [GO:0043023]; RNA binding [GO:0003723]Ccytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleus [GO:0005634]GFUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation (By similarity). {ECO:0000250}.Q9HD20AT131"Manganese-transporting ATPase 13A1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24392018}; Multi-pass membrane protein {ECO:0000269|PubMed:24392018}.cation transport [GO:0006812]VATPase activity [GO:0016887]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]oendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis. {ECO:0000269|PubMed:24392018}.Q8WVQ1CANT1(Soluble calcium-activated nucleotidase 1?SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12234496}; Single-pass type II membrane protein {ECO:0000269|PubMed:12234496}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12234496}; Single-pass type II membrane protein {ECO:0000269|PubMed:12234496}. Note=Processed form: Secreted.positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; proteoglycan biosynthetic process [GO:0030166]; signal transduction [GO:0007165]vcalcium ion binding [GO:0005509]; signal transducer activity [GO:0004871]; uridine-diphosphatase activity [GO:0045134]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]qFUNCTION: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis. {ECO:0000269|PubMed:12234496, ECO:0000269|PubMed:15248776, ECO:0000269|PubMed:22539336}.Q9UMX5NENFNeudesinBSUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.^negative regulation of appetite [GO:0032099]; positive regulation of MAPK cascade [GO:0043410]9heme binding [GO:0020037]; metal ion binding [GO:0046872]endomembrane system [GO:0012505]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]fFUNCTION: Acts as a neurotrophic factor in postnatal mature neurons enhancing neuronal survival. Promotes cell proliferation and neurogenesis in undifferentiated neural pro-genitor cells at the embryonic stage and inhibits differentiation of astrocyte. Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways. Neurotrophic activity is enhanced by binding to heme. Acts also as an anorexigenic neurotrophic factor that contributes to energy balance< (By similarity). Plays a role in the human tumorigenesis (PubMed:22748190). {ECO:0000250|UniProtKB:Q9CQ45, ECO:0000269|PubMed:22748190}.Q9BUQ8DDX23)Probable ATP-dependent RNA helicase DDX23U5XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:9409622}. cis assembly of pre-catalytic spliceosome [GO:0000354]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA secondary structure unwinding [GO:0010501]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]catalytic step 2 spliceosome [GO:0071013]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; U5 snRNP [GO:0005682]FUNCTION: Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. {ECO:0000269|PubMed:18425142}.Q9NV31IMP31U3 small nucleolar ribonucleoprotein protein IMP3GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12655004}.rRNA processing [GO:0006364]=poly(A) RNA binding [GO:0044822]; snoRNA binding [GO:0030515]oMpp10 complex [GO:0034457]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. {ECO:0000269|PubMed:12655004}.Q9Y2Z2MTO1#Protein MTO1 homolog, mitochondrial;mitochondrial tRNA wobble uridine modification [GO:0070899]Rflavin adenine dinucleotide binding [GO:0050660]; poly(A) RNA binding [GO:0044822]FUNCTION: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. {ECO:0000269|PubMed:12011058}.Q96KA5CLP1L9Cleft lip and palate transmembrane protein 1-like proteincFUNCTION: Enhances cisplatin-mediated apoptosis, when overexpressed. {ECO:0000269|PubMed:11162647}.O14925TIM23=Mitochondrial import inner membrane translocase subunit Tim23|SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25997101}; Multi-pass membrane protein {ECO:0000255}.cellular protein metabolic process [GO:0044267]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]yP-P-bond-hydrolysis-driven protein transmembrane transporter activity [GO:0015450]; protein channel activity [GO:0015266]integral component of mitochondrial inner membrane [GO:0031305]; mitochondrial inner membrane [GO:0005743]; mitochondrial inner membrane presequence translocase complex [GO:0005744]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.P46100ATRXTranscriptional regulator ATRX~SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body. Note=Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with CBX5/HP1 alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at the maternal H19 ICR (By similarity). {ECO:0000250}.+cellular response to hydroxyurea [GO:0072711]; chromatin remodeling [GO:0006338]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA duplex unwinding [GO:0032508]; DNA methylation [GO:0006306]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication-independent nucleosome assembly [GO:0006336]; forebrain development [GO:0030900]; multicellular organism growth [GO:0035264]; negative regulation of telomeric RNA transcription from RNA pol II promoter [GO:1901581]; nucleosome assembly [GO:0006334]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; positive regulation of telomere maintenance [GO:0032206]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-embryonic forelimb morphogenesis [GO:0035128]; regulation of transcription, DNA-templated [GO:0006355]; replication fork processing [GO:0031297]; seminiferous tubule development [GO:0072520]; Sertoli cell development [GO:0060009]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]NATP binding [GO:0005524]; chromatin binding [GO:0003682]; chromo shadow domain binding [GO:0070087]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; zinc ion binding [GO:0008270]nuclear heterochromatin [GO:0005720]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; SWI/SNF superfamily-type complex [GO:0070603]; telomeric heterochromatin [GO:0031933]FUNCTION: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (PubMed:24500201) is not sufficient to decrease chromatin condensation at telomers nor to increase expression of telomeric RNA in fibroblasts. May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. {ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:22391447, ECO:0000269|PubMed:22829774, ECO:0000269|PubMed:24500201}.Q00978IRF9Interferon regulatory factor 9 STAT targetSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11846981}. Nucleus {ECO:0000269|PubMed:11846981}. Note=Translocated into the nucleus upon activation by IFN-alpha/beta.kcell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; interferon-gamma-mediated signaling pathway [GO:0060333]; transcription from RNA polymerase II promoter [GO:0006366]; type I interferon biosynthetic process [GO:0045351]; type I interferon signaling pathway [GO:0060337]tregulatory region DNA binding [GO:0000975]; sequence-specific DNA binding transcription factor activity [GO:0003700]-FUNCTION: Transcription factor that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IR< F9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.P78368KC1G2Casein kinase I isoform gamma-2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15077195}.endocytosis [GO:0006897]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; Wnt signaling pathway [GO:0016055]%FUNCTION: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation. {ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:15342122, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18794808, ECO:0000269|PubMed:19005213}.Q7Z4V5HDGR20Hepatoma-derived growth factor-related protein 2=SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UMU9}.Zpositive regulation of cell growth [GO:0030307]; transcription, DNA-templated [GO:0006351]8chromatin binding [GO:0003682]; DNA binding [GO:0003677]Jmitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]}FUNCTION: Involved in cellular growth control, through the regulation of cyclin D1 expression. {ECO:0000269|PubMed:25689719}.P41221WNT5AProtein Wnt-5a:activation of JUN kinase activity [GO:0007257]; activation of MAPK activity [GO:0000187]; activation of protein kinase B activity [GO:0032148]; ameboidal-type cell migration [GO:0001667]; anterior/posterior axis specification, embryo [GO:0008595]; axon guidance [GO:0007411]; canonical Wnt signaling pathway [GO:0060070]; cartilage development [GO:0051216]; cell fate commitment [GO:0045165]; cellular protein localization [GO:0034613]; cellular response to calcium ion [GO:0071277]; cellular response to interferon-gamma [GO:0071346]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cervix development [GO:0060067]; cochlea morphogenesis [GO:0090103]; convergent extension involved in organogenesis [GO:0060029]; dopaminergic neuron differentiation [GO:0071542]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal system development [GO:0048706]; epithelial cell proliferation involved in mammary gland duct elongation [GO:0060750]; epithelial to mesenchymal transition [GO:0001837]; establishment of planar polarity [GO:0001736]; face development [GO:0060324]; genitalia development [GO:0048806]; heart looping [GO:0001947]; hematopoietic stem cell proliferation [GO:0071425]; hindgut morphogenesis [GO:0007442]; hypophysis morphogenesis [GO:0048850]; keratinocyte differentiation [GO:0030216]; lateral sprouting involved in mammary gland duct morphogenesis [GO:0060599]; lens development in camera-type eye [GO:0002088]; lung development [GO:0030324]; male gonad development [GO:0008584]; mammary gland branching involved in thelarche [GO:0060744]; melanocyte proliferation [GO:0097325]; mesenchymal-epithelial cell signaling [GO:0060638]; midbrain development [GO:0030901]; midgut development [GO:0007494]; negative chemotaxis [GO:0050919]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of melanin biosynthetic process [GO:0048022]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of prostatic bud formation [GO:0060686]; negative regulation of synapse assembly [GO:0051964]; negative regulation of transcription, DNA-templated [GO:0045892]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway via JNK cascade [GO:0038031]; olfactory bulb interneuron development [GO:0021891]; optic cup formation involved in camera-type eye development [GO:0003408]; palate development [GO:0060021]; planar cell polarity pathway involved in cardiac muscle tissue morphogenesis [GO:0061350]; planar cell polarity pathway involved in cardiac right atrium morphogenesis [GO:0061349]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; planar cell polarity pathway involved in outflow tract morphogenesis [GO:0061347]; planar cell polarity pathway involved in pericardium morphogenesis [GO:0061354]; planar cell polarity pathway involved in ventricular septum morphogenesis [GO:0061348]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; positive regulation of cGMP metabolic process [GO:0030825]; positive regulation of chemokine biosynthetic process [GO:0045080]; positive regulation of cytokine secretion involved in immune response [GO:0002741]; positive regulation of endocytosis [GO:0045807]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of interleukin-1 beta secretion [GO:0050718]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 secretion [GO:2000484]; positive regulation of macrophage activation [GO:0043032]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of meiotic nuclear division [GO:0045836]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of non-canonical Wnt signaling pathway [GO:2000052]; positive regulation of ossification [GO:0045778]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein kinase C activity [GO:1900020]; positive regulation of protein kinase C signaling [GO:0090037]; positive regulation of response to cytokine stimulus [GO:0060760]; positive regulation of T cell chemotaxis [GO:0010820]; positive regulation of thymocyte apoptotic process [GO:0070245]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; post-anal tail morphogenesis [GO:0036342]; primitive streak formation [GO:0090009]; regulation of branch< ing involved in mammary gland duct morphogenesis [GO:0060762]; response to organic substance [GO:0010033]; somitogenesis [GO:0001756]; type B pancreatic cell development [GO:0003323]; urinary bladder development [GO:0060157]; uterus development [GO:0060065]; vagina development [GO:0060068]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway, calcium modulating pathway [GO:0007223]; wound healing [GO:0042060] frizzled binding [GO:0005109]; receptor agonist activity [GO:0048018]; receptor tyrosine kinase-like orphan receptor binding [GO:0005115]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region DNA binding [GO:0044212]Ncell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells. Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes. {ECO:0000269|PubMed:15735754, ECO:0000269|PubMed:17426020}.Q8NB49AT11C#Phospholipid-transporting ATPase IGUSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Some cell membrane localization observed in the presence of TMEM30B.ion transmembrane transport [GO:0034220]; phospholipid translocation [GO:0045332]; positive regulation of B cell differentiation [GO:0045579]; pre-B cell differentiation [GO:0002329]; transmembrane transport [GO:0055085]uATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phospholipid-translocating ATPase activity [GO:0004012]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]hFUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage. Seems to mediate phosphatidylserine (PS) flipping in pro-B cells. May be involved in the transport of cholestatic bile acids (By similarity). {ECO:0000250}.Q96S52PIGS GPI transamidase component PIG-SSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Multi-pass membrane protein {ECO:0000269|PubMed:11483512}.attachment of GPI anchor to protein [GO:0016255]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; post-translational protein modification [GO:0043687]pendoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; membrane [GO:0016020]Q96GQ5RUS1RUS1 family protein C16orf58P17676CEBPB#CCAAT/enhancer-binding protein betaQSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}. Cytoplasm {ECO:0000269|PubMed:9374525}. Note=Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity). {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:9374525}.acute-phase response [GO:0006953]; brown fat cell differentiation [GO:0050873]; cellular response to amino acid stimulus [GO:0071230]; defense response to bacterium [GO:0042742]; embryonic placenta development [GO:0001892]; granuloma formation [GO:0002432]; hepatocyte proliferation [GO:0072574]; immune response [GO:0006955]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; liver regeneration [GO:0097421]; mammary gland epithelial cell differentiation [GO:0060644]; mammary gland epithelial cell proliferation [GO:0033598]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription, DNA-templated [GO:0045892]; neuron differentiation [GO:0030182]; ovarian follicle development [GO:0001541]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress [GO:1990440]; regulation of interleukin-6 biosynthetic process [GO:0045408]; regulation of osteoclast differentiation [GO:0045670]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription involved in cell fate commitment [GO:0060850]; response to endoplasmic reticulum stress [GO:0034976]; response to lipopolysaccharide [GO:0032496]; T-helper 1 cell activation [GO:0035711]; transcription from RNA polymerase II promoter [GO:0006366]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]CHOP-C/EBP complex [GO:0036488]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:9374525, PubMed:12048245, PubMed:18647749). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylat< ion, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12048245, ECO:0000269|PubMed:18647749, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:9374525, ECO:0000303|PubMed:25451943}.; FUNCTION: Isoform 2: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250|UniProtKB:P28033}.; FUNCTION: Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11741938}.A6NJ78MET15*Probable methyltransferase-like protein 15"rRNA base methylation [GO:0070475];rRNA (cytosine-N4-)-methyltransferase activity [GO:0071424]VFUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase. {ECO:0000250}.Q07954LRP15Prolow-density lipoprotein receptor-related protein 1Receptor4SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane; Single-pass type I membrane protein. Membrane, coated pit.; SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane; Peripheral membrane protein; Extracellular side. Membrane, coated pit.; SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related protein 1 intracellular domain: Cytoplasm. Nucleus. Note=After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.vaging [GO:0007568]; aorta morphogenesis [GO:0035909]; apoptotic cell clearance [GO:0043277]; beta-amyloid clearance [GO:0097242]; cell proliferation [GO:0008283]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron projection development [GO:0010977]; negative regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000587]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of Wnt signaling pathway [GO:0030178]; phototransduction, visible light [GO:0007603]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of lipid transport [GO:0032370]; positive regulation of protein transport [GO:0051222]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]; receptor-mediated endocytosis [GO:0006898]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cholesterol transport [GO:0032374]; regulation of phospholipase A2 activity [GO:0032429]; retinoid metabolic process [GO:0001523]apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; lipoprotein particle receptor binding [GO:0070325]; lipoprotein transporter activity [GO:0042954]; poly(A) RNA binding [GO:0044822]; protein complex binding [GO:0032403]; receptor activity [GO:0004872]clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endocytic vesicle membrane [GO:0030666]; endosome [GO:0005768]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]eFUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.; FUNCTION: Functions as a receptor for Pseudomonas aeruginosa exotoxin A.Q9UL25RAB21Ras-related protein Rab-21SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19745841}. Golgi apparatus membrane. Early endosome membrane. Cytoplasmic vesicle membrane. Cleavage furrow. Note=Colocalizes with ANKRD27 and VAMP7 in neurites (By similarity). In nonpolarized epithelial Caco-2 cells, found in the endoplasmic reticulum; in polarized cells, observed in vesicles in the apical cytoplasm. During mitosis, in mid-telophase, localized in the ingressing cleavage furrow. In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells. {ECO:0000250|UniProtKB:P35282, ECO:0000250|UniProtKB:Q6AXT5}.anterograde axon cargo transport [GO:0008089]; intracellular protein transport [GO:0006886]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of receptor-mediated endocytosis [GO:0048260]; Rab protein signal transduction [GO:0032482]; regulation of axon extension [GO:0030516]; regulation of exocytosis [GO:0017157]cleavage furrow [GO:0032154]; cytoplasmic side of early endosome membrane [GO:0098559]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi cisterna membrane [GO:0032580]; neuron projection [GO:0043005]; trans-Golgi network [GO:0005802]; vesicle membrane [GO:0012506]FUNCTION: Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration (By similarity). During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis. Involved in neurite growth (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q6AXT5, ECO:0000269|PubMed:18804435}.Q8WVM8SCFD1'Sec1 family domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.cell morphogenesis [GO:0000902]; negative regulation of autophagosome assembly [GO:1902902]; phagocytosis [GO:0006909]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; regulation of ER to Golgi vesicle-mediated transport [GO:0060628]; regulation of protein transport [GO:0051223]; response to hypoxia [GO:0001666]; response to toxic substance [GO:0009636]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; toxin transport [GO:1901998]; vesicle docking involved in exocytosis [GO:0006904]syntaxin binding [GO:0019905]cis-Golgi network [GO:0005801]; endoplasmic reticulum membrane [GO:0005789]; Golgi-associated vesicle [GO:0005798]; Golgi cisterna membrane [GO:0032580]; Golgi transport complex [GO:0017119]; plasma membrane [GO:0005886]FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with COG4. Involved in vesicular transport between the endoplasmic reticulum and the Golgi (By similarity). {ECO:0000250}.Q8N3U4STAG2Cohesin subunit SA-2YSUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophas< e it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex.cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of DNA endoreduplication [GO:0032876]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; sister chromatid cohesion [GO:0007062]; stem cell maintenance [GO:0019827]chromatin binding [GO:0003682]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]Aactin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269|PubMed:12034751}.P16234PGFRA-Platelet-derived growth factor receptor alpha7SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-pass type I membrane protein {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Note=The activated receptor is rapidly internalized and degraded.: adrenal gland development [GO:0030325]; cardiac myofibril assembly [GO:0055003]; cell activation [GO:0001775]; cell chemotaxis [GO:0060326]; cellular response to amino acid stimulus [GO:0071230]; cellular response to reactive oxygen species [GO:0034614]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic skeletal system morphogenesis [GO:0048704]; epidermal growth factor receptor signaling pathway [GO:0007173]; estrogen metabolic process [GO:0008210]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gliogenesis [GO:0042063]; hematopoietic progenitor cell differentiation [GO:0002244]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; in utero embryonic development [GO:0001701]; Leydig cell differentiation [GO:0033327]; lung development [GO:0030324]; luteinization [GO:0001553]; male genitalia development [GO:0030539]; metanephric glomerular capillary formation [GO:0072277]; negative regulation of platelet activation [GO:0010544]; neurotrophin TRK receptor signaling pathway [GO:0048011]; odontogenesis of dentin-containing tooth [GO:0042475]; palate development [GO:0060021]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet aggregation [GO:0070527]; platelet-derived growth factor receptor-alpha signaling pathway [GO:0035790]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway [GO:0038091]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA replication [GO:0045740]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of phospholipase C activity [GO:0010863]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of chemotaxis [GO:0050920]; regulation of mesenchymal stem cell differentiation [GO:2000739]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to hyperoxia [GO:0055093]; response to inorganic substance [GO:0010035]; retina vasculature development in camera-type eye [GO:0061298]; signal transduction involved in regulation of gene expression [GO:0023019]; viral process [GO:0016032]; wound healing [GO:0042060]ATP binding [GO:0005524]; platelet-derived growth factor alpha-receptor activity [GO:0005018]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; vascular endothelial growth factor-activated receptor activity [GO:0005021]; vascular endothelial growth factor binding [GO:0038085]Gcytoplasm [GO:0005737]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; integral component of plasma membrane [GO:0005887]; intrinsic component of plasma membrane [GO:0031226]; membrane [GO:0016020]; microvillus [GO:0005902]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:10947961, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664, ECO:0000269|< PubMed:8760137, ECO:0000269|PubMed:8943348}.Q12830BPTF)Nucleosome-remodeling factor subunit BPTFSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In brains of Alzheimer disease patients, present in a subset of amyloid-containing plaques.anterior/posterior pattern specification [GO:0009952]; brain development [GO:0007420]; chromatin remodeling [GO:0006338]; embryonic placenta development [GO:0001892]; endoderm development [GO:0007492]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]tsequence-specific DNA binding [GO:0043565]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NURF complex [GO:0016589]FUNCTION: Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors.O95479G6PE)GDH/6PGL endoplasmic bifunctional protein`SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomes, endoplasmic reticulum lumen.Lglucose metabolic process [GO:0006006]; pentose-phosphate shunt [GO:0006098]6-phosphogluconolactonase activity [GO:0017057]; glucose 1-dehydrogenase [NAD(P)] activity [GO:0047936]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661](endoplasmic reticulum lumen [GO:0005788]YFUNCTION: Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates.P62820RAB1ARas-related protein Rab-1ASUBCELLULAR LOCATION: Golgi apparatus. Endoplasmic reticulum. Early endosome. Cytoplasm, cytosol. Membrane. Melanosome {ECO:0000250}. Note=Alternates between membrane-associated and cytosolic forms.autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cargo loading into COPII-coated vesicle [GO:0090110]; cell migration [GO:0016477]; defense response to bacterium [GO:0042742]; endocytosis [GO:0006897]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; growth hormone secretion [GO:0030252]; interleukin-8 secretion [GO:0072606]; intracellular protein transport [GO:0006886]; melanosome transport [GO:0032402]; mitotic cell cycle [GO:0000278]; positive regulation of glycoprotein metabolic process [GO:1903020]; Rab protein signal transduction [GO:0032482]; substrate adhesion-dependent cell spreading [GO:0034446]; vesicle-mediated transport [GO:0016192]; vesicle transport along microtubule [GO:0047496]; virion assembly [GO:0019068]cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport. {ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236, ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626}.Q8IXI2MIRO1Mitochondrial Rho GTPase 1 SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:19528298}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:19528298}. Note=Colocalizes with MGARP and RHOT2 at the mitochondria.cellular homeostasis [GO:0019725]; mitochondrial outer membrane permeabilization [GO:0097345]; mitochondrion transport along microtubule [GO:0047497]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]Xcalcium ion binding [GO:0005509]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]cytosol [GO:0005829]; integral component of mitochondrial outer membrane [GO:0031307]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:16630562}.Q9NXF1TEX10$Testis-expressed sequence 10 proteiniSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:12429849}; Multi-pass membrane protein {ECO:0000269|PubMed:12429849}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000250}.cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; MLL1 complex [GO:0071339]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]FUNCTION: Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:22872859}.Q9P2E9RRBP1Ribosome-binding protein 1xSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.aosteoblast differentiation [GO:0001649]; protein transport [GO:0015031]; translation [GO:0006412]@poly(A) RNA binding [GO:0044822]; receptor activity [GO:0004872]endoplasmic reticulum [GO:0005783]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]; ribosome [GO:0005840]FUNCTION: Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}.P18627LAG3$Lymphocyte activation gene 3 proteincell surface receptor signaling pathway [GO:0007166]; negative regulation of interleukin-2 biosynthetic process [GO:0045085]; negative regulation of T cell activation [GO:0050868]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]antigen binding [GO:0003823]; MHC class II protein binding [GO:0042289]; transmembrane signaling receptor activity [GO:0004888]Zexternal side of plasma membrane [GO:0009897]; integral component of membrane [GO:0016021]LFUNCTION: Involved in lymphocyte activation. Binds to HLA class-II antigens.O75396SC22B"Vesicle-trafficking protein SEC22b-SNARE interactions in vesicular transport(34)pSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.ER to Golgi vesicle-mediated transport [GO:0006888]; positive regulation of prot< ein catabolic process [GO:0045732]; protein transport [GO:0015031]; regulation of organelle organization [GO:0033043]endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; melanosome [GO:0042470]FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}.Q8TB22SPT20%Spermatogenesis-associated protein 20rcell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; spermatogenesis [GO:0007283]!extracellular region [GO:0005576]AFUNCTION: May play a role in fertility regulation. {ECO:0000250}.P35052GPC1 Glypican-1NSUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP Abeta peptides in lipid rafts in Alzheimer disease brains.; SUBCELLULAR LOCATION: Secreted glypican-1: Secreted, extracellular space.axon guidance [GO:0007411]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan catabolic process [GO:0030200]; myelin assembly [GO:0032288]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; phototransduction, visible light [GO:0007603]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; retinoid metabolic process [GO:0001523]; Schwann cell differentiation [GO:0014037]; small molecule metabolic process [GO:0044281]lcopper ion binding [GO:0005507]; fibroblast growth factor binding [GO:0017134]; laminin binding [GO:0043236]_anchored component of membrane [GO:0031225]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; lysosomal lumen [GO:0043202]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. {ECO:0000250, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:21642435}.Q8NCN5PDPRDPyruvate dehydrogenase phosphatase regulatory subunit, mitochondrialcellular metabolic process [GO:0044237]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; small molecule metabolic process [GO:0044281]$oxidoreductase activity [GO:0016491]9cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]FUNCTION: Decreases the sensitivity of PDP1 to magnesium ions, and this inhibition is reversed by the polyamine spermine. {ECO:0000250}.Q96PU4UHRF2!E3 ubiquitin-protein ligase UHRF2SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:12176013, ECO:0000269|PubMed:23404503}. Note=Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 (By similarity). {ECO:0000250}.cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; maintenance of DNA methylation [GO:0010216]; positive regulation of cell cycle arrest [GO:0071158]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation of cell cycle [GO:0051726]; regulation of methylation-dependent chromatin silencing [GO:0090308]; ubiquitin-dependent protein catabolic process [GO:0006511]DNA binding [GO:0003677]; histone binding [GO:0042393]; ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]Tnuclear heterochromatin [GO:0005720]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131. {ECO:0000269|PubMed:12176013, ECO:0000269|PubMed:14741369, ECO:0000269|PubMed:15178429, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:23404503}.Q12874SF3A3Splicing factor 3A subunit 3&SUBCELLULAR LOCATION: Nucleus speckle.gene expression [GO:0010467]; mRNA 3'-splice site recognition [GO:0000389]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]dFUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.Q16630CPSF69Cleavage and polyadenylation specificity factor subunit 6SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:9659921}. Note=In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles.emRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; protein tetramerization [GO:0051262]\mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]membrane [GO:0016020]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; paraspeckles [GO:0042382]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Involved in association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. CPSF6 binds to cleavage and polyadenylation RNA substrates and promotes RNA looping. {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.Q9HCU5PREB,Prolactin regulatory element-binding proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER to Golgi vesicle-mediated transport [GO:0006888]; IRE1-mediated unfolded protein response [GO:0036498]; membrane organization [GO:0061024]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; protein transport [GO:0015031]; regu< lation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]XFUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription (By similarity). Guanine nucleotide exchange factor that activates SARA2. Required for the formation of COPII transport vesicles from the ER. {ECO:0000250}.P20226TBPTATA-box-binding protein Basal TFsEchromatin silencing at rDNA [GO:0000183]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of gene expression, epigenetic [GO:0040029]; spermatogenesis [GO:0007283]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase III promoter [GO:0006383]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]\enzyme binding [GO:0019899]; repressing transcription factor binding [GO:0070491]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; transcription factor TFIIA complex [GO:0005672]; transcription factor TFIID complex [GO:0005669]FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. {ECO:0000269|PubMed:15970593}.Q96A26F162AProtein FAM162ASUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:15082785, ECO:0000269|PubMed:16698020}.factivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cellular response to hypoxia [GO:0071456]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic process [GO:0043065]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; transformed cell apoptotic process [GO:0006927]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]; nucleus [GO:0005634]HFUNCTION: Proposed to be involved in regulation of apoptosis; the exact mechanism may differ between cell types/tissues. May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition. May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus; however, the involvement of caspases has been reported conflictingly. {ECO:0000269|PubMed:15082785}.P29992GNA113Guanine nucleotide-binding protein subunit alpha-11SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18703424}; Lipid-anchor {ECO:0000305|PubMed:18703424}. Cytoplasm {ECO:0000269|PubMed:18703424}. Note=In testicular cells, expressed exclusively in the cytoplasm.action potential [GO:0001508]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; blood coagulation [GO:0007596]; cellular response to pH [GO:0071467]; developmental pigmentation [GO:0048066]; entrainment of circadian clock [GO:0009649]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; heart development [GO:0007507]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; phototransduction, visible light [GO:0007603]; platelet activation [GO:0030168]; regulation of melanocyte differentiation [GO:0045634]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]G-protein beta/gamma-subunit complex binding [GO:0031683]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]; type 2A serotonin receptor binding [GO:0031826]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; lysosomal membrane [GO:0005765]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.Q9BXJ8T120ATransmembrane protein 120AwSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein {ECO:0000255}.`FUNCTION: Necessary for efficient adipogenesis (PubMed:26024229). {ECO:0000269|PubMed:26024229}.Q8TC12RDH11Retinol dehydrogenase 11SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12036956}; Single-pass type II membrane protein {ECO:0000269|PubMed:12036956}.adaptation of rhodopsin mediated signaling [GO:0016062]; phototransduction, visible light [GO:0007603]; retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]]NADP-retinol dehydrogenase activity [GO:0052650]; retinol dehydrogenase activity [GO:0004745]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; photoreceptor inner segment [GO:0001917]$FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected.Q5HYI8RABL3Rab-like protein 3Zintracellular protein transport [GO:0006886]; Rab protein signal transduction [GO:0032482]Q15393SF3B3Splicing factor 3B subunit 3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.&gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of protein catabolic process [GO:0042177]; protein complex assembly [GO:0006461]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.Q9H307PININPinin< SUBCELLULAR LOCATION: Nucleus speckle. Cell junction, desmosome. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein.cell adhesion [GO:0007155]; mRNA splicing, via spliceosome [GO:0000398]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]eDNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; structural molecule activity [GO:0005198]catalytic step 2 spliceosome [GO:0071013]; cell-cell junction [GO:0005911]; desmosome [GO:0030057]; intermediate filament [GO:0005882]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma. {ECO:0000269|PubMed:12051732, ECO:0000269|PubMed:14517304, ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15735603, ECO:0000269|PubMed:22388736}.Q8IU81I2BP10Interferon regulatory factor 2-binding protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12799427}.<ligase activity [GO:0016874]; metal ion binding [GO:0046872]gaggresome [GO:0016235]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]GFUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation. {ECO:0000269|PubMed:12799427, ECO:0000269|PubMed:18671972}.P61018RAB4BRas-related protein Rab-4Bglucose import [GO:0046323]; intracellular protein transport [GO:0006886]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]insulin-responsive compartment [GO:0032593]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]cFUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}.Q9H061T126ATransmembrane protein 126ASUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19327736, ECO:0000269|PubMed:23500070}; Multi-pass membrane protein {ECO:0000269|PubMed:19327736, ECO:0000269|PubMed:23500070}.$optic nerve development [GO:0021554]O15042SR1401U2 snRNP-associated SURP motif-containing protein<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}.Q86UY8NT5D3+5'-nucleotidase domain-containing protein 3Ocytosol [GO:0005829]; mitochondrion [GO:0005739]; receptor complex [GO:0043235]P23468PTPRD0Receptor-type tyrosine-protein phosphatase delta3heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; negative regulation of JAK-STAT cascade [GO:0046426]; neuron differentiation [GO:0030182]; peptidyl-tyrosine dephosphorylation [GO:0035335]; phosphate-containing compound metabolic process [GO:0006796]; positive regulation of dendrite morphogenesis [GO:0050775]; presynaptic membrane assembly [GO:0097105]; protein dephosphorylation [GO:0006470]; regulation of immune response [GO:0050776]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185]cell adhesion molecule binding [GO:0050839]; receptor binding [GO:0005102]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]Q99653CHP1"Calcineurin B homologous protein 1CSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633}. Note=Localizes in cytoplasmic compartments in dividing cells. Localizes in the nucleus in quiescent cells. Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) and CRM1-dependent pathway. May shuttle between nucleus and cytoplasm. Localizes with the microtubule-organizing center (MTOC) and extends toward the periphery along microtubules. Associates with membranes of the early secretory pathway in a GAPDH-independent, N-myristoylation- and calcium-dependent manner. Colocalizes with the mitotic spindle microtubules. Colocalizes with GAPDH along microtubules. Colocalizes with SLC9A1/NHE1 at the reticulum endoplasmic. Colocalizes with STK17B at the plasma membrane (By similarity). Colocalizes with SLC9A1/NHE1 at the cell membrane. {ECO:0000250}.(calcium ion-dependent exocytosis [GO:0017156]; carbohydrate metabolic process [GO:0005975]; cellular response to acidic pH [GO:0071468]; cytoplasmic microtubule organization [GO:0031122]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; membrane docking [GO:0022406]; membrane fusion [GO:0061025]; membrane organization [GO:0061024]; microtubule bundle formation [GO:0001578]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of phosphatase activity [GO:0010923]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of protein glycosylation [GO:0060050]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of protein transport [GO:0051222]; positive regulation of sodium:proton antiporter activity [GO:0032417]; potassium ion transport [GO:0006813]; protein export from nucleus [GO:0006611]; protein oligomerization [GO:0051259]; protein stabilization [GO:0050821]; regulation of intracellular pH [GO:0051453]; regulation of neuron death [GO:1901214]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; kinase binding [GO:0019900]; microtubule binding [GO:0008017]; potassium channel regulator activity [GO:0015459]; protein kinase inhibitor activity [GO:0004860]; transporter activity [GO:0005215]lcytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]FUNCTION: Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (< TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner. {ECO:0000269|PubMed:10593895, ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}.Q5JRA6MIA3&Melanoma inhibitory activity protein 3YSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19269366}; Single-pass type I membrane protein {ECO:0000269|PubMed:19269366}. Note=Localizes at endoplasmic reticulum exit sites. After loading of COL7A1 into transport carriers, it is not incorporated into COPII carriers and remains in the endoplasmic reticulum membrane.}chondrocyte development [GO:0002063]; collagen fibril organization [GO:0030199]; exocytosis [GO:0006887]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell migration [GO:0030336]; positive regulation of bone mineralization [GO:0030501]; positive regulation of leukocyte migration [GO:0002687]; protein transport [GO:0015031]; wound healing [GO:0042060]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]FUNCTION: Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. May participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. {ECO:0000269|PubMed:19269366}.Q9NS69TOM223Mitochondrial import receptor subunit TOM22 homologmSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.cellular protein metabolic process [GO:0044267]; protein import into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626]7protein transmembrane transporter activity [GO:0008320]integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]FUNCTION: Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore. {ECO:0000269|PubMed:10982837}.P78345RPP38"Ribonuclease P protein subunit p387SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; tRNA processing [GO:0008033]$ribonuclease P activity [GO:0004526]Cnucleolar ribonuclease P complex [GO:0005655]; nucleus [GO:0005634]FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus.Q9BQG0MBB1AMyb-binding protein 1AqSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12429849}. Nucleus {ECO:0000269|PubMed:12429849}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Note=Shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1 (By similarity). Predominantly nucleolar. {ECO:0000250|UniProtKB:Q7TPV4}.Dcellular response to glucose starvation [GO:0042149]; circadian regulation of gene expression [GO:0032922]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleocytoplasmic transport [GO:0006913]; osteoblast differentiation [GO:0001649]; positive regulation of anoikis [GO:2000210]; positive regulation of cell cycle arrest [GO:0071158]; regulation of transcription, DNA-templated [GO:0006355]; respiratory electron transport chain [GO:0022904]; transcription, DNA-templated [GO:0006351]core promoter binding [GO:0001047]; DNA-directed DNA polymerase activity [GO:0003887]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding [GO:0043565]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2. Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter. {ECO:0000250|UniProtKB:Q7TPV4}.Q14728MFS10:Major facilitator superfamily domain-containing protein 10XSUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.apoptotic process [GO:0006915]; tetracycline transport [GO:0015904]; transmembrane transport [GO:0055085]; transport [GO:0006810]rsubstrate-specific transmembrane transporter activity [GO:0022891]; tetracycline transporter activity [GO:0008493]FUNCTION: Confers cellular resistance to apoptosis induced by the non-steroidal anti-inflammatory drugs indomethacin and diclofenac. May act as an efflux pump. {ECO:0000269|PubMed:17362938}.P49748ACADV>Very long-chain specific acyl-CoA dehydrogenase, mitochondrialFatty acid degradationcellular lipid metabolic process [GO:0044255]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; energy derivation by oxidation of organic compounds [GO:0015980]; epithelial cell differentiation [GO:0030855]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; IRE1-mediated unfolded protein response [GO:0036498]; lipid homeostasis [GO:0055088]; negative regulation of fatty acid biosynthetic process [GO:0045717]; negative regulation of fatty acid oxidation [GO:0046322]; regulation of cholesterol metabolic process [GO:0090181]; small molecule metabolic process [GO:0044281]; temperature homeostasis [GO:0001659]; very long-chain fatty acid catabolic process [GO:0042760]acyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; long-chain-acyl-CoA dehydrogenase activity [GO:0004466]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]; very-long-chain-acyl-CoA dehydrogenase activity [GO:0017099]cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondr< ion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634](FUNCTION: Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. {ECO:0000269|PubMed:18227065}.P51991ROA3*Heterogeneous nuclear ribonucleoprotein A3OSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; RNA splicing [GO:0008380]mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA transmembrane transporter activity [GO:0051033]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; ribonucleoprotein granule [GO:0035770]FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:11886857}.Q9P0L0VAPA8Vesicle-associated membrane protein-associated protein ASUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19289470}; Single-pass type IV membrane protein {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19289470}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells.cell death [GO:0008219]; COPII-coated vesicle budding [GO:0090114]; ER to Golgi vesicle-mediated transport [GO:0006888]; membrane fusion [GO:0061025]; negative regulation by host of viral genome replication [GO:0044828]; neuron projection development [GO:0031175]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation by host of viral release from host cell [GO:0044791]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein localization to endoplasmic reticulum [GO:0070972]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]FFAT motif binding [GO:0033149]; microtubule binding [GO:0008017]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; signal transducer activity [GO:0004871]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]; vesicle [GO:0031982]mFUNCTION: May play a role in vesicle trafficking. {ECO:0000269|PubMed:11511104, ECO:0000269|PubMed:19289470}.Q9H488OFUT1)GDP-fucose protein O-fucosyltransferase 1:SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.angiogenesis [GO:0001525]; embryo development [GO:0009790]; fucose metabolic process [GO:0006004]; heart development [GO:0007507]; nervous system development [GO:0007399]; Notch signaling pathway [GO:0007219]; O-glycan processing [GO:0016266]; protein O-linked fucosylation [GO:0036066]; protein O-linked glycosylation [GO:0006493]; regulation of transcription, DNA-templated [GO:0006355]; somitogenesis [GO:0001756]\fucosyltransferase activity [GO:0008417]; peptide-O-fucosyltransferase activity [GO:0046922]9endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]tFUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs). {ECO:0000269|PubMed:11524432, ECO:0000269|PubMed:8358148}.Q8N2K0ABD12Monoacylglycerol lipase ABHD12{SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99LR1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99LR1}.acylglycerol catabolic process [GO:0046464]; adult walking behavior [GO:0007628]; phosphatidylserine catabolic process [GO:0006660]; response to auditory stimulus [GO:0010996])acylglycerol lipase activity [GO:0047372]alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [GO:0032281]; integral component of membrane [GO:0016021]wFUNCTION: Lysophosphatidylserine (LPS) lipase that plays a key role in the central nervous system. Represents a major LPS lipase in the brain (By similarity). May also have a 2-arachidonoylglycerol (2-AG) hydrolase activity and act as a regulator of endocannabinoid signaling pathways. {ECO:0000250|UniProtKB:Q99LR1, ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:24027063}.P62879GBB2@Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2GPCR/Gprotein/RasGRFscellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; G-protein coupled receptor signaling pathway [GO:0007186]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]calcium channel regulator activity [GO:0005246]; GTPase activity [GO:0003924]; GTPase binding [GO:0051020]; protein complex binding [GO:0032403]; signal transducer activity [GO:0004871]Mcell body [GO:0044297]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; myelin sheath [GO:0043209]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; vesicle [GO:0031982]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.O75323NIPS2Protein NipSnap homolog 2ATP biosynthetic process [GO:0006754]; negative regulation of ATP citrate synthase activity [GO:2000984]; oxidative phosphorylation [GO:0006119]eintegral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrion [GO:0005739]O15254ACOX3%Peroxisomal acyl-coenzyme A oxidase 3/SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; small molecule metabolic process [GO:0044281]^acyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]; pristanoyl-CoA oxidase activity [GO:0016402]; receptor binding [GO:0005102]kmembrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]RFUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids. {ECO:0000250}.Q96DZ1ERLECEndoplasmic reticulum lectin 1mSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18502753}.ERAD pathway [GO:0036503]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]< Hglycoprotein binding [GO:0001948]; unfolded protein binding [GO:0051082]hendoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum quality control compartment [GO:0044322]SFUNCTION: Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins. {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753}.Q8N163CCAR2,Cell cycle and apoptosis regulator protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:23352644, ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:25661920}. Cytoplasm {ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:24824780}. Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis. {ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:24824780}.cell cycle [GO:0007049]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to heat [GO:0034605]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mRNA processing [GO:0006397]; negative regulation of catalytic activity [GO:0043086]; negative regulation of cell growth [GO:0030308]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of DNA damage checkpoint [GO:2000003]; regulation of cellular response to heat [GO:1900034]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription, elongation [GO:0032784]; regulation of protein deacetylation [GO:0090311]; regulation of protein stability [GO:0031647]; response to UV [GO:0009411]; rhythmic process [GO:0048511]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core binding [GO:0000993]cytoplasm [GO:0005737]; DBIRD complex [GO:0044609]; mitochondrial matrix [GO:0005759]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]a FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress. Regulates the circadian expression of the core clock components NR1D1 and ARNTL/BMAL1. Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:18235501, PubMed:18235502, PubMed:19131338, PubMed:19218236, PubMed:22446626, PubMed:23352644, PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978). {ECO:0000269|PubMed:18235501, ECO:0000269|PubMed:18235502, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:22446626, ECO:0000269|PubMed:23352644, ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25661920, ECO:0000269|PubMed:25732823}.O43143DHX15BPutative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15U2(21)2SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus.7mRNA processing [GO:0006397]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; RNA helicase activity [GO:0003724]cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U12-type spliceosomal complex [GO:0005689]^FUNCTION: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. {ECO:0000269|PubMed:19103666}.O75027ABCB79ATP-binding cassette sub-family B member 7, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.cellular iron ion homeostasis [GO:0006879]; heme transport [GO:0015886]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; transport [GO:0006810]ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; heme transporter activity [GO:0015232]FUNCTION: Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins.Q99805TM9S2$Transmembrane 9 superfamily member 2aSUBCELLULAR LOCATION: Endosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]eFUNCTION: In the intracellular compartments, may function as a channel or small molecule transporter.Q86SR1GLT100Polypeptide N-acetylgalactosaminyltransferase 10cellular protein metabolic process [GO:0044267]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]HGolgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.Q96A33CCD47(Coiled-coil domain-containing protein 47calcium ion homeostasis [GO:0055074]; endoplasmic reticulum organization [GO:0007029]; ER-associated ubiquitin-dependent protein catabolic process [GO:00< 30433]; ER overload response [GO:0006983]; osteoblast differentiation [GO:0001649]; post-embryonic development [GO:0009791]lintegral component of membrane [GO:0016021]; membrane [GO:0016020]; rough endoplasmic reticulum [GO:0005791]Q15459SF3A1Splicing factor 3A subunit 1gene expression [GO:0010467]; mRNA 3'-splice site recognition [GO:0000389]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U2-type spliceosomal complex [GO:0005684]Q9H2U2IPYR2*Inorganic pyrophosphatase 2, mitochondrialdiphosphate metabolic process [GO:0071344]; gene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]inorganic diphosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287]; protein serine/threonine phosphatase activity [GO:0004722]Eextracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]Q96S55WRIP1 ATPase WRNIP1|SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with WRN in granular structures in the nucleus. {ECO:0000250}.DNA replication [GO:0006260]; DNA synthesis involved in DNA repair [GO:0000731]; regulation of DNA-dependent DNA replication initiation [GO:0030174]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]Ymembrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]1FUNCTION: Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis. {ECO:0000269|PubMed:15670210}.Q15907RB11BRas-related protein Rab-11BSUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305|PubMed:21255211}; Lipid-anchor {ECO:0000305|PubMed:21255211}; Cytoplasmic side {ECO:0000305|PubMed:21255211}. Note=Recruited to phagosomes containing S.aureus.cellular response to acidic pH [GO:0071468]; constitutive secretory pathway [GO:0045054]; establishment of protein localization to membrane [GO:0090150]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; intracellular protein transport [GO:0006886]; melanosome transport [GO:0032402]; Rab protein signal transduction [GO:0032482]; receptor recycling [GO:0001881]; regulated secretory pathway [GO:0045055]; regulation of anion transport [GO:0044070]; regulation of endocytic recycling [GO:2001135]; regulation of protein localization to cell surface [GO:2000008]; retrograde transport, endosome to plasma membrane [GO:1990126]; transferrin transport [GO:0033572]oGDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin V binding [GO:0031489]7cell junction [GO:0030054]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]CFUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:14627637, ECO:0000269|PubMed:19029296, ECO:0000269|PubMed:19244346, ECO:0000269|PubMed:20717956, ECO:0000269|PubMed:21248079, ECO:0000269|PubMed:22129970}.O75208COQ93Ubiquinone biosynthesis protein COQ9, mitochondrialCSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}.omitochondrial electron transport, NADH to ubiquinone [GO:0006120]; ubiquinone biosynthetic process [GO:0006744]Jlipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]Emitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]GFUNCTION: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Binds a phospholipid of at least 10 carbons in each acyl group. May be required to present its bound-lipid to COQ7. {ECO:0000269|PubMed:25339443}.Q14980NUMA1#Nuclear mitotic apparatus protein 1SUBCELLULAR LOCATION: Nucleus matrix. Chromosome. Cytoplasm, cytoskeleton, spindle pole. Note=Resides in the nuclear matrix during interphases. Dissociates from condensing chromosomes during early prophase, and relocates to the spindle poles via dynein/dynamin association, it remain there until the anaphase onset. Before the complete disintegration of the nuclear lamina. As mitosis progresses it reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident.; SUBCELLULAR LOCATION: Isoform Numa-m: Cytoplasm. Note=Mainly clustered at the centrosomal region.; SUBCELLULAR LOCATION: Isoform Numa-s: Cytoplasm. Note=Mainly clustered at the centrosomal region.Hcell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; G2/M transition of mitotic cell cycle [GO:0000086]; lung epithelial cell differentiation [GO:0060487]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; nucleus organization [GO:0006997]apical part of cell [GO:0045177]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; neuronal cell body [GO:0043025]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]FUNCTION: Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority if the nuclear volume. Required for maintenance and establishment of the mitotic spindle poles, functionning as a tether linking bulk microtubules of the spindle to centrosomes. May be involved in coordination of the alignment of the mitotic spindle to the cellular polarity axis, which is a prerequisite for asymmetric cell divisions. {ECO:0000269|PubMed:19255246}.P0C867YB052-Putative uncharacterized protein LOC100130201Q9UGP8SEC63#Translocation protein SEC63 homologJcellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; liver development [GO:0001889]; multicellular organismal aging [GO:0010259]; nitrogen compound metabolic process [GO:0006807]; posttranslational protein targeting to membrane [GO:0006620]; posttranslational protein targeting to membrane, translocation [GO:0031204]; protein targeting to membrane [GO:0006612]; renal system development [GO:0072001]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]kpoly(A) RNA binding [GO:0044822]; protein transporter acti< vity [GO:0008565]; receptor activity [GO:0004872]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]yFUNCTION: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.Q8WVC0LEO1&RNA polymerase-associated protein LEO1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15791002}._endodermal cell fate commitment [GO:0001711]; histone H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; mRNA polyadenylation [GO:0006378]; negative regulation of myeloid cell differentiation [GO:0045638]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; stem cell maintenance [GO:0019827]; transcription elongation from RNA polymerase II promoter [GO:0006368]; Wnt signaling pathway [GO:0016055]QCdc73/Paf1 complex [GO:0016593]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling. {ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15791002, ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}.P08253MMP272 kDa type IV collagenasemmp_SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Mitochondrion.angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood vessel maturation [GO:0001955]; bone trabecula formation [GO:0060346]; cellular protein metabolic process [GO:0044267]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; embryo implantation [GO:0007566]; endodermal cell differentiation [GO:0035987]; ephrin receptor signaling pathway [GO:0048013]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; intramembranous ossification [GO:0001957]; positive regulation of innate immune response [GO:0045089]; proteolysis [GO:0006508]; response to hypoxia [GO:0001666]metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270]extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]; sarcomere [GO:0030017]FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.; FUNCTION: Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.Q8TBM8DJB14"DnaJ homolog subfamily B member 14SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23018488}; Single-pass membrane protein {ECO:0000269|PubMed:23018488}.FUNCTION: Acts as a co-chaperone with HSPA8 and promotes the degradation of misfolded transmembrane proteins in the ER-associated degradation (ERAD) pathway. {ECO:0000269|PubMed:23018488}.Q9Y6C2EMIL1EMILIN-1SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Note=Found mainly at the interface between amorphous elastin and microfibrils.Jcell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]collagen trimer [GO:0005581]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.Q8TB37NUBPLIron-sulfur protein NUBPLBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19752196}.imitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrion morphogenesis [GO:0070584]g4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). May deliver of one or more Fe-S clusters to complex I subunits. {ECO:0000269|PubMed:19752196}.Q9H8M9EVA1AProtein eva-1 homolog ASUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17492404}; Single-pass membrane protein {ECO:0000269|PubMed:17492404}. Lysosome membrane {ECO:0000269|PubMed:17492404}; Single-pass membrane protein {ECO:0000269|PubMed:17492404}.6apoptotic process [GO:0006915]; autophagy [GO:0006914]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]FUNCTION: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis. {ECO:0000269|PubMed:17492404, ECO:0000269|PubMed:19029833}.Q9BVC6TM109Transmembrane protein 109SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Sarcoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.cellular response to gamma radiation [GO:0071480]; intrinsic ap< optotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; negative regulation of cell death [GO:0060548]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; nuclear outer membrane [GO:0005640]; sarcoplasmic reticulum membrane [GO:0033017]O15269SPTC1Serine palmitoyltransferase 1Sphingolipid metabolismoSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.Eceramide biosynthetic process [GO:0046513]; small molecule metabolic process [GO:0044281]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512]]pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339]FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. {ECO:0000269|PubMed:19416851}.Q9UBG0MRC2C-type mannose receptor 2jcollagen catabolic process [GO:0030574]; endocytosis [GO:0006897]; osteoblast differentiation [GO:0001649]@carbohydrate binding [GO:0030246]; collagen binding [GO:0005518]_focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:12972549}.P11169GTR3ASolute carrier family 2, facilitated glucose transporter member 3carbohydrate metabolic process [GO:0005975]; glucose import [GO:0046323]; glucose transport [GO:0015758]; hexose transmembrane transport [GO:0035428]; hexose transport [GO:0008645]; L-ascorbic acid metabolic process [GO:0019852]; proton transport [GO:0015992]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]eglucose transmembrane transporter activity [GO:0005355]; sugar:proton symporter activity [GO:0005351]textracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]TFUNCTION: Facilitative glucose transporter. Probably a neuronal glucose transporter.P22087FBRL'rRNA 2'-O-methyltransferase fibrillarinSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14583623, ECO:0000269|PubMed:2026646, ECO:0000269|PubMed:2414294, ECO:0000269|PubMed:24352239}. Note=Fibrillar region of the nucleolus.box C/D snoRNA 3'-end processing [GO:0000494]; histone glutamine methylation [GO:1990258]; osteoblast differentiation [GO:0001649]; rRNA methylation [GO:0031167]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033]histone-glutamine methyltransferase activity [GO:1990259]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; rRNA methyltransferase activity [GO:0008649]box C/D snoRNP complex [GO:0031428]; Cajal body [GO:0015030]; dense fibrillar component [GO:0001651]; extracellular exosome [GO:0070062]; granular component [GO:0001652]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239). {ECO:0000269|PubMed:24352239}.P29590PML Protein PMLSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=Isoform PML-1 can shuttle between the nucleus and cytoplasm. Isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 are nuclear isoforms whereas isoform PML-7 and isoform PML-14 lacking the nuclear localization signal are cytoplasmic isoforms. Detected in the nucleolus after DNA damage. Acetylation at Lys-487 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein.0activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell cycle arrest [GO:0007050]; cell fate commitment [GO:0045165]; cellular protein metabolic process [GO:0044267]; cellular response to interleukin-4 [GO:0071353]; cellular senescence [GO:0090398]; circadian regulation of gene expression [GO:0032922]; common-partner SMAD protein phosphorylation [GO:0007182]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; entrainment of circadian clock by photoperiod [GO:0043153]; extrinsic apoptotic signaling pathway [GO:0097191]; fibroblast migration [GO:0010761]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; maintenance of protein location in nucleus [GO:0051457]; myeloid cell differentiation [GO:0030099]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell growth [GO:0030308]; negative < regulation of cell proliferation [GO:0008285]; negative regulation of interleukin-1 beta secretion [GO:0050713]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000059]; negative regulation of telomerase activity [GO:0051974]; negative regulation of telomere maintenance via telomerase [GO:0032211]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of translation in response to oxidative stress [GO:0032938]; negative regulation of viral release from host cell [GO:1902187]; PML body organization [GO:0030578]; positive regulation of apoptotic process involved in mammary gland involution [GO:0060058]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of histone deacetylation [GO:0031065]; post-translational protein modification [GO:0043687]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein complex assembly [GO:0006461]; protein stabilization [GO:0050821]; protein sumoylation [GO:0016925]; protein targeting [GO:0006605]; regulation of calcium ion transport into cytosol [GO:0010522]; regulation of cell adhesion [GO:0030155]; regulation of circadian rhythm [GO:0042752]; regulation of double-strand break repair [GO:2000779]; regulation of MHC class I biosynthetic process [GO:0045343]; regulation of protein phosphorylation [GO:0001932]; regulation of transcription, DNA-templated [GO:0006355]; response to cytokine [GO:0034097]; response to gamma radiation [GO:0010332]; response to hypoxia [GO:0001666]; response to UV [GO:0009411]; retinoic acid receptor signaling pathway [GO:0048384]; SMAD protein import into nucleus [GO:0007184]; transcription, DNA-templated [GO:0006351]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]5cobalt ion binding [GO:0050897]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; SUMO binding [GO:0032183]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]1cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; extrinsic component of endoplasmic reticulum membrane [GO:0042406]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]h FUNCTION: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration.; FUNCTION: Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HCMV) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription.Q9H1B5XYLT2Xylosyltransferase 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.chondroitin sulfate biosynthetic process [GO:0030206]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210]eacetylglucosaminyltransferase activity [GO:0008375]; protein xylosyltransferase activity [GO:0030158]uendoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]sFUNCTION: Probably catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes (By similarity). Its enzyme activity has not been demonstrated. {ECO:0000250}.P98194AT2C1,Calcium-transporting ATPase type 2C member 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12707275}; Multi-pass membrane protein {ECO:0000269|PubMed:12707275}.actin cytoskeleton reorganization [GO:0031532]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cellular calcium ion homeostasis [GO:0006874]; cellular manganese ion homeostasis [GO:0030026]; epidermis development [GO:0008544]; Golgi calcium ion homeostasis [GO:0032468]; Golgi calcium ion transport [GO:0032472]; ion transmembrane transport [GO:0034220]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-transporting ATPase activity [GO:0005388];< manganese ion binding [GO:0030145]; manganese-transporting ATPase activity [GO:0015410]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]tFUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium.Q71F56MD13L;Mediator of RNA polymerase II transcription subunit 13-like)transcription, DNA-templated [GO:0006351]>RNA polymerase II transcription cofactor activity [GO:0001104]mediator complex [GO:0016592]FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway.Q8TCJ2STT3BLDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3BFco-translational protein modification [GO:0043686]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; glycoprotein catabolic process [GO:0006516]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; response to unfolded protein [GO:0006986]Pdolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]FUNCTION: Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient cotranslational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation. Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation. {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:22607976}.Q92878RAD50DNA repair protein RAD50SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents.cellular response to DNA damage stimulus [GO:0006974]; chromosome organization involved in meiosis [GO:0070192]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; positive regulation of kinase activity [GO:0033674]; positive regulation of protein autophosphorylation [GO:0031954]; reciprocal meiotic recombination [GO:0007131]; regulation of mitotic cell cycle [GO:0007346]; regulation of mitotic recombination [GO:0000019]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein binding, bridging [GO:0030674]membrane [GO:0016020]; Mre11 complex [GO:0030870]; nuclear chromosome, telomeric region [GO:0000784]; nucleoplasm [GO:0005654]; pronucleus [GO:0045120]; site of double-strand break [GO:0035861]FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation. {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11741547, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9651580, ECO:0000269|PubMed:9705271}.A6NIZ1RP1BL'Ras-related protein Rap-1b-like proteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=May shuttle between plasma membrane and cytosol. {ECO:0000250}.6small GTPase mediated signal transduction [GO:0007264]P38117ETFB+Electron transfer flavoprotein subunit beta&electron carrier activity [GO:0009055]extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]?FUNCTION: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).Q13263TIF1B(Transcription intermediary factor 1-betaSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177, ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:9016654}. Note=Associated with centromeric heterochromatin during cell differentiation through CBX1. {ECO:0000250}.5convergent extension involved in axis elongation [GO:0060028]; DNA methylation involved in embryo development [GO:0043045]; DNA repair [GO:0006281]; embryo implantation [GO:0007566]; embryonic placenta morphogenesis [GO:0060669]; epithelial to mesenchymal transition [GO:0001837]; gene expression [GO:0010467]; innate immune response [GO:0045087]; negative regulation of DNA demethylation [GO:1901536]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of viral release from host cell [GO:1902187]; positive regulation of DNA repair [GO:0045739]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription factor import into nucleus [GO:0042993]; protein autophosphorylation [GO:0046777]; protein oligomerization [GO:0051259]; protein sumoylation [GO:0016925]; protein ubiquitination [GO:0016567]; regulation of genetic imprinting [GO:2000653]; transcription initiation from RNA polymerase II promoter [GO:0006367]9chromo shadow domain binding [GO:0070087]; DNA binding [GO:0003677]; Krueppel-associated box domain binding [GO:0035851]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0< 004672]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]nuclear euchromatin [GO:0005719]; nuclear heterochromatin [GO:0005720]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription factor complex [GO:0090575]*FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg) (PubMed:23543754). {ECO:0000269|PubMed:10347202, ECO:0000269|PubMed:11959841, ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:16107876, ECO:0000269|PubMed:16862143, ECO:0000269|PubMed:17079232, ECO:0000269|PubMed:17178852, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17942393, ECO:0000269|PubMed:18060868, ECO:0000269|PubMed:18082607, ECO:0000269|PubMed:20424263, ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:21940674, ECO:0000269|PubMed:23543754, ECO:0000269|PubMed:23665872, ECO:0000269|PubMed:8769649, ECO:0000269|PubMed:9016654}.Q6UW02CP20ACytochrome P450 20A1heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]Q9GZS1RPA49+DNA-directed RNA polymerase I subunit RPA49=gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; regulation of gene expression, epigenetic [GO:0040029]; RNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript [GO:0001189]; rRNA transcription [GO:0009303]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]zDNA-directed RNA polymerase I complex [GO:0005736]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF (By similarity). {ECO:0000250}.Q8WXF1PSPC1Paraspeckle component 1SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus speckle. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-dependent manner. May cycles between paraspeckles and nucleolus. In telophase, when daughter nuclei form, localizes to perinucleolar caps.negative regulation of transcription, DNA-templated [GO:0045892]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511]; transcription, DNA-templated [GO:0006351]ecore promoter binding [GO:0001047]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; paraspeckles [GO:0042382]FUNCTION: Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line (By similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Together with NONO, required for the formation of nuclear paraspeckles. {ECO:0000250, ECO:0000269|PubMed:22416126}.Q86SF2GALT7#N-acetylgalactosaminyltransferase 7carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]UFUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.Q13243SRSF5&Serine/arginine-rich splicing factor 5gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; regulation of cell cycle [GO:0051726]; response to wounding [GO:0009611]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]zcytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]kFUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.P51532SMCA4Transcription activator BRG1bSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:20418909}.ATP-dependent chromatin remodeling [GO:0043044]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of cell growth [GO:0030308]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription from RNA polymerase II promoter during mitosis [GO:0007070]; nervous system development [GO:0007399]; neural retina development [GO:0003407]; nucleosome disassembly [GO:0006337]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of pri-miRNA transcription from RNA polymerase II promoter [GO:1902895]; positive regulation of sequence-specific DNA bindin< g transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spermatid development [GO:0007286] androgen receptor binding [GO:0050681]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA-dependent ATPase activity [GO:0008094]; DNA polymerase binding [GO:0070182]; helicase activity [GO:0004386]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039]; protein N-terminus binding [GO:0047485]; RNA polymerase II transcription coactivator activity [GO:0001105]; Tat protein binding [GO:0030957]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]extracellular space [GO:0005615]; membrane [GO:0016020]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]& FUNCTION: Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. {ECO:0000250, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909}.Q15118PDK1N[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrialWarburg EffectPDHA inhibitorISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:22195962}.Tactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cell proliferation [GO:0008283]; cellular metabolic process [GO:0044237]; glucose metabolic process [GO:0006006]; hypoxia-inducible factor-1alpha signaling pathway [GO:0097411]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; protein phosphorylation [GO:0006468]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; regulation of glucose metabolic process [GO:0010906]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]xmitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress. {ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:18541534, ECO:0000269|PubMed:22195962, ECO:0000269|PubMed:7499431}.Q13523PRP4B,Serine/threonine-protein kinase PRP4 homologlmRNA splicing, via spliceosome [GO:0000398]; protein phosphorylation [GO:0006468]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]\catalytic step 2 spliceosome [GO:0071013]; chromosome [GO:0005694]; nucleoplasm [GO:0005654]BFUNCTION: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.O75934SPF27Pre-mRNA-splicing factor SPF27SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12169396, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20176811}.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]cell junction [GO:0030054]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]qFUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000269|PubMed:24332808}.Q13011ECH1:Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrialLSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Peroxisome {ECO:0000250}.&fatty acid beta-oxidation [GO:0006635]>isomerase activity [GO:0016853]; receptor binding [GO:0005102]nextracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]cFUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA. {ECO:0000250}.Q9P2I0CPSF29Cleavage and polyadenylation specificity factor subunit 2gene expression [GO:0010467]; histone mRNA 3'-end processing [GO:0006398]; mRNA 3'-end processing [GO:0031124]; mRNA cleavage [GO:0006379]; mRNA export from nucleus [GO:0006406]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]zmembrane [GO:0016020]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing. {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:18688255}.Q9NUQ2PLCE61-acyl-sn-glycerol-3-phosphate acyltransferase epsilonSUBCELLULAR LOCATION: E< ndoplasmic reticulum membrane {ECO:0000269|PubMed:21173190}; Multi-pass membrane protein {ECO:0000269|PubMed:21173190}. Nucleus envelope {ECO:0000269|PubMed:21173190}. Mitochondrion {ECO:0000269|PubMed:21173190}.CDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; glycerophospholipid biosynthetic process [GO:0046474]; hematopoietic progenitor cell differentiation [GO:0002244]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid biosynthetic process [GO:0008654]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]B1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635] FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable. {ECO:0000269|PubMed:21173190}.Q13427PPIG%Peptidyl-prolyl cis-trans isomerase GSUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:15358154}. Nucleus speckle {ECO:0000269|PubMed:15358154}. Note=Colocalizes with RNA splicing factors at nuclear speckles.kprotein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; RNA splicing [GO:0008380]cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.O43818U3IP2,U3 small nucleolar RNA-interacting protein 2xbox C/D snoRNP complex [GO:0031428]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA.O76062ERG24Delta(14)-sterol reductaseSteroid biosynthesisSUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein {ECO:0000269|PubMed:9878250}.\cholesterol biosynthetic process [GO:0006695]; small molecule metabolic process [GO:0044281].delta14-sterol reductase activity [GO:0050613]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; receptor complex [GO:0043235]aFUNCTION: Involved in the conversion of lanosterol to cholesterol. {ECO:0000269|PubMed:11784322}.P06280AGALAlpha-galactosidase Aglycoside catabolic process [GO:0016139]; glycosphingolipid catabolic process [GO:0046479]; glycosphingolipid metabolic process [GO:0006687]; glycosylceramide catabolic process [GO:0046477]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of nitric-oxide synthase activity [GO:0051001]; oligosaccharide metabolic process [GO:0009311]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]alpha-galactosidase activity [GO:0004557]; catalytic activity [GO:0003824]; galactoside binding [GO:0016936]; hydrolase activity [GO:0016787]; protein homodimerization activity [GO:0042803]; raffinose alpha-galactosidase activity [GO:0052692]; receptor binding [GO:0005102]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]Q99848EBP2%Probable rRNA-processing protein EBP2SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19170763, ECO:0000269|PubMed:2879624}. Note=Associated with the nucleolus in an RNA-dependent manner. ribosome biogenesis [GO:0042254]IFUNCTION: Required for the processing of the 27S pre-rRNA. {ECO:0000250}.Q969G3SMCE1]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1bSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:12192000}.,ATP-dependent chromatin remodeling [GO:0043044]; chromatin remodeling [GO:0006338]; negative regulation of transcription, DNA-templated [GO:0045892]; nervous system development [GO:0007399]; nucleosome disassembly [GO:0006337]; regulation of transcription from RNA polymerase II promoter [GO:0006357]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; ligand-dependent nuclear receptor binding [GO:0016922]; N-acetyltransferase activity [GO:0008080]; protein N-terminus binding [GO:0047485]; RNA binding [GO:0003723]; transcription coactivator activity [GO:0003713]nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]; transcriptional repressor complex [GO:0017053]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by Swi/Snf complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. {ECO:0000250}.Q96QC0PP1RA<Serine/threonine-protein phosphatase 1 regulatory subunit 10_SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:9450550}. Note=Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:0000250}.Sprotein import into nucleus [GO:0006606]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein phosphatase inhibitor activity [GO:0004864]pchromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PTW/PP1 phosphatase complex [GO:0072357]HFUNCTION: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control < of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity). {ECO:0000250}.P27824CALXCalnexin!SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. The palmitoylated form preferentially localizes to the perinuclear rough ER.gaging [GO:0007568]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; chaperone-mediated protein folding [GO:0061077]; clathrin-mediated endocytosis [GO:0072583]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; protein N-linked glycosylation via asparagine [GO:0018279]; protein secretion [GO:0009306]; synaptic vesicle endocytosis [GO:0048488]ecalcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; poly(A) RNA binding [GO:0044822]naxon [GO:0030424]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; ER-mitochondrion membrane contact site [GO:0044233]; extracellular exosome [GO:0070062]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; melanosome [GO:0042470]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; protein complex [GO:0043234]; ribosome [GO:0005840]; rough endoplasmic reticulum [GO:0005791]; smooth endoplasmic reticulum [GO:0005790][FUNCTION: Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.P42126ECI1*Enoyl-CoA delta isomerase 1, mitochondrialcellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; small molecule metabolic process [GO:0044281]idodecenoyl-CoA delta-isomerase activity [GO:0004165]; intramolecular oxidoreductase activity [GO:0016860]vFUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.Q14249NUCGEndonuclease G, mitochondrialaging [GO:0007568]; apoptotic DNA fragmentation [GO:0006309]; cellular response to calcium ion [GO:0071277]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; DNA recombination [GO:0006310]; in utero embryonic development [GO:0001701]; neuron death in response to oxidative stress [GO:0036475]; positive regulation of apoptotic DNA fragmentation [GO:1902512]; positive regulation of hydrogen peroxide-mediated programmed cell death [GO:1901300]; response to antibiotic [GO:0046677]; response to estradiol [GO:0032355]; response to mechanical stimulus [GO:0009612]; response to tumor necrosis factor [GO:0034612]deoxyribonuclease activity [GO:0004536]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nuclease activity [GO:0004518]; nucleic acid binding [GO:0003676]_cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]PFUNCTION: Cleaves DNA at double-stranded (DG)n.(DC)n and at single-stranded (DC)n tracts. In addition to deoxyribonuclease activities, also has ribonuclease (RNase) and RNase H activities. Capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA (By similarity). {ECO:0000250}.Q9UM00TMCO19Transmembrane and coiled-coil domain-containing protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10393320}; Multi-pass membrane protein {ECO:0000269|PubMed:10393320}. Golgi apparatus membrane {ECO:0000269|PubMed:10393320}; Multi-pass membrane protein {ECO:0000269|PubMed:10393320}.endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]Q9GZR7DDX24 ATP-dependent RNA helicase DDX24RRNA metabolic process [GO:0016070]; RNA secondary structure unwinding [GO:0010501]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]; RNA helicase activity [GO:0003724]-membrane [GO:0016020]; nucleolus [GO:0005730]4FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}.Q9NV66TYW1AS-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthasetRNA processing [GO:0008033]4 iron, 4 sulfur cluster binding [GO:0051539]; FMN binding [GO:0010181]; iron ion binding [GO:0005506]; lyase activity [GO:0016829]; oxidoreductase activity [GO:0016491]FUNCTION: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity). {ECO:0000250}.Q9BTV4TMM43Transmembrane protein 43zSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Nucleus inner membrane; Multi-pass membrane protein. Note=Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrophilic domain resides in the endoplasmic reticulum lumen (By similarity). {ECO:0000250}.*nuclear membrane organization [GO:0071763]endoplasmic reticulum lumen [GO:0005788]; Golgi apparatus [GO:0005794]; integral component of nuclear inner membrane [GO:0005639]FUNCTION: May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). {ECO:0000250}.Q15286RAB35Ras-related protein Rab-352SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Endosome. Melanosome. Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes.antigen processing and presentation [GO:0019882]; cellular response to nerve growth factor stimulus [GO:1990090]; cytokinesis [GO:0000910]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; neuron projection development [GO:0031175]; plasma membrane to endosome transport [GO:0048227]; protein localization [GO:0008104]; protein localization to endosome [GO:0036010]; Rab protein signal transduction [GO:0032482]GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546](cell projection membrane [GO:0031253]; clathrin-coated endocytic vesicle [GO:0045334]; coated pit [GO:0005905]; endosome membrane< [GO:0010008]; extracellular exosome [GO:0070062]; intercellular bridge [GO:0045171]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]}FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}.Q96T83SL9A7Sodium/hydrogen exchanger 7SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}.ion transport [GO:0006811]; potassium ion transmembrane transport [GO:0071805]; regulation of pH [GO:0006885]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]potassium:proton antiporter activity [GO:0015386]; protein homodimerization activity [GO:0042803]; sodium:proton antiporter activity [GO:0015385]Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]FUNCTION: Mediates electroneutral exchange of protons for Na(+) and K(+) across endomembranes. May contribute to Golgi volume and cation homeostasis. {ECO:0000269|PubMed:11279194}.O76031CLPXGATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrialRSUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid.positive regulation of peptidase activity [GO:0010952]; protein folding [GO:0006457]; proteolysis involved in cellular protein catabolic process [GO:0051603]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; peptidase activator activity [GO:0016504]cytoplasm [GO:0005737]; endopeptidase Clp complex [GO:0009368]; mitochondrial endopeptidase Clp complex [GO:0009841]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:22710082, ECO:0000269|PubMed:22841477}.Q6NVY1HIBCH03-hydroxyisobutyryl-CoA hydrolase, mitochondrialPropanoate metabolismbranched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; small molecule metabolic process [GO:0044281]; valine catabolic process [GO:0006574]73-hydroxyisobutyryl-CoA hydrolase activity [GO:0003860] FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA. {ECO:0000269|PubMed:8824301}.Q9HAC8UBTD1%Ubiquitin domain-containing protein 1Q86VR2F134CProtein FAM134CQ9UH62ARMX3.Armadillo repeat-containing X-linked protein 3}cellular protein localization [GO:0034613]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]?integral component of mitochondrial outer membrane [GO:0031307]Q8NEW0ZNT7Zinc transporter 7SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12446736}; Multi-pass membrane protein {ECO:0000269|PubMed:12446736}.cellular protein metabolic process [GO:0044267]; sequestering of zinc ion [GO:0032119]; transmembrane transport [GO:0055085]; zinc II ion transport [GO:0006829]6cation transmembrane transporter activity [GO:0008324]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; vesicle [GO:0031982]FUNCTION: Seems to facilitate zinc transport from the cytoplasm into the Golgi apparatus. Partly regulates cellular zinc homeostasis. Required with ZNT5 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and the vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT5 and ZNT6 for the activation of TNAP (By similarity). {ECO:0000250}.O15321TM9S1$Transmembrane 9 superfamily member 1SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19029833}; Multi-pass membrane protein {ECO:0000269|PubMed:19029833}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:19029833}; Multi-pass membrane protein {ECO:0000269|PubMed:19029833}.autophagy [GO:0006914]autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]NFUNCTION: Plays an essential role in autophagy. {ECO:0000269|PubMed:19029833}.Q709F0ACD11'Acyl-CoA dehydrogenase family member 11SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:21237683}. Note=Has been detected associated with mitochondrial membrane, but no matrix, in kidney and cerebellum, as well as in a neuroblastoma cell line, but not in skin fibroblasts, where it is observed in cytoplasmic vesicles (PubMed:21237683). No mitochondrial targeting signals could be predicted for any known isoform, including a putative isoform starting at Met-316. {ECO:0000269|PubMed:21237683}.cfatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; long-chain-acyl-CoA dehydrogenase activity [GO:0004466]; medium-chain-acyl-CoA dehydrogenase activity [GO:0070991]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]; very-long-chain-acyl-CoA dehydrogenase activity [GO:0017099]Rmitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; peroxisome [GO:0005777]zFUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. {ECO:0000269|PubMed:21237683}.Q9Y4B6VPRBP Protein VPRBPSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis.nB cell differentiation [GO:0030183]; cell competition in a multicellular organism [GO:0035212]; histone H2A-T120 phosphorylation [GO:1990245]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; protein ubiquitination [GO:0016567]; transcription, DNA-templated [GO:0006351]; V(D)J recombination [GO:0033151]; viral process [GO:0016032]RATP binding [GO:0005524]; histone kinase activity (H2A-T120 specific) [GO:1990244]Dcytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]` FUNCTION: Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and < histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: VPRBP is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. {ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17559673, ECO:0000269|PubMed:17609381, ECO:0000269|PubMed:17620334, ECO:0000269|PubMed:17626091, ECO:0000269|PubMed:17630831, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18464893, ECO:0000269|PubMed:18524771, ECO:0000269|PubMed:18606781, ECO:0000269|PubMed:19264781, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:19923175, ECO:0000269|PubMed:20644714, ECO:0000269|PubMed:22184063, ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:24116224, ECO:0000269|PubMed:24140421, ECO:0000269|PubMed:24336198}.Q92820GGHGamma-glutamyl hydrolaseSUBCELLULAR LOCATION: Secreted, extracellular space. Lysosome. Melanosome. Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.glutamine metabolic process [GO:0006541]; proteolysis [GO:0006508]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to zinc ion [GO:0010043]yexopeptidase activity [GO:0008238]; gamma-glutamyl-peptidase activity [GO:0034722]; omega peptidase activity [GO:0008242]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosome [GO:0005764]; melanosome [GO:0042470]; nucleus [GO:0005634]oFUNCTION: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.Q92544TM9S4$Transmembrane 9 superfamily member 4P43304GPDM1Glycerol-3-phosphate dehydrogenase, mitochondrial.camera-type eye development [GO:0043010]; cellular lipid metabolic process [GO:0044255]; gluconeogenesis [GO:0006094]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerol catabolic process [GO:0019563]; multicellular organism growth [GO:0035264]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; glycerol-3-phosphate dehydrogenase activity [GO:0004368]; sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity [GO:0052591]bglycerol-3-phosphate dehydrogenase complex [GO:0009331]; mitochondrial inner membrane [GO:0005743]O43505B3GN1>N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferaseSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:23359570}. Note=Localizes near the trans-Golgi apparatus. {ECO:0000269|PubMed:25279699}.taxon guidance [GO:0007411]; carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; poly-N-acetyllactosamine biosynthetic process [GO:0030311]; protein O-linked mannosylation [GO:0035269]; small molecule metabolic process [GO:0044281]glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity [GO:0008532]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of Golgi membrane [GO:0030173]pFUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosphorylated O-mannosyl glycan (PubMed:25279699, PubMed:25279697). Phosphorylated O-mannosyl glycan is a carbohydrate is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279699, PubMed:25279697). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity). {ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.Q9NSE4SYIM&Isoleucine--tRNA ligase, mitochondrialgene expression [GO:0010467]; isoleucyl-tRNA aminoacylation [GO:0006428]; mitochondrial translation [GO:0032543]; tRNA aminoacylation for protein translation [GO:0006418]taminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; isoleucine-tRNA ligase activity [GO:0004822]kcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]Q8WYA6CTBL1Beta-catenin-like protein 1dSUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}.apoptotic process [GO:0006915]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of apoptotic process [GO:0043065]; RNA splicing [GO:0008380]; somatic diversification of immunoglobulins [GO:0016445]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis.Q8N5A5ZGPAT<Zinc finger CCCH-type with G patch domain-containing proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19644445}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus {ECO:0000269|PubMed:20233718}.negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated < [GO:0006351]metal ion binding [GO:0046872]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration. Its ability to repress genes of the EGFR pathway suggest it may act as a tumor suppressor. Able to suppress breast carcinogenesis. {ECO:0000269|PubMed:19644445}.; FUNCTION: Isoform 4: Antagonizes the transcription repression by isoform 1 by competing for the binding of the NuRD complex. Does not bind DNA. {ECO:0000269|PubMed:19644445}.Q99470SDF2Stromal cell-derived factor 2Oprotein glycosylation [GO:0006486]; protein O-linked mannosylation [GO:0035269]Ldolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]7extracellular space [GO:0005615]; membrane [GO:0016020]Q8WVX9FACR1Fatty acyl-CoA reductase 1SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:24108123}; Single-pass membrane protein {ECO:0000269|PubMed:24108123}.#cellular lipid metabolic process [GO:0044255]; ether lipid biosynthetic process [GO:0008611]; glycerophospholipid biosynthetic process [GO:0046474]; long-chain fatty-acyl-CoA metabolic process [GO:0035336]; small molecule metabolic process [GO:0044281]; wax biosynthetic process [GO:0010025]{fatty-acyl-CoA reductase (alcohol-forming) activity [GO:0080019]; long-chain-fatty-acyl-CoA reductase activity [GO:0050062]integral component of membrane [GO:0016021]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols. {ECO:0000269|PubMed:15220348}.Q6UWJ1TMCO39Transmembrane and coiled-coil domain-containing protein 3.solute:proton antiporter activity [GO:0015299]8FUNCTION: Probable Na(+)/H(+) antiporter. {ECO:0000250}.Q8WTV0SCRB1#Scavenger receptor class B member 1SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane, caveola; Multi-pass membrane protein. Note=Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae.adhesion of symbiont to host [GO:0044406]; androgen biosynthetic process [GO:0006702]; blood vessel endothelial cell migration [GO:0043534]; cell adhesion [GO:0007155]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; detection of lipopolysaccharide [GO:0032497]; endothelial cell proliferation [GO:0001935]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; lipopolysaccharide transport [GO:0015920]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle clearance [GO:0034383]; phospholipid transport [GO:0015914]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of triglyceride biosynthetic process [GO:0010867]; receptor-mediated endocytosis [GO:0006898]; recognition of apoptotic cell [GO:0043654]; regulation of phagocytosis [GO:0050764]; regulation of phosphatidylcholine catabolic process [GO:0010899]; reverse cholesterol transport [GO:0043691]; small molecule metabolic process [GO:0044281]; triglyceride homeostasis [GO:0070328]; viral process [GO:0016032]; vitamin transmembrane transport [GO:0035461]; wound healing [GO:0042060]1-phosphatidylinositol binding [GO:0005545]; apolipoprotein A-I binding [GO:0034186]; apolipoprotein binding [GO:0034185]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor activity [GO:0070506]; lipopolysaccharide binding [GO:0001530]; lipopolysaccharide receptor activity [GO:0001875]; low-density lipoprotein particle binding [GO:0030169]; phosphatidylserine binding [GO:0001786]; transporter activity [GO:0005215]caveola [GO:0005901]; cell surface [GO:0009986]; endocytic vesicle membrane [GO:0030666]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]FUNCTION: Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate. Plays an important role in the uptake of HDL cholesteryl ester (By similarity). {ECO:0000250}.Q6UVK1CSPG4"Chondroitin sulfate proteoglycan 4SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Note=Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. Localizes to the plasma membrane of oligodendrocytes (By similarity). {ECO:0000250}.activation of MAPK activity [GO:0000187]; angiogenesis [GO:0001525]; carbohydrate metabolic process [GO:0005975]; cell proliferation [GO:0008283]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; glial cell migration [GO:0008347]; glycosaminoglycan metabolic process [GO:0030203]; intracellular signal transduction [GO:0035556]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; small molecule metabolic process [GO:0044281]; tissue remodeling [GO:0048771]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]3apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; lamellipodium membrane [GO:0031258]; lysosomal lumen [GO:0043202]FUNCTION: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation< . May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. {ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:11278606, ECO:0000269|PubMed:15210734}.Q9NW15ANO10 Anoctamin-10USUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane.cation transmembrane transport [GO:0098655]; cation transport [GO:0006812]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]~calcium activated cation channel activity [GO:0005227]; intracellular calcium activated chloride channel activity [GO:0005229]FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.O43852CALU CalumeninSUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Secreted. Melanosome. Sarcoplasmic reticulum lumen {ECO:0000250}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.blood coagulation [GO:0007596]; peripheral nervous system axon regeneration [GO:0014012]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; response to organic cyclic compound [GO:0014070]Hcalcium ion binding [GO:0005509]; enzyme inhibitor activity [GO:0004857]endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane [GO:0016020]; sarcoplasmic reticulum lumen [GO:0033018]FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250}.P62314SMD1%Small nuclear ribonucleoprotein Sm D1U1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:18984161}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.yactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; positive regulation of defense response to virus by host [GO:0002230]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]ecatalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U4 snRNP [GO:0005687]FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.Q15428SF3A2Splicing factor 3A subunit 2ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]Q9NPA0EMC7%ER membrane protein complex subunit 7SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22119785}; Single-pass type I membrane protein {ECO:0000269|PubMed:22119785}.!carbohydrate binding [GO:0030246]UER membrane protein complex [GO:0072546]; integral component of membrane [GO:0016021]O15258RER1 Protein RER1LSUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein.positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]cell surface [GO:0009986]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; integral component of Golgi membrane [GO:0030173]FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}.P35914HMGCL.Hydroxymethylglutaryl-CoA lyase, mitochondrial" Metabolic intermediate metabolism]SUBCELLULAR LOCATION: Mitochondrion matrix. Peroxisome. Note=Unprocessed form is peroxisomal.acyl-CoA metabolic process [GO:0006637]; cellular ketone body metabolic process [GO:0046950]; cellular lipid metabolic process [GO:0044255]; ketone body biosynthetic process [GO:0046951]; leucine catabolic process [GO:0006552]; liver development [GO:0001889]; mitochondrion organization [GO:0007005]; protein tetramerization [GO:0051262]; response to fatty acid [GO:0070542]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]7carboxylic acid binding [GO:0031406]; fatty-acyl-CoA binding [GO:0000062]; hydroxymethylglutaryl-CoA lyase activity [GO:0004419]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]jFUNCTION: Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism. {ECO:0000269|PubMed:22847177, ECO:0000269|PubMed:22865860, ECO:0000269|PubMed:8566388}.Q8IWB9TEX2#Testis-expressed sequence 2 proteinMsignal transduction [GO:0007165]; sphingolipid metabolic process [GO:0006665]Q9P0U4CXXC1CXXC-type zinc finger protein 1SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12200428, ECO:0000269|PubMed:17355966}. Note=Associated with euchromatin. During mitosis, excluded from condensed chromosomes.qcellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; histone H3-K4 methylation [GO:0051568]; IRE1-mediated unfolded protein response [GO:0036498]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]core promoter proximal region sequence-specific DNA binding [GO:0000987]; unmethylated CpG binding [GO:0045322]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; histone methyltransferase complex [GO:0035097]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]FUNCTION: Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG. {ECO:0000269|PubMed:21407193}.O95292VAPB:Vesicle-associated membrane protein-associated protein B/C-SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Present in mitochondria-associated membranes that are endoplasmic reticulu< m membrane regions closely apposed to the outer mitochondrial membrane. {ECO:0000269|PubMed:22131369}.activation of signaling protein activity involved in unfolded protein response [GO:0006987]; cellular calcium ion homeostasis [GO:0006874]; COPII-coated vesicle budding [GO:0090114]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER to Golgi vesicle-mediated transport [GO:0006888]; modulation by virus of host morphology or physiology [GO:0019048]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation by host of viral release from host cell [GO:0044790]; negative regulation by virus of viral protein levels in host cell [GO:0046725]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation by host of viral release from host cell [GO:0044791]; positive regulation of viral genome replication [GO:0045070]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]beta-tubulin binding [GO:0048487]; enzyme binding [GO:0019899]; FFAT motif binding [GO:0033149]; microtubule binding [GO:0008017]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. {ECO:0000269|PubMed:16891305, ECO:0000269|PubMed:20940299, ECO:0000269|PubMed:22131369}.Q14766LTBP18Latent-transforming growth factor beta-binding protein 1extracellular matrix organization [GO:0030198]; sequestering of TGFbeta in extracellular matrix [GO:0035583]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]calcium ion binding [GO:0005509]; microfibril binding [GO:0050436]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; microfibril [GO:0001527]; proteinaceous extracellular matrix [GO:0005578]; protein complex [GO:0043234]FUNCTION: May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).Q9NVH0EXD2-Exonuclease 3'-5' domain-containing protein 28nucleic acid phosphodiester bond hydrolysis [GO:0090305]J3'-5' exonuclease activity [GO:0008408]; nucleic acid binding [GO:0003676]P04843RPN1HDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.Wcellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; gene expression [GO:0010467]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]rdolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; poly(A) RNA binding [GO:0044822]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; melanosome [GO:0042470]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.Q96LW7BINCABcl10-interacting CARD proteinSUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:23633586}. Note=Coexpression with BCL10 induced translocation from nucleus to cytosol.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23633586}; Single-pass membrane protein {ECO:0000269|PubMed:23633586}. Mitochondrion membrane {ECO:0000269|PubMed:23633586}; Single-pass membrane protein {ECO:0000269|PubMed:23633586}.Gnegative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124] CARD domain binding [GO:0050700]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]FUNCTION: Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner. {ECO:0000269|PubMed:15637807}.Q96K49TM87BTransmembrane protein 87BQ1KMD3HNRL28Heterogeneous nuclear ribonucleoprotein U-like protein 2=SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00PI9}.+membrane [GO:0016020]; nucleus [GO:0005634]P43243MATR3Matrin-3%SUBCELLULAR LOCATION: Nucleus matrix.>posttranscriptional regulation of gene expression [GO:0010608]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270]qmembrane [GO:0016020]; nuclear inner membrane [GO:0005637]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] FUNCTION: May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. {ECO:0000269|PubMed:11525732}.O95476CNEP1"CTD nuclear envelope phosphatase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.gamete generation [GO:0007276]; mesoderm development [GO:0007498]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; nuclear envelope organization [GO:0006998]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of triglyceride biosynthetic process [GO:0010867]; protein dephosphorylation [GO:0006470]; protein localization to nucleus [GO:0034504]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; Nem1-Spo7 phosphatase complex [GO:0071595]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling. {ECO:0000269|PubMed:17420445, ECO:0000269|PubMed:22134922}.Q9Y4C8RBM19Probable RNA-binding protein 19SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16027046}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In discrete foci distributed throughout the cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula stage, but not in the periphery of the nucleolar precursor body (NPB). During blastocyst development, becomes increasingly localized to the nucleolus and less to the cytoplasm. At the late blastocyst stage, localized predominantly in the nucleolus. Localized in the nucleolus during interphase and to the perichromosomal sheath during mitosis. Does not colocalize in the cytoplasm wit< h GW182 in P-bodies. May translocate to the nucleolus upon early embryonic development (By similarity). Colocalizes with NPM1 during interphase. By late prophase, metaphase, anaphase and telophase, associates with the chromosome periphery. By telophase localizes to NPB. {ECO:0000250}.lmulticellular organismal development [GO:0007275]; positive regulation of embryonic development [GO:0040019]chromosome [GO:0005694]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]MFUNCTION: Plays a role in embryo pre-implantation development. {ECO:0000250}.Q86XE3MICU3'Calcium uptake protein 3, mitochondrialvSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.IFUNCTION: May play a role in mitochondrial calcium uptake. {ECO:0000250}.O60941DTNBDystrobrevin beta,cytoplasm [GO:0005737]; synapse [GO:0045202]P36551HEM6>Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial8SUBCELLULAR LOCATION: Mitochondrion intermembrane space.heme biosynthetic process [GO:0006783]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to arsenic-containing substance [GO:0046685]; response to insecticide [GO:0017085]; response to iron ion [GO:0010039]; response to lead ion [GO:0010288]; response to methylmercury [GO:0051597]; small molecule metabolic process [GO:0044281]coproporphyrinogen oxidase activity [GO:0004109]; protein homodimerization activity [GO:0042803]; structural constituent of eye lens [GO:0005212]cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.P45877PPIC%Peptidyl-prolyl cis-trans isomerase CPprotein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]]cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]Q76FK4NOL8Nucleolar protein 8SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15132771, ECO:0000269|PubMed:16963496}. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis.kDNA replication [GO:0006260]; positive regulation of cell growth [GO:0030307]; rRNA processing [GO:0006364]_FUNCTION: Plays an essential role in the survival of diffuse-type gastric cancer cells. Acts as a nucleolar anchoring protein for DDX47. May be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells. {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771, ECO:0000269|PubMed:16963496}.Q8NBS9TXND5'Thioredoxin domain-containing protein 5YSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}..apoptotic cell clearance [GO:0043277]; cell redox homeostasis [GO:0045454]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; post-Golgi vesicle-mediated transport [GO:0006892]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]1protein disulfide isomerase activity [GO:0003756]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]FUNCTION: Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). {ECO:0000250}.P08476INHBAInhibin beta A chain activin receptor signaling pathway [GO:0032924]; cell-cell signaling [GO:0007267]; cell cycle arrest [GO:0007050]; cell development [GO:0048468]; cell differentiation [GO:0030154]; cell surface receptor signaling pathway [GO:0007166]; cellular response to cholesterol [GO:0071397]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; defense response [GO:0006952]; endodermal cell differentiation [GO:0035987]; erythrocyte differentiation [GO:0030218]; extrinsic apoptotic signaling pathway [GO:0097191]; eyelid development in camera-type eye [GO:0061029]; G1/S transition of mitotic cell cycle [GO:0000082]; GABAergic neuron differentiation [GO:0097154]; growth [GO:0040007]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; mesodermal cell differentiation [GO:0048333]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of follicle-stimulating hormone secretion [GO:0046882]; negative regulation of interferon-gamma biosynthetic process [GO:0045077]; negative regulation of macrophage differentiation [GO:0045650]; negative regulation of phosphorylation [GO:0042326]; nervous system development [GO:0007399]; odontogenesis [GO:0042476]; ovarian follicle development [GO:0001541]; palate development [GO:0060021]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of follicle-stimulating hormone secretion [GO:0046881]; positive regulation of gene expression [GO:0010628]; positive regulation of ovulation [GO:0060279]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; progesterone secretion [GO:0042701]; regulation of follicle-stimulating hormone secretion [GO:0046880]; regulation of MAPK cascade [GO:0043408]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to drug [GO:0042493]; SMAD protein signal transduction [GO:0060395]; striatal medium spiny neuron differentiation [GO:0021773]cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; peptide hormone binding [GO:0017046]; transforming growth factor beta receptor binding [GO:0005160]; type II activin receptor binding [GO:0070699]activin A complex [GO:0043509]; cell [GO:0005623]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512]FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.Q96DF8DGC14Protein DGCR14TmRNA splicing, via spliceosome [GO:0000398]; nervous system development [GO:0007399]?catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]/FUNCTION: May be involved in pre-mRNA splicing.O43166SI1L18Signal-induced proliferation-associated 1-like protein 1^SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons (By similarity). {ECO:0000250}.actin cytoskeleton reorganization [GO:0031532]; activation of GTPase activity [GO:0090630]; ephrin receptor signaling pathway [GO:0048013]; regulation of axonogenesis [GO:0050770]; regulation of dendritic spine morphogenesi< s [GO:0061001]; regulation of GTPase activity [GO:0043087]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of synaptic plasticity [GO:0048167]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity). {ECO:0000250}.Q9Y6R1S4A4/Electrogenic sodium bicarbonate cotransporter 1SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:15273250, ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:17661077}; Multi-pass membrane protein {ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:15273250}.)anion transmembrane transport [GO:0098656]; bicarbonate transport [GO:0015701]; ion transport [GO:0006811]; regulation of intracellular pH [GO:0051453]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085]; transport [GO:0006810]cinorganic anion exchanger activity [GO:0005452]; sodium:bicarbonate symporter activity [GO:0008510]basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886] FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH. {ECO:0000269|PubMed:10069984, ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:17661077, ECO:0000269|PubMed:9235899, ECO:0000269|PubMed:9651366}.; FUNCTION: Isoform 2: May have a higher activity than isoform 1. {ECO:0000269|PubMed:16769890}.O43306ADCY6Adenylate cyclase type 6cSUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, cilium {ECO:0000250}.activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; cAMP biosynthetic process [GO:0006171]; cellular response to catecholamine stimulus [GO:0071870]; cellular response to glucagon stimulus [GO:0071377]; cellular response to prostaglandin E stimulus [GO:0071380]; dopamine receptor signaling pathway [GO:0007212]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative regulation of neuron projection development [GO:0010977]; neurotrophin TRK receptor signaling pathway [GO:0048011]; renal water homeostasis [GO:0003091]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; water transport [GO:0006833]adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]cilium [GO:0005929]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; membrane [GO:0016020]; plasma membrane [GO:0005886]NFUNCTION: Membrane-bound, calcium-inhibitable adenylyl cyclase. {ECO:0000250}.Q96N66MBOA7"Lysophospholipid acyltransferase 7(glycerophospholipid biosynthetic process [GO:0046474]; layer formation in cerebral cortex [GO:0021819]; phosphatidylinositol acyl-chain remodeling [GO:0036149]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; ventricular system development [GO:0021591]6lysophospholipid acyltransferase activity [GO:0071617]FUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:18772128}.Q9NUI1DECR2%Peroxisomal 2,4-dienoyl-CoA reductase/SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.8unsaturated fatty acid biosynthetic process [GO:0006636]2,4-dienoyl-CoA reductase (NADPH) activity [GO:0008670]; receptor binding [GO:0005102]; trans-2-enoyl-CoA reductase (NADPH) activity [GO:0019166]peroxisome [GO:0005777]FUNCTION: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.Q9BSJ8ESYT1Extended synaptotagmin-1>SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Peripheral membrane protein. Note=Localizes primarily to the endoplasmic reticulum. Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels.Ametal ion binding [GO:0046872]; phospholipid binding [GO:0005543]endoplasmic reticulum [GO:0005783]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]; organelle membrane contact site [GO:0044232]; plasma membrane [GO:0005886]FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. {ECO:0000250, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24183667}.Q13445TMED1/Transmembrane emp24 domain-containing protein 1`SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein.bcell-cell signaling [GO:0007267]; protein transport [GO:0015031]; signal transduction [GO:0007165]receptor binding [GO:0005102]Gendoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.O00116ADAS4Alkyldihydroxyacetonephosphate synthase, peroxisomal Glycerolipid metabolismjSUBCELLULAR LOCATION: Peroxisome membrane. Note=Localized to the inner aspect of the peroxisomal membrane.cellular lipid metabolic process [GO:0044255]; ether lipid biosynthetic process [GO:0008611]; lipid biosynthetic process [GO:0008610]; small molecule metabolic process [GO:0044281]alkylglyc< erone-phosphate synthase activity [GO:0008609]; FAD binding [GO:0071949]; UDP-N-acetylmuramate dehydrogenase activity [GO:0008762]intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. {ECO:0000250}.Q8N766EMC1%ER membrane protein complex subunit 1Q96S66CLCC1$Chloride channel CLIC-like protein 1SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum. Golgi apparatus. Nucleus {ECO:0000250}.&chloride channel activity [GO:0005254]chloride channel complex [GO:0034707]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]@FUNCTION: Seems to act as a chloride ion channel. {ECO:0000250}.P80303NUCB2Nucleobindin-2SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11749975}. Membrane {ECO:0000269|PubMed:11749975}; Peripheral membrane protein {ECO:0000269|PubMed:11749975}. Cytoplasm {ECO:0000269|PubMed:11749975}. Secreted {ECO:0000269|PubMed:11749975}. Endoplasmic reticulum {ECO:0000250}. Nucleus envelope {ECO:0000250}. Note=Golgi retention is mediated by its N-terminal region.; SUBCELLULAR LOCATION: Nesfatin-1: Secreted.:calcium ion binding [GO:0005509]; DNA binding [GO:0003677]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]FUNCTION: Calcium-binding protein. May have a role in calcium homeostasis.; FUNCTION: Nesfatin-1: Anorexigenic peptide, seems to play an important role in hypothalamic pathways regulating food intake and energy homeostasis, acting in a leptin-independent manner. May also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance (By similarity). {ECO:0000250}.Q92466DDB2DNA damage-binding protein 2fSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10777490, ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11705987, ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16713579, ECO:0000269|PubMed:17635991, ECO:0000269|PubMed:18593899}. Note=Accumulates at sites of DNA damage following UV irradiation.gDNA repair [GO:0006281]; histone H2A monoubiquitination [GO:0035518]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; pyrimidine dimer repair [GO:0006290]; response to UV [GO:0009411]; UV-damage excision repair [GO:0070914]:damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]cell junction [GO:0030054]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]QFUNCTION: Required for DNA repair. Binds to DDB1 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as the substrate recognition module for the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. The DDB1-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA repair. {ECO:0000269|PubMed:10882109, ECO:0000269|PubMed:11278856, ECO:0000269|PubMed:11705987, ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:9892649}.O15118NPC1Niemann-Pick C1 protein%minor lysosomal membrane proteins(20)SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319}.adult walking behavior [GO:0007628]; autophagy [GO:0006914]; bile acid metabolic process [GO:0008206]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to steroid hormone stimulus [GO:0071383]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; endocytosis [GO:0006897]; establishment of protein localization to membrane [GO:0090150]; lysosomal transport [GO:0007041]; membrane raft organization [GO:0031579]; negative regulation of cell death [GO:0060548]; negative regulation of macroautophagy [GO:0016242]; positive regulation of cholesterol homeostasis [GO:2000189]; protein glycosylation [GO:0006486]; response to cadmium ion [GO:0046686]; response to drug [GO:0042493]; signal transduction [GO:0007165]; viral entry into host cell [GO:0046718]cholesterol binding [GO:0015485]; hedgehog receptor activity [GO:0008158]; receptor activity [GO:0004872]; sterol transporter activity [GO:0015248]; transmembrane signaling receptor activity [GO:0004888]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]<FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals. {ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:19563754}.Q3SXM5HSDL14Inactive hydroxysteroid dehydrogenase-like protein 1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19026618}.P49184DNSL1Deoxyribonuclease-1-like 1JSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:16107205}.WDNA catabolic process, endonucleolytic [GO:0000737]; DNA metabolic process [GO:0006259]deoxyribonuclease activity [GO:0004536]; DNA binding [GO:0003677]; endodeoxyribonuclease activity [GO:0004520]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]\endoplasmic reticulum [GO:0005783]; extrac< ellular exosome [GO:0070062]; nucleus [GO:0005634]O75746CMC15Calcium-binding mitochondrial carrier protein Aralar1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:9722566}; Multi-pass membrane protein {ECO:0000269|PubMed:9722566}.aspartate transport [GO:0015810]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; L-aspartate transmembrane transport [GO:0089712]; L-glutamate transmembrane transport [GO:0089711]; L-glutamate transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle. {ECO:0000269|PubMed:11566871}.Q9NWB6ARGL1%Arginine and glutamate-rich protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454576}. Note=Recruited, in an estrogen-dependent manner, to ESR1 target gene promoters. Colocalizes with MED1.4mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Required for the estrogen-dependent expression of ESR1 target genes. Can act in cooperation with MED1. {ECO:0000269|PubMed:21454576}.Q15165PON2 Serum paraoxonase/arylesterase 2xSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11579088}; Peripheral membrane protein {ECO:0000269|PubMed:11579088}.[aromatic compound catabolic process [GO:0019439]; response to oxidative stress [GO:0006979]jarylesterase activity [GO:0004064]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]extracellular region [GO:0005576]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]sFUNCTION: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis. {ECO:0000269|PubMed:11579088, ECO:0000269|PubMed:15772423}.O43251RFOX2#RNA binding protein fox-1 homolog 27SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}./dendrite morphogenesis [GO:0048813]; intracellular estrogen receptor signaling pathway [GO:0030520]; mRNA processing [GO:0006397]; negative regulation of transcription, DNA-templated [GO:0045892]; neuromuscular process controlling balance [GO:0050885]; radial glia guided migration of Purkinje cell [GO:0021942]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of cell proliferation [GO:0042127]; regulation of definitive erythrocyte differentiation [GO:0010724]; RNA metabolic process [GO:0016070]; RNA splicing [GO:0008380]mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha. {ECO:0000250, ECO:0000269|PubMed:11875103}.P61803DAD1KDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1nSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; cellular protein metabolic process [GO:0044267]; negative regulation of apoptotic process [GO:0043066]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279]; response to drug [GO:0042493]; response to nutrient [GO:0007584]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]2FUNCTION: Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis (By similarity). {ECO:0000250}.O60669MOT2Monocarboxylate transporter 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:9786900}; Multi-pass membrane protein {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:9786900}.lactate transmembrane transport [GO:0035873]; plasma membrane lactate transport [GO:0035879]; pyruvate transmembrane transport [GO:1901475]; transmembrane transport [GO:0055085]lactate transmembrane transporter activity [GO:0015129]; pyruvate secondary active transmembrane transporter activity [GO:0005477]; pyruvate transmembrane transporter activity [GO:0050833]; symporter activity [GO:0015293]hcytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]}FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Functions as high-affinity pyruvate transporter. {ECO:0000269|PubMed:9786900}.Q15005SPCS2"Signal peptidase complex subunit 2SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.-cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; protein targeting to ER [GO:0045047]; regulation of insulin secretion [GO:0050796]; signal peptide processing [GO:0006465]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]peptidase activity [GO:0008233]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; signal peptidase complex [GO:0005787]Q9P035HACD34Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:18554506}.activation of JUN kinase activity [GO:0007257]; fatty acid elongation [GO:0030497]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; positive regulation by virus of viral protein levels in host cell [GO:0046726]; positive regulation of GTPase activity [GO:0043547]; positive regulation of viral genome replication [GO:0045070]; Rac protein signal transduction [GO:0016601]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; very long-chain fatty acid biosynthetic process [GO:0042761]x3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]FUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of tw< o carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May be involved in Rac1-signaling pathways leading to the modulation of gene expression. {ECO:0000269|PubMed:10747961, ECO:0000269|PubMed:18554506}.O95140MFN2 Mitofusin-2fSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051}; Multi-pass membrane protein {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051}. Note=Colocalizes with BAX during apoptosis.Mapoptotic process [GO:0006915]; autophagy [GO:0006914]; blastocyst formation [GO:0001825]; blood coagulation [GO:0007596]; camera-type eye morphogenesis [GO:0048593]; mitochondrial fusion [GO:0008053]; mitochondrial membrane organization [GO:0007006]; mitochondrion localization [GO:0051646]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of smooth muscle cell proliferation [GO:0048662]; protein localization to pre-autophagosomal structure [GO:0034497]; protein targeting to mitochondrion [GO:0006626]; response to unfolded protein [GO:0006986]eGTPase activity [GO:0003924]; GTP binding [GO:0005525]; ubiquitin protein ligase binding [GO:0031625]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intrinsic component of mitochondrial outer membrane [GO:0031306]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]GFUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN2 acts independently of the cytoskeleton. It therefore plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Overexpression induces the formation of mitochondrial networks. Plays an important role in the regulation of vascular smooth muscle cell proliferation. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PARK2 recruitment to dysfunctional mitochondria. Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress. Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions. {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:15322553, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23921378}.Q8NBU5ATAD1-ATPase family AAA domain-containing protein 1qSUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}.cytoplasmic microtubule organization [GO:0031122]; learning [GO:0007612]; memory [GO:0007613]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; positive regulation of receptor internalization [GO:0002092]iATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule-severing ATPase activity [GO:0008568]cell junction [GO:0030054]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; postsynaptic membrane [GO:0045211]mFUNCTION: ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity). {ECO:0000250}.Q8IV08PLD3Phospholipase D3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15794758}; Single-pass type II membrane protein {ECO:0000269|PubMed:15794758}.glycerophospholipid biosynthetic process [GO:0046474]; lipid catabolic process [GO:0016042]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]tN-acylphosphatidylethanolamine-specific phospholipase D activity [GO:0070290]; phospholipase D activity [GO:0004630]|endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]MFUNCTION: Probably involved in APP processing. {ECO:0000269|PubMed:24336208}.P215895NTD5'-nucleotidase>SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.adenosine biosynthetic process [GO:0046086]; AMP catabolic process [GO:0006196]; brain development [GO:0007420]; DNA metabolic process [GO:0006259]; leukocyte cell-cell adhesion [GO:0007159]; negative regulation of inflammatory response [GO:0050728]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of lipid biosynthetic process [GO:0046889]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]; purine nucleotide catabolic process [GO:0006195]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside catabolic process [GO:0046135]; response to aluminum ion [GO:0010044]; small molecule metabolic process [GO:0044281]i5'-nucleotidase activity [GO:0008253]; ferrous iron binding [GO:0008198]; nucleotide binding [GO:0000166]anchored component of membrane [GO:0031225]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synaptic membrane [GO:0097060]FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. {ECO:0000269|PubMed:21933152}.Q9Y4W6AFG32AFG3-like protein 2SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:10395799}; Multi-pass membrane protein {ECO:0000269|PubMed:10395799}.axonogenesis [GO:0007409]; cristae formation [GO:0042407]; death [GO:0016265]; mitochondrial fusion [GO:0008053]; mitochondrial protein processing [GO:0034982]; muscle fiber development [GO:0048747]; myelination [GO:0042552]; nerve development [GO:0021675]; neuromuscular junction development [GO:0007528]; regulation of multicellular organism growth [GO:0040014]; righting reflex [GO:0060013]ATP binding [GO:0005524]; metalloendopeptidase activity [GO:0004222]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270]ZFUNCTION: ATP-dependent protease which is essential for axonal development. {ECO:0000250}.P51659DHB4)Peroxisomal multifunctional enzyme type 2!SUBCELLULAR LOCATION: Peroxisome.alpha-linolenic acid metabolic process [GO:0036109]; androgen metabolic process [GO:0008209]; bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; cellular lipid metabolic process [GO:0044255]; estrogen metabolic process [GO:0008210]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; medium-chain fatty-acyl-CoA metabolic process [GO:0036112]; osteoblast differentiation [GO:0001649]; oxidation-reduction process [GO:0055114]; Sertoli cell development [GO:0060009]; small molecule metabolic process [GO:0044281]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid metabolic process [GO:0000038]; very long-chain fatty-acyl-CoA metabolic process [GO:0036111]{17-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0044594]; 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity [GO:0033989]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; isomerase activity [GO:0016853]; long-chain-enoyl-CoA hydratase activity [GO:0016508]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]intracellular membrane-bounded organelle [< GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. {ECO:0000269|PubMed:8902629, ECO:0000269|PubMed:9089413}.Q9HDC9APMAP,Adipocyte plasma membrane-associated proteinSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18513186}; Single-pass type II membrane protein {ECO:0000269|PubMed:18513186}.!biosynthetic process [GO:0009058]Parylesterase activity [GO:0004064]; strictosidine synthase activity [GO:0016844]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. May play a role in adipocyte differentiation. {ECO:0000269|PubMed:18513186}.Q9NV96CC50ACell cycle control protein 50ASUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}. Apical cell membrane {ECO:0000250}.drug transmembrane transport [GO:0006855]; phospholipid translocation [GO:0045332]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein exit from endoplasmic reticulum [GO:0070863]; protein localization to endosome [GO:0036010]apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; transport vesicle membrane [GO:0030658]FUNCTION: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations. {ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21289302}.O96011PX11B Peroxisomal membrane protein 11BSUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}; Single-pass membrane protein {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}.peroxisome fission [GO:0016559]; peroxisome organization [GO:0007031]; protein homooligomerization [GO:0051260]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165]extracellular exosome [GO:0070062]; integral component of peroxisomal membrane [GO:0005779]; membrane [GO:0016020]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein complex [GO:0043234]rFUNCTION: Involved in peroxisomal proliferation (PubMed:9792670). May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane (PubMed:12618434). Promotes membrane protrusion and elongation on the peroxisomal surface (PubMed:20826455). {ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670}.Q9Y6C9MTCH2Mitochondrial carrier homolog 2hepatocyte apoptotic process [GO:0097284]; protein localization to mitochondrion [GO:0070585]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634][FUNCTION: The substrate transported is not yet known. Induces mitochondrial depolarization.Q5T3F8CSCL2CSC1-like protein 2SFUNCTION: Acts as an osmosensitive calcium-permeable cation channel. {ECO:0000250}.Q9UM47NOTC3(Neurogenic locus notch homolog protein 3SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Notch 3 intracellular domain: Nucleus. Note=Following proteolytical processing NICD is translocated to the nucleus.forebrain development [GO:0030900]; gene expression [GO:0010467]; glomerular capillary formation [GO:0072104]; negative regulation of neuron differentiation [GO:0045665]; neuron fate commitment [GO:0048663]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of transcription, DNA-templated [GO:0006355]; transcription initiation from RNA polymerase II promoter [GO:0006367]>actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). {ECO:0000250}.Q9Y639NPTN NeuroplastinSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Enriched at postsynaptic density. {ECO:0000250}.7homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; long-term synaptic potentiation [GO:0060291]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein phosphorylation [GO:0001934]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]cell adhesion molecule binding [GO:0050839]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; type 1 fibroblast growth factor receptor binding [GO:0005105]cell surface [GO:0009986]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; presynaptic membrane [GO:0042734]@FUNCTION: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). {ECO:0000250}.Q99943PLCA41-acyl-sn-glycerol-3-phosphate acyltransferase alphaSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21873652}; Multi-pass membrane protein {ECO:0000269|PubMed< :21873652}.LCDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; energy reserve metabolic process [GO:0006112]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; positive regulation of cellular metabolic process [GO:0031325]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of cytokine production [GO:0001819]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:21873652}.P61019RAB2ARas-related protein Rab-2ASUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:17081065}; Lipid-anchor {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Endoplasmic reticulum membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; mitotic cell cycle [GO:0000278]; Rab protein signal transduction [GO:0032482]endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; nucleus [GO:0005634]]FUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex.P20908CO5A1Collagen alpha-1(V) chainCollagenqSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.axon guidance [GO:0007411]; blood vessel development [GO:0001568]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; collagen biosynthetic process [GO:0032964]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular fibril organization [GO:0043206]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; eye morphogenesis [GO:0048592]; heart morphogenesis [GO:0003007]; integrin biosynthetic process [GO:0045112]; negative regulation of endodermal cell differentiation [GO:1903225]; regulation of cellular component organization [GO:0051128]; skin development [GO:0043588]; tendon development [GO:0035989]; wound healing, spreading of epidermal cells [GO:0035313]extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; proteoglycan binding [GO:0043394]basement membrane [GO:0005604]; collagen type V trimer [GO:0005588]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]FUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.Q9P2C4TM181Transmembrane protein 181pathogenesis [GO:0009405]$toxic substance binding [GO:0015643]FUNCTION: Mediates action of cytolethal distending toxins (CDT), which are secreted by many pathogenic bacteria. Expression level of TMEM181 is rate-limiting for intoxication. {ECO:0000269|PubMed:19965467}.P09543CN37,2',3'-cyclic-nucleotide 3'-phosphodiesteraseSUBCELLULAR LOCATION: Membrane; Lipid-anchor. Melanosome. Note=Firmly bound to membrane structures of brain white matter. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.adult locomotory behavior [GO:0008344]; aging [GO:0007568]; axonogenesis [GO:0007409]; cyclic nucleotide catabolic process [GO:0009214]; forebrain development [GO:0030900]; microtubule cytoskeleton organization [GO:0000226]; oligodendrocyte differentiation [GO:0048709]; regulation of mitochondrial membrane permeability [GO:0046902]; response to lipopolysaccharide [GO:0032496]; response to toxic substance [GO:0009636]; substantia nigra development [GO:0021762]; synaptic transmission [GO:0007268]2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; cyclic nucleotide binding [GO:0030551]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; melanosome [GO:0042470]; membrane [GO:0016020]; microtubule [GO:0005874]; microvillus [GO:0005902]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; myelin sheath abaxonal region [GO:0035748]; myelin sheath adaxonal region [GO:0035749]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]FUNCTION: May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. {ECO:0000250}.P13987CD59CD59 glycoproteinxSUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Note=Soluble form found in a number of tissues.gblood coagulation [GO:0007596]; cell surface receptor signaling pathway [GO:0007166]; innate immune response [GO:0045087]; negative regulation of activation of membrane attack complex [GO:0001971]; negative regulation of apoptotic process [GO:0043066]; positive regulation of T cell proliferation [GO:0042102]; regulation of complement activation [GO:0030449]complement binding [GO:0001848]Banchored component of external side of plasma membrane [GO:0031362]; cell surface [GO:0009986]; compact myelin [GO:0043218]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; vesicle [GO:0031982]DFUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.; FUNCTION: The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.Q14BN4SLMAP'Sarcolemmal membrane-associated proteinSUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Membrane-associated. Distributed in the transverse tubules and near the junctional sarcoplasmic reticulum. Detected along the Z- and M-lines in cardiomyocytes. Centrosome. Localizes to the centrosomes in a microtubule- dependent manner (By similarity). {ECO:0000250}.muscle contraction [GO:0006936]integral component of plasma membrane [GO:0005887]; microtubule organizing center [GO:0005815]; sarcolemma [GO:0042383]; smooth endoplasmic reticulum [GO:0005790]@FUNCTION: May play a role during myoblast fusion. {ECO:0000250}.P51572BAP31%B-cell receptor-associated protein 31SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Note=May shuttle between the ER and the intermediate compartment/cis-Golgi complex.Pantigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular component disassembly involved in execution phase of apopt< osis [GO:0006921]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; positive regulation of retrograde protein transport, ER to cytosol [GO:1904154]; programmed cell death [GO:0012501]; protein localization to endoplasmic reticulum exit site [GO:0070973]; spermatogenesis [GO:0007283]clathrin-coated vesicle [GO:0030136]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; integral component of plasma membrane [GO:0005887]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. May be involved in CASP8-mediated apoptosis. {ECO:0000269|PubMed:10958671, ECO:0000269|PubMed:18287538, ECO:0000269|PubMed:9396746}.Q14789GOGB1Golgin subfamily B member 1TSUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I membrane protein.Golgi organization [GO:0007030]cis-Golgi network [GO:0005801]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of membrane [GO:0016021]; membrane [GO:0016020]WFUNCTION: May participate in forming intercisternal cross-bridges of the Golgi complex.Q96BY9SARAF9Store-operated calcium entry-associated regulatory factorSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22464749}; Single-pass type I membrane protein {ECO:0000269|PubMed:22464749}. Note=Translocates to the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner following cytosolic Ca(2+) elevation.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane; Single-pass type I membrane protein.[calcium ion transport [GO:0006816]; regulation of store-operated calcium entry [GO:2001256]Aintegral component of endoplasmic reticulum membrane [GO:0030176]2FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions. {ECO:0000269|PubMed:22464749}.Q9ULX6AKP8LA-kinase anchor protein 8-likeSUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm. Note=Colocalizes with PRPF40A in the nuclear matrix (By similarity). Nuclear at steady state but shuttles between the nucleus and cytoplasm. Associated with the nuclear matrix. {ECO:0000250}.DEAD/H-box RNA helicase binding [GO:0017151]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]ccytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]KFUNCTION: Could play a role in constitutive transport element (CTE)-mediated gene expression. Does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May regulate the initiation phase of DNA replication when associated with TMPO-beta.Q9UBS4DJB11"DnaJ homolog subfamily B member 11SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998, ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}. Note=Associated with the ER membrane in a C-terminally epitope-tagged construct.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; protein folding [GO:0006457]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; membrane [GO:0016020]FUNCTION: Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676}.Q5JTZ9SYAM#Alanine--tRNA ligase, mitochondrialcSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:21549344}.gene expression [GO:0010467]; mitochondrial alanyl-tRNA aminoacylation [GO:0070143]; mitochondrial respiratory chain complex assembly [GO:0033108]; tRNA aminoacylation for protein translation [GO:0006418]}alanine-tRNA ligase activity [GO:0004813]; ATP binding [GO:0005524]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_03133}.Q9H3K2GHITM.Growth hormone-inducible transmembrane proteinSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18417609}; Multi-pass membrane protein {ECO:0000269|PubMed:18417609}.zextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]FUNCTION: Required for the mitochondrial tubular network and cristae organization. Involved in apoptotic release of cytochrome c. {ECO:0000269|PubMed:18417609}.O96005CLPT1,Cleft lip and palate transmembrane protein 1cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; regulation of T cell differentiation in thymus [GO:0033081]xexternal side of plasma membrane [GO:0009897]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]?FUNCTION: May play a role in T-cell development. {ECO:0000250}.P04844RPN2HDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2aging [GO:0007568]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; gene expression [GO:0010467]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]^ribosome binding [GO:0043022]; transferase activity, transferring glycosyl groups [GO:0016757](autophagosome membrane [GO:0000421]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791]O75063XYLKGlycosaminoglycan xylosylkinaseSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19473117}; Single-pass type II membrane protein {ECO:0000269|PubMed:19473117}.Fpositive regulation of< protein targeting to mitochondrion [GO:1903955]ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. {ECO:0000269|PubMed:19473117, ECO:0000269|PubMed:24425863}.P61619S61A17Protein transport protein Sec61 subunit alpha isoform 1antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cell growth [GO:0016049]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; posttranslational protein targeting to membrane [GO:0006620]; protein targeting to ER [GO:0045047]; response to interferon-gamma [GO:0034341]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]ribosome binding [GO:0043022]cytosol [GO:0005829]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. Required for assembly of membrane and secretory proteins. Tightly associated with membrane-bound ribosomes, either directly or through adapter proteins.Q15067ACOX1%Peroxisomal acyl-coenzyme A oxidase 1alpha-linolenic acid metabolic process [GO:0036109]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; fatty acid oxidation [GO:0019395]; generation of precursor metabolites and energy [GO:0006091]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; peroxisome fission [GO:0016559]; positive regulation of cholesterol homeostasis [GO:2000189]; prostaglandin metabolic process [GO:0006693]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid metabolic process [GO:0000038]acyl-CoA dehydrogenase activity [GO:0003995]; acyl-CoA oxidase activity [GO:0003997]; electron carrier activity [GO:0009055]; FAD binding [GO:0071949]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]; palmitoyl-CoA oxidase activity [GO:0016401]; PDZ domain binding [GO:0030165]; protein N-terminus binding [GO:0047485]; receptor binding [GO:0005102]+intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA. {ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:17603022}.Q9NX47MARH5"E3 ubiquitin-protein ligase MARCH5_SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane. Note=Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301). {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:16874301}.!negative regulation of cell aging [GO:0090344]; positive regulation of mitochondrial fission [GO:0090141]; protein autoubiquitination [GO:0051865]; protein localization to mitochondrion [GO:0070585]; protein polyubiquitination [GO:0000209]; regulation of mitochondrial fission [GO:0090140]GTPase binding [GO:0051020]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:20103533}.P13674P4HA1$Prolyl 4-hydroxylase subunit alpha-12SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.mcollagen fibril organization [GO:0030199]; peptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; procollagen-proline 4-dioxygenase activity [GO:0004656]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; procollagen-proline 4-dioxygenase complex [GO:0016222]FUNCTION: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.P35625TIMP3Metalloproteinase inhibitor 3:aging [GO:0007568]; cellular response to organic substance [GO:0071310]; central nervous system development [GO:0007417]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of metalloenzyme activity [GO:0048553]; response to cytokine [GO:0034097]; response to estrogen [GO:0043627]; response to folic acid [GO:0051593]; response to hormone [GO:0009725]; response to mechanical stimulus [GO:0009612]; tissue regeneration [GO:0042246]; visual perception [GO:0007601]smetal ion binding [GO:0046872]; metalloendopeptidase inhibitor activity [GO:0008191]; protease binding [GO:0002020]basement membrane [GO:0005604]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634]; proteinaceous extracellular matrix [GO:0005578](FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.Q8NBI5S43A3!Solute carrier family 43 member 3$transmembrane transport [GO:0055085].FUNCTION: Putative transporter. {ECO:0000250< }.Q8NFQ8TOIP2Torsin-1A-interacting protein 2eSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane.endoplasmic reticulum organization [GO:0007029]; positive regulation of ATPase activity [GO:0032781]; protein localization to nuclear envelope [GO:0090435]CATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]*FUNCTION: Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity. {ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.O95302FKBP9)Peptidyl-prolyl cis-trans isomerase FKBP9SSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.chaperone-mediated protein folding [GO:0061077]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]wcalcium ion binding [GO:0005509]; FK506 binding [GO:0005528]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]gcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]NFUNCTION: PPIases accelerate the folding of proteins during protein synthesis.Q5T160SYRM-Probable arginine--tRNA ligase, mitochondrialarginyl-tRNA aminoacylation [GO:0006420]; gene expression [GO:0010467]; mitochondrial translation [GO:0032543]; tRNA aminoacylation for protein translation [GO:0006418]farginine-tRNA ligase activity [GO:0004814]; ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]Ucytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]O94874UFL1E3 UFM1-protein ligase 1SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063}. Cytoplasm, cytosol {ECO:0000269|PubMed:20228063}.negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein ubiquitination [GO:0031397]; osteoblast differentiation [GO:0001649]; positive regulation of cell proliferation [GO:0008284]; positive regulation of glial cell proliferation [GO:0060252]; protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of protein localization [GO:0032880]; response to endoplasmic reticulum stress [GO:0034976]; response to L-glutamate [GO:1902065]Dligase activity [GO:0016874]; UFM1 transferase activity [GO:0071568]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498). May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription (PubMed:25219498). {ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:25219498}.P16070CD44 CD44 antigenSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Colocalizes with actin in membrane protrusions at wounding edges. {ECO:0000250}.blood coagulation [GO:0007596]; branching involved in prostate gland morphogenesis [GO:0060442]; branching involved in ureteric bud morphogenesis [GO:0001658]; carbohydrate metabolic process [GO:0005975]; cartilage development [GO:0051216]; cell-matrix adhesion [GO:0007160]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cytokine-mediated signaling pathway [GO:0019221]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; interferon-gamma-mediated signaling pathway [GO:0060333]; leukocyte migration [GO:0050900]; monocyte aggregation [GO:0070487]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of monocyte aggregation [GO:1900625]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; single organismal cell-cell adhesion [GO:0016337]; small molecule metabolic process [GO:0044281]; Wnt signaling pathway [GO:0016055]; wound healing involved in inflammatory response [GO:0002246]tcollagen binding [GO:0005518]; hyaluronic acid binding [GO:0005540]; hyalurononglucosaminidase activity [GO:0004415]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; macrophage migration inhibitory factor receptor complex [GO:0035692]; plasma membrane [GO:0005886]FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. {ECO:0000269|PubMed:16541107}.O60353FZD6 Frizzled-6SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q61089}. Apical cell membrane; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q61089}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FZD3 at the apical face of cells (By similarity). {ECO:0000250|UniProtKB:Q61089}.ecanonical Wnt signaling pathway [GO:0060070]; cell proliferation in midbrain [GO:0033278]; embryonic nail plate morphogenesis [GO:0035880]; establishment of planar polarity [GO:0001736]; hair follicle development [GO:0001942]; inner ear morphogenesis [GO:0042472]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; neural tube closure [GO:0001843]; non-canonical Wnt signaling pathway [GO:0035567]; platelet activation [GO:0030168]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]G-protein coupled receptor activity [< GO:0004930]; ubiquitin protein ligase binding [GO:0031625]; Wnt-activated receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]qFUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear (By similarity). {ECO:0000250|UniProtKB:Q61089}.Q92922SMRC1SWI/SNF complex subunit SMARCC1SWI_SNF ATP-dependent chromatin remodeling [GO:0043044]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; insulin receptor signaling pathway [GO:0008286]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; nervous system development [GO:0007399]; nucleosome disassembly [GO:0006337]; organ morphogenesis [GO:0009887]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; protein N-terminus binding [GO:0047485]; transcription coactivator activity [GO:0003713]nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]; XY body [GO:0001741]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.P00533EGFR Epidermal growth factor receptorBSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome. Endosome membrane. Nucleus. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF).; SUBCELLULAR LOCATION: Isoform 2: Secreted. activation of MAPKK activity [GO:0000186]; activation of phospholipase A2 activity by calcium-mediated signaling [GO:0043006]; activation of phospholipase C activity [GO:0007202]; axon guidance [GO:0007411]; cell proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; cellular response to amino acid stimulus [GO:0071230]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to estradiol stimulus [GO:0071392]; cerebral cortex cell migration [GO:0021795]; digestive tract morphogenesis [GO:0048546]; embryonic placenta development [GO:0001892]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; hair follicle development [GO:0001942]; innate immune response [GO:0045087]; learning or memory [GO:0007611]; MAPK cascade [GO:0000165]; morphogenesis of an epithelial fold [GO:0060571]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of protein catabolic process [GO:0042177]; neurotrophin TRK receptor signaling pathway [GO:0048011]; ossification [GO:0001503]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of catenin import into nucleus [GO:0035413]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein autophosphorylation [GO:0046777]; protein insertion into membrane [GO:0051205]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to stress [GO:0006950]; response to UV-A [GO:0070141]; salivary gland morphogenesis [GO:0007435]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]actin filament binding [GO:0051015]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; epidermal growth factor-activated receptor activity [GO:0005006]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; receptor signaling protein tyrosine kinase activity [GO:0004716]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane signaling receptor activity [GO:0004888]; ubiquitin protein ligase binding [GO:0031625]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellu< lar space [GO:0005615]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; membrane raft [GO:0045121]; multivesicular body, internal vesicle lumen [GO:0097489]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; Shc-EGFR complex [GO:0070435]4FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.Q13162PRDX4Peroxiredoxin-4dSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9388242}. Secreted {ECO:0000269|PubMed:9388242}.4-hydroxyproline metabolic process [GO:0019471]; cell redox homeostasis [GO:0045454]; extracellular matrix organization [GO:0030198]; I-kappaB phosphorylation [GO:0007252]; male gonad development [GO:0008584]; negative regulation of male germ cell proliferation [GO:2000255]; protein maturation by protein folding [GO:0022417]; reactive oxygen species metabolic process [GO:0072593]; spermatogenesis [GO:0007283],thioredoxin peroxidase activity [GO:0008379]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. {ECO:0000269|PubMed:9388242}.Q92643GPI8GPI-anchor transamidaseattachment of GPI anchor to protein [GO:0016255]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]cysteine-type peptidase activity [GO:0008234]; GPI-anchor transamidase activity [GO:0003923]; protein disulfide isomerase activity [GO:0003756]endoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.O43709WBS222Probable 18S rRNA (guanine-N(7))-methyltransferaseSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Cytoplasm. Note=Localized diffusely throughout the nucleus and the cytoplasm. Localization is not affected by glucocorticoid treatment.chromatin modification [GO:0016568]; regulation of transcription, DNA-templated [GO:0006355]; rRNA processing [GO:0006364]; transcription, DNA-templated [GO:0006351]Imethyltransferase activity [GO:0008168]; poly(A) RNA binding [GO:0044822])FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA (By similarity). Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492}.Q9Y6A9SPCS1"Signal peptidase complex subunit 1Gcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; protein targeting to ER [GO:0045047]; proteolysis [GO:0006508]; regulation of insulin secretion [GO:0050796]; signal peptide processing [GO:0006465]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; signal peptidase complex [GO:0005787]P22307NLTP#Non-specific lipid-transfer proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17157249}. Mitochondrion {ECO:0000269|PubMed:17157249}. Note=Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues.; SUBCELLULAR LOCATION: Isoform SCPx: Peroxisome. Note=Interaction with PEX5 is essential for peroxisomal import.; SUBCELLULAR LOCATION: Isoform SCP2: Mitochondrion {ECO:0000305}.Falpha-linolenic acid metabolic process [GO:0036109]; bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; inositol trisphosphate biosynthetic process [GO:0032959]; lipid hydroperoxide transport [GO:1901373]; lipid transport [GO:0006869]; peroxisome organization [GO:0007031]; phospholipid transport [GO:0015914]; positive regulation of intracellular cholesterol transport [GO:0032385]; positive regulation of steroid metabolic process [GO:0045940]; progesterone biosynthetic process [GO:0006701]; protein localization to plasma membrane [GO:0072659]; small molecule metabolic process [GO:0044281]; steroid biosynthetic process [GO:0006694]; unsaturated fatty acid metabolic process [GO:0033559]$cholesterol binding [GO:0015485]; fatty-acyl-CoA binding [GO:0000062]; long-chain fatty acyl-CoA binding [GO:0036042]; oleic acid binding [GO:0070538]; phosphatidylinositol transporter activity [GO:0008526]; propanoyl-CoA C-acyltransferase activity [GO:0033814]; receptor binding [GO:0005102]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; protein complex [GO:0043234]FUNCTION: Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. {ECO:0000269|PubMed:17157249, ECO:0000269|PubMed:8300590}.P01112RASH GTPase HRasSUBCELLULAR LOCATION: Cell membrane. Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with GNB2L1 to the perinuclear region. activation of MAPKK activity [GO:0000186]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; cellular senescence [GO:0090398]; chemotaxis [GO:0006935]; endocytosis [GO:0006897]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor sign< aling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway [GO:0097193]; leukocyte migration [GO:0050900]; MAPK cascade [GO:0000165]; mitotic cell cycle checkpoint [GO:0007093]; negative regulation of cell proliferation [GO:0008285]; negative regulation of gene expression [GO:0010629]; negative regulation of GTPase activity [GO:0034260]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ morphogenesis [GO:0009887]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA replication [GO:0045740]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of ruffle assembly [GO:1900029]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of wound healing [GO:0090303]; protein heterooligomerization [GO:0051291]; Ras protein signal transduction [GO:0007265]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; social behavior [GO:0035176]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; synaptic transmission [GO:0007268]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]_GTPase activity [GO:0003924]; GTP binding [GO:0005525]; protein C-terminus binding [GO:0008022]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:9020151}.Q8TBA6GOGA5Golgin subfamily A member 5SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:9915833}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9915833}. Note=Found throughout the Golgi, both on cisternae and, at higher abundance, on the tubulo-vesicular structures of the cis-Golgi network.Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; retrograde transport, vesicle recycling within Golgi [GO:0000301]Oprotein homodimerization activity [GO:0042803]; Rab GTPase binding [GO:0017137]Mcis-Golgi network [GO:0005801]; COPI-coated vesicle membrane [GO:0030663]; Golgi apparatus [GO:0005794]; Golgi cis cisterna [GO:0000137]; Golgi cisterna [GO:0031985]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport. {ECO:0000269|PubMed:12538640, ECO:0000269|PubMed:15718469}.Q969V3NCLNNicalinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15257293, ECO:0000269|PubMed:20538592}; Single-pass membrane protein {ECO:0000269|PubMed:15257293, ECO:0000269|PubMed:20538592}.protein destabilization [GO:0031648]; regulation of protein complex assembly [GO:0043254]; regulation of signal transduction [GO:0009966]FUNCTION: May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning. {ECO:0000250}.Q7L3T8SYPM,Probable proline--tRNA ligase, mitochondrial9SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.gene expression [GO:0010467]; prolyl-tRNA aminoacylation [GO:0006433]; tRNA aminoacylation for protein translation [GO:0006418]CATP binding [GO:0005524]; proline-tRNA ligase activity [GO:0004827]Q96CP6GRM1A!GRAM domain-containing protein 1AP35613BASIBasiginiSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15946952}; Single-pass type I membrane protein {ECO:0000303|PubMed:15946952}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Colocalizes with SLC16A1 and SLC16A8. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P18572, ECO:0000269|PubMed:17081065}.oblood coagulation [GO:0007596]; cell surface receptor signaling pathway [GO:0007166]; cellular metabolic process [GO:0044237]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; leukocyte migration [GO:0050900]; odontogenesis of dentin-containing tooth [GO:0042475]; protein targeting to plasma membrane [GO:0072661]; pyruvate metabolic process [GO:0006090]; response to cAMP [GO:0051591]; response to mercury ion [GO:0046689]; response to peptide hormone [GO:0043434]; small molecule metabolic process [GO:0044281]mannose binding [GO:0005537]Pacrosomal membrane [GO:0002080]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]FUNCTION: Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. {ECO:0000269|PubMed:17127621}.Q15424SAFB1Scaffold attachment factor B1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19674106}.chromatin organization [GO:0006325]; growth [GO:0040007]; hormone metabolic process [GO:0042445]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). Can inhibit cell proliferation. {ECO:0000250}.O00192ARVC?Armadillo repeat protein deleted in velo-cardio-facial syndromecalcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; multicellular organismal development [GO:0007275]; single organismal cell-cell adhesion [GO:0016337]cell junction [GO:0030054]; cytoplasm [GO:0005737]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]IFUNCTION: Involved in protein-protein interactions at adherens junctions.Q9Y673ALG5+Dolichyl-phosphate beta-glucosyltransferasewSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250< }.;cellular protein metabolic process [GO:0044267]; determination of left/right symmetry [GO:0007368]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279]sdolichyl-phosphate beta-glucosyltransferase activity [GO:0004581]; oligosaccharyl transferase activity [GO:0004576]O15484CAN5 Calpain-5granulosa cell differentiation [GO:0060014]; luteinization [GO:0001553]; ovarian follicle development [GO:0001541]; proteolysis [GO:0006508]; signal transduction [GO:0007165]Ccalcium-dependent cysteine-type endopeptidase activity [GO:0004198]rcell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]P00505AATM)Aspartate aminotransferase, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9537447}. Cell membrane {ECO:0000269|PubMed:9537447}. Note=Exposure to alcohol promotes translocation to the cell membrane.2-oxoglutarate metabolic process [GO:0006103]; 4-hydroxyproline catabolic process [GO:0019470]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; carbohydrate metabolic process [GO:0005975]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; fatty acid transport [GO:0015908]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glutamate catabolic process to 2-oxoglutarate [GO:0019551]; glutamate catabolic process to aspartate [GO:0019550]; glutamate metabolic process [GO:0006536]; oxaloacetate metabolic process [GO:0006107]; response to ethanol [GO:0045471]; small molecule metabolic process [GO:0044281]Tamino acid binding [GO:0016597]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-phenylalanine:2-oxoglutarate aminotransferase activity [GO:0080130]; phospholipid binding [GO:0005543]; poly(A) RNA binding [GO:0044822]; pyridoxal phosphate binding [GO:0030170]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein complex [GO:0043234]EFUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. {ECO:0000269|PubMed:9537447}.Q9Y394DHRS7+Dehydrogenase/reductase SDR family member 7Q02818NUCB1Nucleobindin-1SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=A small fraction of the protein may be cytoplasmic. {ECO:0000250}.Pregulation of protein targeting [GO:1903533]; response to cisplatin [GO:0072718]0cis-Golgi network [GO:0005801]; early endosome [GO:0005769]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of Golgi membrane [GO:0090498]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; Golgi cisterna membrane [GO:0032580]; lumenal side of Golgi membrane [GO:0098547]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; rough endoplasmic reticulum [GO:0005791]; trans-Golgi network [GO:0005802]|FUNCTION: Major calcium-binding protein of the Golgi. May have a role in calcium homeostasis (By similarity). {ECO:0000250}.Q9H4E5RHOJ$Rho-related GTP-binding protein RhoJAactin cytoskeleton organization [GO:0030036]; regulation of cell shape [GO:0008360]; regulation of small GTPase mediated signal transduction [GO:0051056]; retina vasculature morphogenesis in camera-type eye [GO:0061299]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]Vcytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: GTP-binding protein with GTPase activity. Elicits the formation of F-actin-rich structures in fibroblasts and is involved in the regulation of cell morphology (By similarity). {ECO:0000250}.P11182ODB2jLipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial*Valine, leucine and isoleucine degradationbranched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; small molecule metabolic process [GO:0044281]dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity [GO:0043754]; ubiquitin protein ligase binding [GO:0031625]mitochondrial alpha-ketoglutarate dehydrogenase complex [GO:0005947]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.Q7Z7H5TMED4/Transmembrane emp24 domain-containing protein 4vSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein transport [GO:0015031]; signal transduction [GO:0007165]FUNCTION: Involved in vesicular protein trafficking, mainly in the early secretory pathway. targeting. Involved in the maintenance of the Golgi apparatus. Appears to play a role in the biosynthesis of secreted cargo including processing. Involved in endoplasmic reticulum stress response. May play a role in the regulation of heat-shock response and apoptosis (By similarity). {ECO:0000250}.P31431SDC4 Syndecan-4Organizers(11)SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein. Secreted. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted.carbohydrate metabolic process [GO:0005975]; cell migration [GO:0016477]; chondroitin sulfate metabolic process [GO:0030204]; extracellular matrix organization [GO:0030198]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; inner ear receptor stereocilium organization [GO:0060122]; neural tube closure [GO:0001843]; phototransduction, visible light [GO:0007603]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of stress fiber assembly [GO:0051496]; regulation of fibroblast migration [GO:0010762]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]; ureteric bud development [GO:0001657]; wound healing [GO:0042060]-thrombospondin receptor activity [GO:0070053]cell surface [GO:0009986]; costamere [GO:0043034]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; lysosomal lumen [GO:0043202]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]?FUNCTION: Cell surface proteoglycan that bears heparan sulfate.Q92521PIGBGPI mannosyltransferase 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:886195< 4}; Multi-pass membrane protein {ECO:0000269|PubMed:8861954}.cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; GPI anchor biosynthetic process [GO:0006506]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; preassembly of GPI anchor in ER membrane [GO:0016254]FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly. {ECO:0000269|PubMed:8861954}.Q92508PIEZ13Piezo-type mechanosensitive ion channel component 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20016066}; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane. Cell membrane {ECO:0000250|UniProtKB:E2JF22}; Multi-pass membrane protein. Note=In erythrocytes, located in the plasma membrane. In response to shear stress there is an accumulation at the leading apical lamellipodia. {ECO:0000269|PubMed:25119035}.cation transport [GO:0006812]; detection of mechanical stimulus [GO:0050982]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of integrin activation [GO:0033625]; regulation of membrane potential [GO:0042391]Zcation channel activity [GO:0005261]; mechanically-gated ion channel activity [GO:0008381]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]$FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship and are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensors that promote endothelial cell organization and alignment in the direction of blood flow. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology. {ECO:0000250|UniProtKB:E2JF22, ECO:0000269|PubMed:20016066}.Q9Y3C1NOP16Nucleolar protein 16/ribosomal large subunit biogenesis [GO:0042273]cintracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleus [GO:0005634]Q9BQE4SELSSelenoprotein SlSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm {ECO:0000250}.cell redox homeostasis [GO:0045454]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oxidative stress [GO:0034599]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; ER overload response [GO:0006983]; establishment of protein localization [GO:0045184]; negative regulation of acute inflammatory response to antigenic stimulus [GO:0002865]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of glucose import [GO:0046325]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of macrophage apoptotic process [GO:2000110]; negative regulation of nitric-oxide synthase biosynthetic process [GO:0051771]; negative regulation of tumor necrosis factor production [GO:0032720]; regulation of gluconeogenesis [GO:0006111]; regulation of nitric oxide metabolic process [GO:0080164]; response to glucose [GO:0009749]; response to redox state [GO:0051775]; retrograde protein transport, ER to cytosol [GO:0030970]antioxidant activity [GO:0016209]; ATPase binding [GO:0051117]; enzyme binding [GO:0019899]; receptor activity [GO:0004872]; selenium binding [GO:0008430]; ubiquitin-specific protease binding [GO:1990381]0cytoplasmic microtubule [GO:0005881]; Derlin-1-VIMP complex [GO:0036502]; endoplasmic reticulum [GO:0005783]; integral component of endoplasmic reticulum membrane [GO:0030176]; low-density lipoprotein particle [GO:0034362]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination. {ECO:0000269|PubMed:15215856}.O60313OPA1+Dynamin-like 120 kDa protein, mitochondrialtSUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion intermembrane space.apoptotic process [GO:0006915]; axon transport of mitochondrion [GO:0019896]; cellular senescence [GO:0090398]; inner mitochondrial membrane organization [GO:0007007]; mitochondrial fission [GO:0000266]; mitochondrial fusion [GO:0008053]; mitochondrial genome maintenance [GO:0000002]; mitochondrion organization [GO:0007005]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neural tube closure [GO:0001843]; positive regulation of dendrite development [GO:1900006]; positive regulation of mitochondrial fusion [GO:0010636]; positive regulation of neuron maturation [GO:0014042]; visual perception [GO:0007601]ZGTPase activity [GO:0003924]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]cytoplasm [GO:0005737]; dendrite [GO:0030425]; extrinsic component of mitochondrial inner membrane [GO:0031314]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]$FUNCTION: Dynamin-related GTPase required for mitochondrial fusion and regulation of apoptosis. May form a diffusion barrier for proteins stored in mitochondrial cristae. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. May also play a role in mitochondrial genome maintenance. {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:18158317}.; FUNCTION: Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. {ECO:0000269|PubMed:20038677}.Q96RQ3MCCA<Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16023992}.Obiotin metabolic process [GO:0006768]; branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; leucine catabolic process [GO:0006552]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin carboxylase activity [GO:0004075]; metal ion binding [GO:0046872]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]~cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA car< boxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000269|PubMed:17360195}.Q7Z6M4MTEF41Transcription termination factor 4, mitochondrial|SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335, ECO:0000269|PubMed:22949673, ECO:0000269|PubMed:23022348}.(camera-type eye development [GO:0043010]; heart development [GO:0007507]; protein targeting to mitochondrion [GO:0006626]; regulation of transcription, DNA-templated [GO:0006355]; ribosome assembly [GO:0042255]; rRNA processing [GO:0006364]; transcription from mitochondrial promoter [GO:0006390]Cdouble-stranded DNA binding [GO:0003690]; rRNA binding [GO:0019843]fcytoplasm [GO:0005737]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrion [GO:0005739]FUNCTION: Regulator of mitochondrial ribosome biogenesis and translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S and targets NSUN4 RNA methyltransferase to the mitochondrial large ribosomal subunit (39S). {ECO:0000269|PubMed:21531335}.Q92784DPF3Zinc finger protein DPF3Iactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; chromatin modification [GO:0016568]; nervous system development [GO:0007399]; positive regulation of defense response to virus by host [GO:0002230]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]nBAF complex [GO:0071565]FUNCTION: Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development. {ECO:0000250, ECO:0000269|PubMed:18765789}.O14734ACOT8Acyl-coenzyme A thioesterase 8acyl-CoA metabolic process [GO:0006637]; alpha-linolenic acid metabolic process [GO:0036109]; bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; cellular lipid metabolic process [GO:0044255]; dicarboxylic acid catabolic process [GO:0043649]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; peroxisome fission [GO:0016559]; small molecule metabolic process [GO:0044281]; unsaturated fatty acid metabolic process [GO:0033559]; viral process [GO:0016032] acyl-CoA hydrolase activity [GO:0047617]; carboxylic ester hydrolase activity [GO:0052689]; choloyl-CoA hydrolase activity [GO:0033882]; medium-chain acyl-CoA hydrolase activity [GO:0052815]; palmitoyl-CoA hydrolase activity [GO:0016290]; receptor binding [GO:0005102];mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs (By similarity). May be involved in the metabolic regulation of peroxisome proliferation. {ECO:0000250, ECO:0000269|PubMed:15194431}.P19338NUCL NucleolinSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.Tangiogenesis [GO:0001525]; cellular response to lipopolysaccharide [GO:0071222]; endocytosis [GO:0006897]; liver regeneration [GO:0097421]; negative regulation of apoptotic process [GO:0043066]; positive regulation of interleukin-6 secretion [GO:2000778]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter [GO:1901838]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of rRNA processing [GO:2000232]; spermatogenesis [GO:0007283]calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; RNA binding [GO:0003723]; rRNA primary transcript binding [GO:0042134]; selenocysteine insertion sequence binding [GO:0035368]; single-stranded DNA binding [GO:0003697]; telomeric DNA binding [GO:0042162]Ycell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasmic ribonucleoprotein granule [GO:0036464]; dense fibrillar component [GO:0001651]; extracellular exosome [GO:0070062]; fibrillar center [GO:0001650]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529] FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. {ECO:0000269|PubMed:10393184}.Q9Y4P3TBL2Transducin beta-like protein 2cellular response to glucose starvation [GO:0042149]; cellular response to hypoxia [GO:0071456]; endoplasmic reticulum unfolded protein response [GO:0030968]phosphoprotein binding [GO:0051219]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; translation initiation factor binding [GO:0031369]eendoplasmic reticulum [GO:0005783]; integral component of endoplasmic reticulum membrane [GO:0030176]Q8ND76CCNYCyclin-YcyclinSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}; Lipid-anchor {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}; Cytoplasmic side {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus. cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; regulation of canonical Wnt signaling pathway [GO:0060828]; Wnt signaling pathway [GO:0016055]Pcyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]cytoplasmic cyclin-dependent protein kinase holoenzyme complex [GO:0000308]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Positive regulatory subunit of the cyclin-dependent kinases CDK14/PFTK1 and CDK16. Acts as a cell-cycle regulator of Wnt signaling pathway duri< ng G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway. Recruits CDK16 to the plasma membrane. Isoform 3 might play a role in the activation of MYC-mediated transcription. {ECO:0000269|PubMed:18060517, ECO:0000269|PubMed:19524571, ECO:0000269|PubMed:20059949, ECO:0000269|PubMed:22184064}.P05412JUNTranscription factor AP-1+ aging [GO:0007568]; angiogenesis [GO:0001525]; axon regeneration [GO:0031103]; cellular response to calcium ion [GO:0071277]; cellular response to hormone stimulus [GO:0032870]; cellular response to potassium ion starvation [GO:0051365]; circadian rhythm [GO:0007623]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; leading edge cell differentiation [GO:0035026]; learning [GO:0007612]; liver development [GO:0001889]; membrane depolarization [GO:0051899]; microglial cell activation [GO:0001774]; monocyte differentiation [GO:0030224]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of cell proliferation [GO:0008285]; negative regulation of DNA binding [GO:0043392]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress [GO:1990441]; outflow tract morphogenesis [GO:0003151]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of cell differentiation [GO:0045597]; positive regulation of DNA replication [GO:0045740]; positive regulation of DNA-templated transcription, initiation [GO:2000144]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of GTPase activity [GO:0043547]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cell death [GO:0010941]; regulation of cell proliferation [GO:0042127]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; release of cytochrome c from mitochondria [GO:0001836]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to hydrogen peroxide [GO:0042542]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; response to muscle stretch [GO:0035994]; response to radiation [GO:0009314]; SMAD protein import into nucleus [GO:0007184]; SMAD protein signal transduction [GO:0060395]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]cAMP response element binding [GO:0035497]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; poly(A) RNA binding [GO:0044822]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; RNA polymerase II transcription factor binding transcription activator activity [GO:0001190]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]cytosol [GO:0005829]; nuclear chromosome [GO:0000228]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]; transcription factor complex [GO:0005667]9FUNCTION: Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:17210646}.Q14257RCN2Reticulocalbin-2dendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; nucleolus [GO:0005730]#FUNCTION: Not known. Binds calcium.Q8TAQ2SMRC2SWI/SNF complex subunit SMARCC2_ATP-dependent chromatin remodeling [GO:0043044]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome disassembly [GO:0006337]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of transcription from RNA polymerase II promoter involved in forebrain neuron fate commitment [GO:0021882]; transcription, DNA-templated [GO:0006351]ichromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]HFUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.P05556ITB1Integrin beta-1iSUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium mem< brane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome. Melanosome. Cleavage furrow. Cell projection, lamellipodium. Cell projection, ruffle. Note=Isoform 2 does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. {ECO:0000269|PubMed:10455171, ECO:0000303|PubMed:10455171}.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane, sarcolemma {ECO:0000250}. Cell junction {ECO:0000250}. Note=In cardiac muscle, isoform 5 is found in costameres and intercalated disks. {ECO:0000250}.axon extension [GO:0048675]; axon guidance [GO:0007411]; B cell differentiation [GO:0030183]; blood coagulation [GO:0007596]; calcium-independent cell-matrix adhesion [GO:0007161]; cardiac muscle cell differentiation [GO:0055007]; cell-cell adhesion mediated by integrin [GO:0033631]; cell fate specification [GO:0001708]; cell junction assembly [GO:0034329]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell-substrate adhesion [GO:0031589]; cellular defense response [GO:0006968]; dendrite morphogenesis [GO:0048813]; extracellular matrix organization [GO:0030198]; formation of radial glial scaffolds [GO:0021943]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell migration [GO:0008354]; heterotypic cell-cell adhesion [GO:0034113]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; integrin-mediated signaling pathway [GO:0007229]; in utero embryonic development [GO:0001701]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; leukocyte tethering or rolling [GO:0050901]; mesodermal cell differentiation [GO:0048333]; negative regulation of anoikis [GO:2000811]; negative regulation of cell differentiation [GO:0045596]; negative regulation of Rho protein signal transduction [GO:0035024]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell proliferation [GO:0008284]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; regulation of cell cycle [GO:0051726]; regulation of collagen catabolic process [GO:0010710]; regulation of immune response [GO:0050776]; sarcomere organization [GO:0045214]; small GTPase mediated signal transduction [GO:0007264]; visual learning [GO:0008542]@actin binding [GO:0003779]; cell adhesion molecule binding [GO:0050839]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; virus receptor activity [GO:0001618]@cell surface [GO:0009986]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; integrin alpha10-beta1 complex [GO:0034680]; integrin alpha11-beta1 complex [GO:0034681]; integrin alpha1-beta1 complex [GO:0034665]; integrin alpha2-beta1 complex [GO:0034666]; integrin alpha3-beta1 complex [GO:0034667]; integrin alpha7-beta1 complex [GO:0034677]; integrin alpha8-beta1 complex [GO:0034678]; integrin complex [GO:0008305]; intercalated disc [GO:0014704]; invadopodium membrane [GO:0071438]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; myelin sheath abaxonal region [GO:0035748]; neuromuscular junction [GO:0031594]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; recycling endosome [GO:0055037]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383]; synaptic membrane [GO:0097060]g FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:7523423}.; FUNCTION: Isoform 5: Isoform 5 displaces isoform 1 in striated muscles. {ECO:0000250}.Q14563SEM3A Semaphorin-3A*membrane-bound signaling molecule(PC00152)*apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axonogenesis involved in innervation [GO:0060385]; branchiomotor neuron axon guidance [GO:0021785]; dendrite morphogenesis [GO:0048813]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing < hormone neuronal migration to the hypothalamus [GO:0021828]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of epithelial cell migration [GO:0010633]; nerve development [GO:0021675]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neural crest cell migration involved in sympathetic nervous system development [GO:1903045]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; positive regulation of male gonad development [GO:2000020]; positive regulation of neuron migration [GO:2001224]; regulation of axon extension involved in axon guidance [GO:0048841]; regulation of heart rate [GO:0002027]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; semaphorin-plexin signaling pathway involved in neuron projection guidance [GO:1902285]; sensory system development [GO:0048880]; sympathetic ganglion development [GO:0061549]; sympathetic nervous system development [GO:0048485]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal ganglion development [GO:0061551]; trigeminal nerve structural organization [GO:0021637]; ventral trunk neural crest cell migration [GO:0036486]Echemorepellent activity [GO:0045499]; neuropilin binding [GO:0038191]Kaxon [GO:0030424]; dendrite [GO:0030425]; extracellular region [GO:0005576]GFUNCTION: Involved in the development of the olfactory system and in neuronal control of puberty. Induces the collapse and paralysis of neuronal growth cones. Could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Binds to the complex neuropilin-1/plexin-1. {ECO:0000269|PubMed:22416012}.P14314GLU2BGlucosidase 2 subunit beta6cellular protein metabolic process [GO:0044267]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]calcium ion binding [GO:0005509]; ion channel binding [GO:0044325]; phosphoprotein binding [GO:0051219]; protein kinase C binding [GO:0005080]hendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular [GO:0005622]NFUNCTION: Regulatory subunit of glucosidase II. {ECO:0000269|PubMed:10929008}.O95831AIFM1*Apoptosis-inducing factor 1, mitochondrial IndependentSUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion inner membrane. Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis. Colocalizes with EIF3G in the nucleus and perinuclear region.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion intermembrane space {ECO:0000269|PubMed:20111043}. Mitochondrion inner membrane {ECO:0000269|PubMed:20111043}. Note=Has a stronger membrane anchorage than isoform 1.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm {ECO:0000269|PubMed:16365034}.ractivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cell redox homeostasis [GO:0045454]; chromosome condensation [GO:0030261]; DNA catabolic process [GO:0006308]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; mitochondrial respiratory chain complex I assembly [GO:0032981]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic DNA fragmentation [GO:1902510]DNA binding [GO:0003677]; electron carrier activity [GO:0009055]; FAD binding [GO:0071949]; NAD(P)H oxidase activity [GO:0016174]; oxidoreductase activity, acting on NAD(P)H [GO:0016651]cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Functions both as NADH oxidoreductase and as regulator of apoptosis. In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. In contrast, functions as an antiapoptotic factor in normal mitochondria via its NADH oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. Binds to DNA in a sequence-independent manner. {ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225, ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327}.P09038FGF2Fibroblast growth factor 2SUBCELLULAR LOCATION: Secreted. Nucleus. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57.@ activation of MAPK activity [GO:0000187]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration involved in sprouting angiogenesis [GO:0002042]; chemotaxis [GO:0006935]; chondroblast differentiation [GO:0060591]; embryonic morphogenesis [GO:0048598]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix organization [GO:0030198]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; growth factor dependent regulation of skeletal muscle satellite cell proliferation [GO:0014843]; hyaluronan catabolic process [GO:0030214]; innate immune response [GO:0045087]; inositol phosphate biosynthetic process [GO:0032958]; insulin receptor signaling pathway [GO:0008286]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell death [GO:0060548]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of wound healing [GO:0061045]; nervous system development [GO:0007399]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ morphogenesis [GO:0009887]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; positive chemotaxis [GO:0050918]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell division [GO:0051781]; positive regulation of cell fate specification [GO:0042660]; positive regulation of cell proliferation [GO:0008284]; positive regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000546]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of phospholipase C activity [GO:0010863]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of transcription, DNA-templa< ted [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; Ras protein signal transduction [GO:0007265]; regulation of angiogenesis [GO:0045765]; regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000544]; release of sequestered calcium ion into cytosol [GO:0051209]; signal transduction [GO:0007165]; somatic stem cell maintenance [GO:0035019]; wound healing [GO:0042060]chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]Yextracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. {ECO:0000269|PubMed:1721615, ECO:0000269|PubMed:8663044}.Q92520FAM3C Protein FAM3CSUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic vesicle {ECO:0000269|PubMed:16959614}. Note=Cytoplasmic in some cancer cells.cytokine activity [GO:0005125]cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]fFUNCTION: May be involved in retinal laminar formation. Promotes epithelial to mesenchymal transition.Q5T0B9ZN362Zinc finger protein 3628DNA binding [GO:0003677]; metal ion binding [GO:0046872]8FUNCTION: May be involved in transcriptional regulation.O15320CTGE5cTAGE family member 5&enzyme activator activity [GO:0008047]#FUNCTION: Tumor-associated antigen.Q3T906GNPTA<N-acetylglucosamine-1-phosphotransferase subunits alpha/betaSnare transports(3)ZSUBCELLULAR LOCATION: N-acetylglucosamine-1-phosphotransferase subunit alpha: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: N-acetylglucosamine-1-phosphotransferase subunit beta: Golgi apparatus membrane {ECO:0000269|PubMed:16120602, ECO:0000269|PubMed:16200072, ECO:0000269|PubMed:21719679, ECO:0000269|PubMed:23733939, ECO:0000269|PubMed:24375680}; Single-pass type II membrane protein {ECO:0000305}.carbohydrate phosphorylation [GO:0046835]; cell differentiation [GO:0030154]; lysosome organization [GO:0007040]; N-glycan processing to lysosome [GO:0016256]; protein secretion [GO:0009306]calcium ion binding [GO:0005509]; UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity [GO:0003976]|Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]dFUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment. {ECO:0000269|PubMed:19955174, ECO:0000269|PubMed:23733939}.Q9Y6X1SERP11Stress-associated endoplasmic reticulum protein 1SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; endoplasmic reticulum unfolded protein response [GO:0030968]; glucose metabolic process [GO:0006006]; IRE1-mediated unfolded protein response [GO:0036498]; multicellular organismal aging [GO:0010259]; muscle organ morphogenesis [GO:0048644]; plasma membrane organization [GO:0007009]; positive regulation of growth hormone secretion [GO:0060124]; positive regulation of insulin secretion [GO:0032024]; positive regulation of organ growth [GO:0046622]; positive regulation of translation [GO:0045727]; post-embryonic development [GO:0009791]; protein glycosylation [GO:0006486]; protein transport [GO:0015031]; response to stress [GO:0006950]; skeletal system development [GO:0001501]cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; ribosome [GO:0005840]iFUNCTION: Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity). {ECO:0000250}.Q7L0Y3MRRP1&Mitochondrial ribonuclease P protein 1~SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23473034}.Nmitochondrial RNA 5'-end processing [GO:0000964]; tRNA processing [GO:0008033]Ymitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:21593607}.Q6DD88ATLA3 Atlastin-3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:24459106}; Multi-pass membrane protein {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:24459106}. Note=Localizes to endoplasmic reticulum tubules and accumulates in punctuate structures corresponding to 3-way junctions, which represent crossing-points at which the tubules build a polygonal network.zendoplasmic reticulum organization [GO:0007029]; Golgi organization [GO:0007030]; protein homooligomerization [GO:0051260]^GTPase activity [GO:0003924]; GTP binding [GO:0005525]; identical protein binding [GO:0042802] FUNCTION: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976}.Q5U5X0LYRM7!Complex III assembly factor LYRM7ISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:23168492}.wFUNCTION: Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. {ECO:0000269|PubMed:23168492}.P51148RAB5CRas-related protein Rab-5C2SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.intracellular protein transport [GO:0006886]; plasma membrane to endosome transport [GO:0048227]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]1early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; plasma membrane [GO:0005886]Q7LGA3HS2ST&Heparan sulfate 2-O-sulfotransferase 1carbohydrate metabolic process [GO:0005975]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; small molecule metabolic process [GO:0044281]&sulfotransferase activity [GO:0008146]_Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; < membrane [GO:0016020]FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues (By similarity). {ECO:0000250}.Q6ZMK1CYHR1%Cysteine and histidine-rich protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Shows a prominent perinuclear and cytoplasmic localization. {ECO:0000250}.enuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]Q9P2X0DPM30Dolichol-phosphate mannosyltransferase subunit 3:carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GPI anchor biosynthetic process [GO:0006506]; post-translational protein modification [GO:0043687]; protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan [GO:0018406]; protein mannosylation [GO:0035268]; protein N-linked glycosylation via asparagine [GO:0018279]; protein O-linked mannosylation [GO:0035269]; regulation of protein stability [GO:0031647] dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; mannosyltransferase complex [GO:0031501]; membrane [GO:0016020]FUNCTION: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. {ECO:0000269|PubMed:10835346}.P43155CACPCarnitine O-acetyltransferaseASUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Peroxisome {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Peroxisome {ECO:0000305}.carnitine metabolic process, CoA-linked [GO:0019254]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]Rcarnitine O-acetyltransferase activity [GO:0004092]; receptor binding [GO:0005102]endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]FUNCTION: Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.Q8TAD4ZNT5Zinc transporter 5SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503, ECO:0000269|PubMed:15525635}; Multi-pass membrane protein {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503, ECO:0000269|PubMed:15525635}. Note=Perimeter of granules, localizes to the brush border membrane of the enterocyte. Concentrated in early compartments of the secretory pathway such as COPII-coated vesicles.Jcellular protein metabolic process [GO:0044267]; cellular zinc ion homeostasis [GO:0006882]; cobalt ion transport [GO:0006824]; regulation of proton transport [GO:0010155]; response to zinc ion [GO:0010043]; transmembrane transport [GO:0055085]; zinc II ion transmembrane transport [GO:0071577]; zinc II ion transport [GO:0006829]Wzinc ion binding [GO:0008270]; zinc ion transmembrane transporter activity [GO:0005385]apical plasma membrane [GO:0016324]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667][FUNCTION: Functions as a zinc transporter. May be a transporter of zinc into beta cells in order to form insulin crystals. Partly regulates cellular zinc homeostasis. Required with ZNT7 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6 and ZNT7 for the activation of TNAP. {ECO:0000269|PubMed:11904301, ECO:0000269|PubMed:11937503, ECO:0000269|PubMed:15276077, ECO:0000269|PubMed:15525635, ECO:0000269|PubMed:15994300}.Q96JB5CK5P3,CDK5 regulatory subunit-associated protein 3brain development [GO:0007420]; cell proliferation [GO:0008283]; mitotic G2/M transition checkpoint [GO:0044818]; mitotic G2 DNA damage checkpoint [GO:0007095]; negative regulation of cellular protein catabolic process [GO:1903363]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein ufmylation [GO:0071569]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of neuron differentiation [GO:0045664]cyclin binding [GO:0030332]; MDM2/MDM4 family protein binding [GO:0097371]; NF-kappaB binding [GO:0051059]; protein kinase binding [GO:0019901]; ubiquitin-like protein ligase binding [GO:0044389]centrosome [GO:0005813]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; membrane [GO:0016020]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Potential regulator of CDK5 activity. May be involved in cell proliferation. Regulates CDK5 activity via its interaction with CDK5R1 (By similarity). {ECO:0000250}.O75182SIN3B&Paired amphipathic helix protein Sin3bESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}._cardiac muscle tissue development [GO:0048738]; cellular lipid metabolic process [GO:0044255]; histone deacetylation [GO:0016575]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; skeletal muscle tissue development [GO:0007519]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]achromatin binding [GO:0003682]; RNA polymerase II transcription corepressor activity [GO:0001106]autosome [GO:0030849]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Sin3 complex [GO:0016580]; X chromosome [GO:0000805]; XY body [GO:0001741]; Y chromosome [GO:0000806]hFUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription (By similarity). {ECO:0000250}.P46977STT3ALDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3Acellular protein metabolic process [GO:0044267]; co-translational protein modification [GO:0043686]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]aFUNCTION: Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex < associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A. {ECO:0000269|PubMed:19167329}.Q05519SRS11'Serine/arginine-rich splicing factor 11LSUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with spliceosome components.Ggene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366],FUNCTION: May function in pre-mRNA splicing.Q13423NNTM&NAD(P) transhydrogenase, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.Vcell redox homeostasis [GO:0045454]; cellular metabolic process [GO:0044237]; hydrogen ion transmembrane transport [GO:1902600]; oxidation-reduction process [GO:0055114]; proton transport [GO:0015992]; reactive oxygen species metabolic process [GO:0072593]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]NAD(P)+ transhydrogenase (AB-specific) activity [GO:0008750]; NAD(P)+ transhydrogenase (B-specific) activity [GO:0003957]; NAD(P)+ transhydrogenase activity [GO:0008746]; NAD binding [GO:0051287]; NADP binding [GO:0050661]integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]; mitochondrion [GO:0005739] FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland. {ECO:0000269|PubMed:22634753}.Q9Y3L5RAP2CRas-related protein Rap-2cSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17447155}. Recycling endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.]establishment of endothelial intestinal barrier [GO:0090557]; negative regulation of cell migration [GO:0030336]; positive regulation of protein autophosphorylation [GO:0031954]; Rap protein signal transduction [GO:0032486]; regulation of nucleic acid-templated transcription [GO:1903506]; regulation of protein tyrosine kinase activity [GO:0061097]cGDP binding [GO:0019003]; GTP binding [GO:0005525]; transcription coactivator activity [GO:0003713]bicellular tight junction [GO:0005923]; cell-cell contact zone [GO:0044291]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]1FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May play a role in SRE-mediated gene transcription. {ECO:0000269|PubMed:17447155}.P48060GLIP1%Glioma pathogenesis-related protein 1\cellular lipid metabolic process [GO:0044255]; small molecule metabolic process [GO:0044281]extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q5VUA4ZN318Zinc finger protein 318;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}.meiotic cell cycle [GO:0051321]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]@nucleic acid binding [GO:0003676]; zinc ion binding [GO:0008270]FUNCTION: Repressed AR-mediated transcriptional activation. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division (By similarity). {ECO:0000250}.P13498CY24ACytochrome b-245 light chain_SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585859, ECO:0000269|PubMed:22808130}.rantigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular response to amino acid stimulus [GO:0071230]; cellular response to gamma radiation [GO:0071480]; cellular response to glucose stimulus [GO:0071333]; cellular response to mechanical stimulus [GO:0071260]; cellular response to organic cyclic compound [GO:0071407]; cellular response to tumor necrosis factor [GO:0071356]; cytochrome complex assembly [GO:0017004]; hydrogen peroxide biosynthetic process [GO:0050665]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; interaction with host [GO:0051701]; negative regulation of glomerular filtration by angiotensin [GO:0003106]; oxidation-reduction process [GO:0055114]; phagosome maturation [GO:0090382]; positive regulation of cell growth [GO:0030307]; positive regulation of defense response to bacterium [GO:1900426]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of mucus secretion [GO:0070257]; positive regulation of phagocytosis [GO:0050766]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of toll-like receptor 2 signaling pathway [GO:0034137]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; respiratory burst [GO:0045730]; response to drug [GO:0042493]; response to interleukin-1 [GO:0070555]; response to nutrient levels [GO:0031667]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle hypertrophy [GO:0014895]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]electron carrier activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; SH3 domain binding [GO:0017124]; superoxide-generating NADPH oxidase activity [GO:0016175]apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrion [GO:0005739]; NADPH oxidase complex [GO:0043020]; neuronal cell body [GO:0043025]; perinuclear endoplasmic reticulum [GO:0097038]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. {ECO:0000269|PubMed:15824103}.Q9BVT8TMUB1<Transmembrane and ubiquitin-like domain-containing protein 1.SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19254477}. Nucleus {ECO:0000269|PubMed:19254477}. Note=Predominantly nuclear during growth arrest (By similarity). Actively exported from the nucleus in dividing cells. {ECO:0000250}.HER-associated ubiquitin-dependent protein catabolic process [GO:0030433]]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]FUNCTION: May contribute to the regulation of translation during cell-cycle progression. May contribute to the regulation of cell proliferation (By similarity). {ECO:0000250}.O43615TIM44=Mitochondrial import inner membrane t< ranslocase subunit TIM44ATP binding [GO:0005524]; chaperone binding [GO:0051087]; P-P-bond-hydrolysis-driven protein transmembrane transporter activity [GO:0015450]hmitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]>FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source.Q92504S39A7Zinc transporter SLC39A7SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane.Htransmembrane transport [GO:0055085]; zinc II ion transport [GO:0006829]9metal ion transmembrane transporter activity [GO:0046873]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleoplasm [GO:0005654].FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic reticulum/Golgi apparatus to the cytosol. Transport is stimulated by growth factors, such as EGF, and Ca(2+), as well as by exogenous Zn(2+). {ECO:0000269|PubMed:14525538, ECO:0000269|PubMed:15705588, ECO:0000269|PubMed:22317921}.Q58DX5NADL2DInactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2(FUNCTION: May be catalytically inactive.P60033CD81 CD81 antigenactivation of MAPK activity [GO:0000187]; cell proliferation [GO:0008283]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol metabolic process [GO:0046488]; positive regulation of 1-phosphatidylinositol 4-kinase activity [GO:0043128]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell proliferation [GO:0008284]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein catabolic process in the vacuole [GO:1904352]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein localization [GO:0008104]; protein localization to lysosome [GO:0061462]; receptor-mediated virion attachment to host cell [GO:0046813]; regulation of cell motility [GO:2000145]; regulation of immune response [GO:0050776]; regulation of protein stability [GO:0031647]; viral entry into host cell [GO:0046718]\MHC class II protein complex binding [GO:0023026]; transferrin receptor binding [GO:1990459]extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]; vesicle [GO:0031982]FUNCTION: May play an important role in the regulation of lymphoma cell growth. Interacts with a 16-kDa Leu-13 protein to form a complex possibly involved in signal transduction. May act as the viral receptor for HCV.Q96CS3FAF2FAS-associated factor 2FSUBCELLULAR LOCATION: Cytoplasm. Lipid droplet. Endoplasmic reticulum.ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; lipid particle organization [GO:0034389]; negative regulation of catalytic activity [GO:0043086]; response to unfolded protein [GO:0006986]; retrograde protein transport, ER to cytosol [GO:0030970]lipase binding [GO:0035473]; lipase inhibitor activity [GO:0055102]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]FUNCTION: Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:18711132, PubMed:24215460). {ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:24215460}.P17301ITA2Integrin alpha-2axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; collagen-activated signaling pathway [GO:0038065]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; mesodermal cell differentiation [GO:0048333]; organ morphogenesis [GO:0009887]; substrate-dependent cell migration [GO:0006929]collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; collagen receptor activity [GO:0038064]; metal ion binding [GO:0046872]; virus receptor activity [GO:0001618]basal part of cell [GO:0045178]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; integrin alpha2-beta1 complex [GO:0034666]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.P20337RAB3BRas-related protein Rab-3Bantigen processing and presentation [GO:0019882]; intracellular protein transport [GO:0006886]; peptidyl-cysteine methylation [GO:0018125]; positive regulation of dopamine uptake involved in synaptic transmission [GO:0051586]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0017157]; regulation of vesicle size [GO:0097494]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking involved in exocytosis [GO:0006904]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; synaptic vesicle [GO:0008021]; vesicle [GO:0031982]Q9BQQ3GORS1#Golgi reassembly-stacking protein 1SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11706049}; Peripheral membrane protein {ECO:0000269|PubMed:11706049}; Cytoplasmic side {ECO:0000269|PubMed:11706049}. Note=Undergoes rapid exchange with the cytosol.Golgi organization [GO:0007030]; mitotic cell cycle [GO:0000278]; negative regulation of dendrite morphogenesis [GO:0050774]; protein N-linked glycosylation [GO:0006487]; protein transport [GO:0015031]9Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]FUNCTION: Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis. Also mediates, via its interaction with GM130, the docking of transport vesicles with the Golgi membranes.P67812SC11A1Signal peptidase complex catalytic subunit SEC11AP21796VDAC13Voltage-dependent anion-selective channel protein 1VDAC|SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:7539795}. Cell membrane {ECO:0000269|PubMed:7539795}.anion transport [GO:0006820]; apoptotic process [GO:0006915]; behavioral fear response [GO:0001662]; epithelial cell differentiation [GO:0030855]; learning [GO:0007612]; mitochondrial calcium ion transport [GO:0006851]; neuron-neuron synaptic transmission [GO:0007270]; regulation of anion transmembrane transport [GO:1903959]; regulation of mitochondrion degradation [GO:1903146]; viral process [GO:0016032]sporin activity [GO:0015288]; protein kinase binding [GO:0019901]; voltage-gated anion channel activity [GO:0008308];extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209];< nucleus [GO:0005634]; plasma membrane [GO:0005886]; pore complex [GO:0046930]FUNCTION: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. {ECO:0000269|PubMed:11845315, ECO:0000269|PubMed:15033708, ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:20230784}.Q6NW40RGMBRGM domain family member BwSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Membrane raft {ECO:0000250}.axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; cell adhesion [GO:0007155]; positive regulation of transcription, DNA-templated [GO:0045893]; signal transduction [GO:0007165]Hcoreceptor activity [GO:0015026]; identical protein binding [GO:0042802]anchored component of plasma membrane [GO:0046658]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]rFUNCTION: Member of the repulsive guidance molecule (RGM) family that contributes to the patterning of the developing nervous system (By similarity). Acts as a bone morphogenetic protein (BMP) coreceptor that potentiates BMP signaling (By similarity). Promotes neuronal adhesion (By similarity). May inhibit neurite outgrowth. {ECO:0000250, ECO:0000269|PubMed:19324014}.Q9BQ49SMIM7!Small integral membrane protein 7P11233RALARas-related protein Ral-A RAS/RGL/RalSUBCELLULAR LOCATION: Cell surface. Cell membrane; Lipid-anchor; Cytoplasmic side. Cleavage furrow. Midbody. Note=Prior to LPA treatment found predominantly at the cell surface and in the presence of LPA colocalizes with LPAR1 and LPAR2 in the endocytic vesicles. During early cytokinesis localizes at the cleavage furrow membrane. Colocalizes with EXOC2 at the early midbody ring and persists there till maturation of the midbody.actin cytoskeleton reorganization [GO:0031532]; chemotaxis [GO:0006935]; cytokinesis [GO:0000910]; exocytosis [GO:0006887]; membrane organization [GO:0061024]; membrane raft localization [GO:0051665]; neural tube closure [GO:0001843]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of filopodium assembly [GO:0051491]; Ras protein signal transduction [GO:0007265]; regulation of exocytosis [GO:0017157]; signal transduction [GO:0007165]; viral process [GO:0016032]ATPase binding [GO:0051117]; Edg-2 lysophosphatidic acid receptor binding [GO:0031755]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin binding [GO:0017022]; ubiquitin protein ligase binding [GO:0031625]cell surface [GO:0009986]; cleavage furrow [GO:0032154]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; midbody [GO:0030496]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]]FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. {ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:20005108}.Q99714HCD2&3-hydroxyacyl-CoA dehydrogenase type-2_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18984158}.Sbranched-chain amino acid catabolic process [GO:0009083]; cell aging [GO:0007569]; cellular nitrogen compound metabolic process [GO:0034641]; Leydig cell differentiation [GO:0033327]; lipid metabolic process [GO:0006629]; protein homotetramerization [GO:0051289]; small molecule metabolic process [GO:0044281]; tRNA processing [GO:0008033]3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetoacetyl-CoA reductase activity [GO:0018454]; beta-amyloid binding [GO:0001540]; cholate 7-alpha-dehydrogenase activity [GO:0008709]; estradiol 17-beta-dehydrogenase activity [GO:0004303]; NAD binding [GO:0051287]; poly(A) RNA binding [GO:0044822]; steroid binding [GO:0005496]; testosterone dehydrogenase [NAD(P)] activity [GO:0030283]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. Catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:9338779}.Q15006EMC2%ER membrane protein complex subunit 2USUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22119785}.cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; ER membrane protein complex [GO:0072546]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]Q4ZIN3MBRL MembralinSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16084606}. Note=Cytoplasmic according to PubMed:16084606.Ccytoplasm [GO:0005737]; integral component of membrane [GO:0016021]O00411RPOM*DNA-directed RNA polymerase, mitochondrialgene expression [GO:0010467]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; transcription from mitochondrial promoter [GO:0006390]; transcription initiation from mitochondrial promoter [GO:0006391]mDNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; poly(A) RNA binding [GO:0044822]bmitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000269|PubMed:21278163}.Q9NWT8AKIP#Aurora kinase A-interacting proteiniSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23908630}. Nucleus {ECO:0000269|PubMed:23908630}.Zmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; negative regulation of mitotic nuclear division [GO:0045839]; organelle organization [GO:0006996]; positive regulation of proteolysis [GO:0045862]intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]zFUNCTION: May act as a negative regulator of Aurora-A kinase, by down-regulatio< n through proteasome-dependent degradation.Q9GZM5YIPF3 Protein YIPF3SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Note=Localization to the cytoplasm or to the cell membrane is developmentally and ontogenetically regulated.!cell differentiation [GO:0030154]Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]FUNCTION: Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis. {ECO:0000269|PubMed:12490290, ECO:0000269|PubMed:21757827}.Q9Y3A6TMED5/Transmembrane emp24 domain-containing protein 5SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19948005}; Single-pass type I membrane protein {ECO:0000269|PubMed:19948005}. Note=Probably cycles between compartments of the early secretatory pathway.CGolgi ribbon formation [GO:0090161]; protein transport [GO:0015031]Scis-Golgi network [GO:0005801]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]>FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport. {ECO:0000269|PubMed:19948005}.Q4LE39ARI4B0AT-rich interactive domain-containing protein 4BSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. Cytoplasm {ECO:0000269|PubMed:11481388, ECO:0000269|PubMed:15247124}. Note=Cytoplasmic in breast cancer cells.mchromatin organization [GO:0006325]; establishment of Sertoli cell barrier [GO:0097368]; gene expression [GO:0010467]; histone H3-K9 trimethylation [GO:0036124]; histone H4-K20 trimethylation [GO:0034773]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of gene expression, epigenetic [GO:0040029]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]8transcription regulatory region DNA binding [GO:0044212]FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. {ECO:0000269|PubMed:12724404}.O60476MA1A21Mannosyl-oligosaccharide 1,2-alpha-mannosidase IBUSUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein.cellular protein metabolic process [GO:0044267]; lung alveolus development [GO:0048286]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; respiratory gaseous exchange [GO:0007585]fcalcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).Q9BRT2UQCC2:Ubiquinol-cytochrome-c reductase complex assembly factor 2$SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid. Mitochondrion. Mitochondrion intermembrane space {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. Note=Predominantly expressed in the mitochondrial inner membrane. {ECO:0000250}.mmitochondrial respiratory chain complex III assembly [GO:0034551]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of mitochondrial translation [GO:0070131]; regulation of insulin secretion [GO:0050796]; regulation of oxidative phosphorylation [GO:0002082]; regulation of skeletal muscle cell differentiation [GO:2001014]mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability. {ECO:0000269|PubMed:22363741, ECO:0000269|PubMed:24385928}.Q9BVV7TIM21=Mitochondrial import inner membrane translocase subunit Tim21gSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.cellular protein metabolic process [GO:0044267]; mitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrial respiratory chain complex IV assembly [GO:0033617]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]vintegral component of membrane [GO:0016021]; mitochondrial inner membrane presequence translocase complex [GO:0005744]FUNCTION: Participates in the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Also required for assembly of mitochondrial respiratory chain complex I and complex IV as component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex. TIM21 probably shuttles between the presequence translocase and respiratory-chain assembly intermediates in a process that promotes incorporation of early nuclear-encoded subunits into these complexes. {ECO:0000269|PubMed:23260140}.P07711CATL1 Cathepsin L1aadaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; macrophage apoptotic process [GO:0071888]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; toll-like receptor signaling pathway [GO:0002224]collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; fibronectin binding [GO:0001968]; histone binding [GO:0042393]; proteoglycan binding [GO:0043394]; serpin family protein binding [GO:0097655]endolysosome lumen [GO:0036021]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; nucleus [GO:0005634]IFUNCTION: Important for the overall degradation of proteins in lysosomes.P51689ARSDArylsulfatase D-SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.cellular protein metabolic process [GO:0044267]; glycosphingolipid metabolic process [GO:0006687]; post-translational protein< modification [GO:0043687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]Carylsulfatase activity [GO:0004065]; metal ion binding [GO:0046872]cendoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]Q9NX40OCAD1 OCIA domain-containing protein 1-SUBCELLULAR LOCATION: Endosome {ECO:0000250}.Hendosome [GO:0005768]; membrane [GO:0016020]; mitochondrion [GO:0005739]P28288ABCD3*ATP-binding cassette sub-family D member 3SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:10704444}.cfatty acid beta-oxidation [GO:0006635]; fatty acid biosynthetic process [GO:0006633]; peroxisomal long-chain fatty acid import [GO:0015910]; peroxisome organization [GO:0007031]; response to drug [GO:0042493]; response to organic cyclic compound [GO:0014070]; transmembrane transport [GO:0055085]; very long-chain fatty acid catabolic process [GO:0042760]ATPase activity [GO:0016887]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; long-chain fatty acid transporter activity [GO:0005324]; protein homodimerization activity [GO:0042803]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]pFUNCTION: Probable transporter involved in the transport of branched-chain fatty acids and C27 bile acids into the peroxisome; the latter function is a crucial step in bile acid biosynthesis (PubMed:25168382). The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity (PubMed:11248239). {ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:25168382}.Q10471GALT2/Polypeptide N-acetylgalactosaminyltransferase 2.SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein {ECO:0000269|PubMed:9394011}. Secreted {ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.Ycellular protein metabolic process [GO:0044267]; immunoglobulin biosynthetic process [GO:0002378]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of Golgi membrane [GO:0030173]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. {ECO:0000269|PubMed:12438318, ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:7592619, ECO:0000269|PubMed:9295285}.Q10469MGAT2FAlpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase1cellular protein metabolic process [GO:0044267]; oligosaccharide biosynthetic process [GO:0009312]; oligosaccharide metabolic process [GO:0009311]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]~alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity [GO:0008455]; carbohydrate binding [GO:0030246]Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of membrane [GO:0016021]; membrane [GO:0016020]^FUNCTION: Catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans.O75683SURF6Surfeit locus protein 6SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Granular component of the nucleolus. {ECO:0000250}.TDNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]Qgranular component [GO:0001652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity). {ECO:0000250}.O94919ENDD1(Endonuclease domain-containing 1 proteineendonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]8FUNCTION: May act as a DNase and a RNase. {ECO:0000305}.P56159GFRA1GDNF family receptor alpha-1ZSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.axon guidance [GO:0007411]; cell surface receptor signaling pathway [GO:0007166]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]dglial cell-derived neurotrophic factor receptor activity [GO:0016167]; receptor binding [GO:0005102]anchored component of membrane [GO:0031225]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]FUNCTION: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor (By similarity). {ECO:0000250}.Q13641TPBGTrophoblast glycoproteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24582434}; Single-pass type I membrane protein {ECO:0000269|PubMed:24582434}.Pcell adhesion [GO:0007155]; positive regulation of synapse assembly [GO:0051965]qcell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; integral component of plasma membrane [GO:0005887]FUNCTION: May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization. {ECO:0000269|PubMed:22100263}.Q9HCC0MCCB9Methylcrotonoyl-CoA carboxylase beta chain, mitochondrialfSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:16023992}.zbiotin metabolic process [GO:0006768]; branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; coenzyme A metabolic process [GO:0015936]; leucine catabolic process [GO:0006552]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]OATP binding [GO:0005524]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]Scytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. {ECO:0000269|PubMed:17360195}.P48651PTSS1Phosphatidylserine synthase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250}.glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylserine biosynthetic process [GO:0006659]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]!transferase activity [GO:0016740]7FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine< .Q6NUM9RETST!All-trans-retinol 13,14-reductasenSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.Poxidation-reduction process [GO:0055114]; retinol metabolic process [GO:0042572]]all-trans-retinol 13,14-reductase activity [GO:0051786]; oxidoreductase activity [GO:0016491]endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]rFUNCTION: Retinol saturase carrying out the saturation of the 13-14 double bond of all-trans-retinol to produce all-trans-13,14-dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A (By similarity). {ECO:0000250}.Q86UL3GPAT4&Glycerol-3-phosphate acyltransferase 4SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18238778}; Multi-pass membrane protein {ECO:0000269|PubMed:18238778}.acyl-CoA metabolic process [GO:0006637]; CDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; diacylglycerol metabolic process [GO:0046339]; fatty acid metabolic process [GO:0006631]; glandular epithelial cell maturation [GO:0002071]; glycerophospholipid biosynthetic process [GO:0046474]; lactation [GO:0007595]; lipid biosynthetic process [GO:0008610]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid metabolic process [GO:0006644]; regulation of multicellular organism growth [GO:0040014]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]<glycerol-3-phosphate O-acyltransferase activity [GO:0004366]FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. {ECO:0000269|PubMed:18238778}.Q8N2F6ARM10&Armadillo repeat-containing protein 10SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12839973}; Single-pass membrane protein {ECO:0000269|PubMed:12839973}.!regulation of growth [GO:0040008]tendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]FUNCTION: May play a role in cell survival and cell growth. May suppress the transcriptional activity of p53/TP53. {ECO:0000269|PubMed:12839973, ECO:0000269|PubMed:17904127}.Q12800TFCP2%Alpha-globin transcription factor CP2sSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1732747, ECO:0000269|PubMed:7828600, ECO:0000269|PubMed:8114710}.sregulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; protein C-terminus binding [GO:0008022]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter. {ECO:0000250, ECO:0000269|PubMed:10455131, ECO:0000269|PubMed:1732747, ECO:0000269|PubMed:8035790, ECO:0000269|PubMed:8157699}.P55084ECHB0Trifunctional enzyme subunit beta, mitochondrialFatty acid elongationSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21527675}. Mitochondrion inner membrane {ECO:0000269|PubMed:21527675}. Mitochondrion outer membrane {ECO:0000269|PubMed:21527675}. Endoplasmic reticulum {ECO:0000269|PubMed:21527675}.cardiolipin acyl-chain remodeling [GO:0035965]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; glycerophospholipid biosynthetic process [GO:0046474]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetyl-CoA C-acyltransferase activity [GO:0003988]; enoyl-CoA hydratase activity [GO:0004300]; long-chain-3-hydroxyacyl-CoA dehydrogenase activity [GO:0016509]; poly(A) RNA binding [GO:0044822]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]Q8N0U8VKORL<Vitamin K epoxide reductase complex subunit 1-like protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:24532791}; Multi-pass membrane protein {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:24532791}.cellular response to oxidative stress [GO:0034599]; peptidyl-glutamic acid carboxylation [GO:0017187]; vitamin K metabolic process [GO:0042373]dquinone binding [GO:0048038]; vitamin-K-epoxide reductase (warfarin-sensitive) activity [GO:0047057]xFUNCTION: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K (in vitro), and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins. {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358, ECO:0000269|PubMed:24532791}.P42702LIFR#Leukemia inhibitory factor receptorSUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.;cell surface receptor signaling pathway [GO:0007166]; ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; cytokine-mediated signaling pathway [GO:0019221]; leukemia inhibitory factor signaling pathway [GO:0048861]; negative regulation of muscle cell apoptotic process [GO:0010656]; neuron projection morphogenesis [GO:0048812]; oncostatin-M-mediated signaling pathway [GO:0038165]; organ regeneration [GO:0031100]; positive regulation of cell proliferation [GO:0008284]; response to cytokine [GO:0034097]; response to organic cyclic compound [GO:0014070]ciliary neurotrophic factor receptor binding [GO:0005127]; growth factor binding [GO:0019838]; leukemia inhibitory factor receptor activity [GO:0004923]uextracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; receptor complex [GO:0043235]FUNCTION: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.Q9H1X3DJC25"DnaJ homolog subfamily C member 25Q16850CP51ALanosterol 14-alpha demethylase Steroid biosynthesiseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}. Microsome membrane {ECO:0000305}.cholesterol biosynthetic process [GO:0006695]; demethylation [GO:0070988]; small molecule metabolic process [GO:0044281]; steroid biosynthetic process [GO:0006694]; sterol metabolic process [GO:0016125]; xenobiotic metabolic process [GO:0006805]eheme binding [GO:0020037]; iron ion binding [GO:0005506]; sterol 14-demethylase activity [GO:0008398]FUNCTION: Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. {ECO:0000269|PubMed:20149798}.Q16363LAMA4Laminin subunit alpha-4sSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; regulation of cell adhesion [GO:0030155]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]8extracellular matrix structural constituent [GO:0005201]basal lamina [< GO:0005605]; basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.Q96EY1DNJA30DnaJ homolog subfamily A member 3, mitochondrial7SUBCELLULAR LOCATION: Mitochondrion matrix. Cytoplasm, cytosol {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK. {ECO:0000250}.activation-induced cell death of T cells [GO:0006924]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cell aging [GO:0007569]; mitochondrial DNA replication [GO:0006264]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of interferon-gamma-mediated signaling pathway [GO:0060336]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of programmed cell death [GO:0043069]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuromuscular junction development [GO:0007528]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of T cell proliferation [GO:0042102]; protein folding [GO:0006457]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to heat [GO:0009408]; response to interferon-gamma [GO:0034341]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]; small GTPase mediated signal transduction [GO:0007264]; T cell differentiation in thymus [GO:0033077]GATP binding [GO:0005524]; chaperone binding [GO:0051087]; GTPase regulator activity [GO:0030695]; interferon-gamma receptor binding [GO:0005133]; metal ion binding [GO:0046872]; NF-kappaB binding [GO:0051059]; protein kinase binding [GO:0019901]; transcription factor binding [GO:0008134]; unfolded protein binding [GO:0051082]wcell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of plasma membrane [GO:0019897]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211] FUNCTION: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.Q96F07CYFP2&Cytoplasmic FMR1-interacting protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:17245118}. Cytoplasm, perinuclear region. Cell junction, synapse, synaptosome. Note=Highly expressed in the perinuclear region. Enriched in synaptosomes. Treatment with leptomycin-B triggers translocation to the nucleus. {ECO:0000250|UniProtKB:Q5SQX6, ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:17245118}.activation of cysteine-type endopeptidase activity [GO:0097202]; apoptotic process [GO:0006915]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; positive regulation of proteolysis [GO:0045862]; single organismal cell-cell adhesion [GO:0016337]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; synapse [GO:0045202]FUNCTION: Involved in T-cell adhesion and p53/TP53-dependent induction of apoptosis. Does not bind RNA. {ECO:0000269|PubMed:10449408, ECO:0000269|PubMed:15048733, ECO:0000269|PubMed:17245118}.Q06136KDSR"3-ketodihydrosphingosine reductaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15328338}; Multi-pass membrane protein {ECO:0000269|PubMed:15328338}.3-keto-sphinganine metabolic process [GO:0006666]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]43-dehydrosphinganine reductase activity [GO:0047560]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; membrane [GO:0016020]`FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).Q5JPH6SYEM.Probable glutamate--tRNA ligase, mitochondrialgene expression [GO:0010467]; glutamyl-tRNA aminoacylation [GO:0006424]; tRNA aminoacylation for mitochondrial protein translation [GO:0070127]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; glutamate-tRNA(Gln) ligase activity [GO:0050561]; glutamate-tRNA ligase activity [GO:0004818]; tRNA binding [GO:0000049]=mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.P40939ECHA1Trifunctional enzyme subunit alpha, mitochondrialYcardiolipin acyl-chain remodeling [GO:0035965]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; glycerophospholipid biosynthetic process [GO:0046474]; phospholipid metabolic process [GO:0006644]; response to drug [GO:0042493]; response to insulin [GO:0032868]; small molecule metabolic process [GO:0044281]M3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetyl-CoA C-acetyltransferase activity [GO:0003985]; enoyl-CoA hydratase activity [GO:0004300]; fatty-acyl-CoA binding [GO:0000062]; long-chain-3-hydroxyacyl-CoA dehydrogenase activity [GO:0016509]; long-chain-enoyl-CoA hydratase activity [GO:0016508]; NAD binding [GO:0051287]mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: Bifunctional subunit.O75381PEX14"Peroxisomal membrane protein PEX14SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:19197237}; Peripheral membrane protein {ECO:0000269|PubMed:19197237}; Cytoplasmic side {ECO:0000269|PubMed:19197237}.microtubule anchoring [GO:0034453]; negative regulation of protein binding [GO:0032091]; negative regulation of protein homotetramerization [GO:1901094]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; peroxisome organization [GO:0007031]; peroxisome transport along microtubule [GO:0036250]; protein complex assembly [GO:0006461]; protein homooligomerization [GO:0051260]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, translocation [GO:0016561]beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; protein N-terminus binding [GO:0047485]; receptor binding [GO:0005102]; trans< cription corepressor activity [GO:0003714]integral component of membrane [GO:0016021]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein complex [GO:0043234]NFUNCTION: Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin. {ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:9653144}.Q9UBV2SE1L1Protein sel-1 homolog 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16186509}; Single-pass type I membrane protein {ECO:0000269|PubMed:16186509}.ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; Notch signaling pathway [GO:0007219]; protein stabilization [GO:0050821]; retrograde protein transport, ER to cytosol [GO:0030970]endoplasmic reticulum membrane [GO:0005789]; Hrd1p ubiquitin ligase complex [GO:0000836]; integral component of membrane [GO:0016021]:FUNCTION: May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. {ECO:0000250, ECO:0000269|PubMed:16186509}.O14802RPC1,DNA-directed RNA polymerase III subunit RPC1Wdefense response to virus [GO:0051607]; gene expression [GO:0010467]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of type I interferon production [GO:0032481]; regulation of mitochondrion degradation [GO:1903146]; termination of RNA polymerase III transcription [GO:0006386]; transcription, DNA-templated [GO:0006351]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription from RNA polymerase III promoter [GO:0006383]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; ribonucleoside binding [GO:0032549]; zinc ion binding [GO:0008270]{cytosol [GO:0005829]; DNA-directed RNA polymerase III complex [GO:0005666]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.Q16891MIC60MICOS complex subunit MIC60SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:25781180}.Rcristae formation [GO:0042407]; mitochondrial calcium ion homeostasis [GO:0051560]membrane [GO:0016020]; MICOS complex [GO:0061617]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:22114354, PubMed:25781180). {ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:25781180}.Q9BQA9CQ062 Uncharacterized protein C17orf62Q09472EP300Histone acetyltransferase p300Co-activator(MAML/HATs/SNW1)(8)SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus.apoptotic process [GO:0006915]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to drug [GO:0035690]; cellular response to glucose stimulus [GO:0071333]; cellular response to heat [GO:0034605]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to mineralocorticoid stimulus [GO:0071389]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to retinoic acid [GO:0071300]; cellular response to trichostatin A [GO:0035984]; cellular response to UV [GO:0034644]; chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; digestive tract development [GO:0048565]; G2/M transition of mitotic cell cycle [GO:0000086]; heart development [GO:0007507]; histone H2B acetylation [GO:0043969]; histone H3 acetylation [GO:0043966]; histone H4 acetylation [GO:0043967]; innate immune response [GO:0045087]; internal peptidyl-lysine acetylation [GO:0018393]; internal protein amino acid acetylation [GO:0006475]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; liver development [GO:0001889]; lung development [GO:0030324]; memory [GO:0007613]; mitotic cell cycle [GO:0000278]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of miRNA metabolic process [GO:2000629]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nervous system development [GO:0007399]; Notch signaling pathway [GO:0007219]; N-terminal peptidyl-lysine acetylation [GO:0018076]; organ morphogenesis [GO:0009887]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of axon extension [GO:0045773]; positive regulation of cell death [GO:0010942]; positive regulation of cell size [GO:0045793]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA binding [GO:0043388]; positive regulation of glycoprotein biosynthetic process [GO:0010560]; positive regulation of histone acetylation [GO:0035066]; positive regulation of muscle atrophy [GO:0014737]; positive regulation of protein binding [GO:0032092]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein secretion [GO:0050714]; positive regulation of proteolysis [GO:0045862]; positive regulation of sarcomere organization [GO:0060298]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response [GO:0006990]; positive regulation of translation [GO:0045727]; positive regulation of type I interferon production [GO:0032481]; protein acetylation [GO:0006473]; protein-DNA complex assembly [GO:0065004]; protein kinase B signaling [GO:0043491]; protein stabilization [GO:0050821]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of angiotensin metabolic< process [GO:0060177]; regulation of cell cycle [GO:0051726]; regulation of cellular response to heat [GO:1900034]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of tubulin deacetylation [GO:0090043]; response to calcium ion [GO:0051592]; response to cobalt ion [GO:0032025]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to hypoxia [GO:0001666]; response to tumor necrosis factor [GO:0034612]; skeletal muscle tissue development [GO:0007519]; somitogenesis [GO:0001756]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]acetyltransferase activity [GO:0016407]; activating transcription factor binding [GO:0033613]; androgen receptor binding [GO:0050681]; antigen binding [GO:0003823]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; core promoter binding [GO:0001047]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; histone acetyltransferase activity [GO:0004402]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468]; nuclear hormone receptor binding [GO:0035257]; pre-mRNA intronic binding [GO:0097157]; protein C-terminus binding [GO:0008022]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; transferase activity, transferring acyl groups [GO:0016746]; zinc ion binding [GO:0008270]chromatin [GO:0000785]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription factor complex [GO:0005667] FUNCTION: Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:10733570, PubMed:11430825, PubMed:11701890, PubMed:12402037, PubMed:12586840, PubMed:12929931, PubMed:14645221, PubMed:15186775, PubMed:15890677, PubMed:16617102, PubMed:16762839, PubMed:18722353, PubMed:18995842, PubMed:23415232, PubMed:23911289, PubMed:23934153, PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D. {ECO:0000269|PubMed:10733570, ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12586840, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15890677, ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:18722353, ECO:0000269|PubMed:18995842, ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23415232, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:23934153, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:8945521, ECO:0000305|PubMed:20955178}.O14657TOR1B Torsin-1BSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}.chaperone mediated protein folding requiring cofactor [GO:0051085]; endoplasmic reticulum organization [GO:0007029]; nuclear membrane organization [GO:0071763]; protein homooligomerization [GO:0051260]; response to unfolded protein [GO:0006986]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]EFUNCTION: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. {ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647}.Q15773MLF2Myeloid leukemia factor 2defense response [GO:0006952]Q9Y6I9TX264%Testis-expressed sequence 264 proteinQ70HW3SAMC2S-adenosylmethionine mitochondrial carrier proteinSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14674884}; Multi-pass membrane protein {ECO:0000269|PubMed:14674884}.lS-adenosyl-L-methionine transmembrane transport [GO:1901962]; S-adenosyl-L-methionine transport [GO:0015805]GS-adenosyl-L-methionine transmembrane transporter activity [GO:0000095]FUNCTION: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Specifically mediates the transport of S-adenosylmethionine (SAM) into the mitochondria. {ECO:0000269|PubMed:14674884}.P35556FBN2 Fibrillin-2bone trabecula formation [GO:0060346]; camera-type eye development [GO:0043010]; embryonic eye morphogenesis [GO:0048048]; embryonic limb morphogenesis [GO:0030326]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; positive regulation of bone mineralization [GO:0030501]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of cellular response to growth factor stimulus [GO:0090287]; sequestering of TGFbeta in extracellular matrix [GO:0035583]ecalcium ion binding [GO:0005509]; extracellular matrix constituent conferring elasticity [GO:0030023]^extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; microfibril [GO:0001527]FUNCTION: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TG< F-beta and BMP levels, respectively (By similarity). {ECO:0000250|UniProtKB:Q61555}.O94905ERLN2Erlin-2_SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.%cholesterol metabolic process [GO:0008203]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of fatty acid biosynthetic process [GO:0045717]; SREBP signaling pathway [GO:0032933]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:19240031, PubMed:17502376). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:24217618}.P18031PTN10Tyrosine-protein phosphatase non-receptor type 1BSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}; Peripheral membrane protein {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}; Cytoplasmic side {ECO:0000269|PubMed:1739967, ECO:0000269|PubMed:21135139}. Note=Interacts with EPHA3 at the cell membrane.actin cytoskeleton reorganization [GO:0031532]; activation of JUN kinase activity [GO:0007257]; activation of signaling protein activity involved in unfolded protein response [GO:0006987]; blood coagulation [GO:0007596]; cytokine-mediated signaling pathway [GO:0019221]; endoplasmic reticulum unfolded protein response [GO:0030968]; insulin receptor signaling pathway [GO:0008286]; interferon-gamma-mediated signaling pathway [GO:0060333]; IRE1-mediated unfolded protein response [GO:0036498]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; peptidyl-tyrosine dephosphorylation [GO:0035335]; peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [GO:1990264]; platelet activation [GO:0030168]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of receptor catabolic process [GO:2000646]; protein dephosphorylation [GO:0006470]; regulation of endocytosis [GO:0030100]; regulation of hepatocyte growth factor receptor signaling pathway [GO:1902202]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of intracellular protein transport [GO:0033157]; regulation of signal transduction [GO:0009966]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; type I interferon signaling pathway [GO:0060337] enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; receptor tyrosine kinase binding [GO:0030971]; zinc ion binding [GO:0008270]cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; sorting endosome [GO:0097443]bFUNCTION: Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET. {ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:21135139, ECO:0000269|PubMed:22169477}.P00387NB5R3NADH-cytochrome b5 reductase 3SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Produces the soluble form found in erythrocytes. blood circulation [GO:0008015]; cholesterol biosynthetic process [GO:0006695]; L-ascorbic acid metabolic process [GO:0019852]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ADP binding [GO:0043531]; AMP binding [GO:0016208]; cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; NAD binding [GO:0051287]Rcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; hemoglobin complex [GO:0005833]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]FUNCTION: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.Q96AJ9VTI1A>Vesicle transport through interaction with t-SNAREs homolog 1ASUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:19138172}. Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.zER to Golgi vesicle-mediated transport [GO:0006888]; Golgi ribbon formation [GO:0090161]; Golgi to vacuole transport [GO:0006896]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein targeting to vacuole [GO:0006623]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion with Golgi apparatus [GO:0048280]; voluntary musculoskeletal movement [GO:0050882]?SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]clathrin-coated vesicle [GO:0030136]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; neuronal cell body [GO:0043025]; neuron projection terminus [GO:0044306]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]aFUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be involved in increased cytokine secretion associated with cellular senescence. {ECO:0000269|PubMed:18195106, ECO:0000269|PubMed:1913< 8172}.Q8N4H5TOM52Mitochondrial import receptor subunit TOM5 homologSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18331822}; Single-pass membrane protein {ECO:0000269|PubMed:18331822}.`cellular protein metabolic process [GO:0044267]; protein targeting to mitochondrion [GO:0006626]integral component of membrane [GO:0016021]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]Q658P3STEA3Metalloreductase STEAP3p53Exosome mediated secretionSUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to vesicular-like structures at the plasma membrane and around the nucleus.yapoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular iron ion homeostasis [GO:0006879]; copper ion import [GO:0015677]; ferric iron import into cell [GO:0097461]; oxidation-reduction process [GO:0055114]; positive regulation of apoptotic process [GO:0043065]; protein secretion [GO:0009306]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]~cupric reductase activity [GO:0008823]; ferric-chelate reductase (NADPH) activity [GO:0052851]; metal ion binding [GO:0046872]tendosome membrane [GO:0010008]; integral component of plasma membrane [GO:0005887]; multivesicular body [GO:0005771]%FUNCTION: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP. {ECO:0000269|PubMed:15319436, ECO:0000269|PubMed:16651434}.Q9NR28DBLOHDiablo homolog, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14523016}. Note=Released into the cytosol when cells undergo apoptosis.Eactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic process [GO:0006915]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; neuron apoptotic process [GO:0051402]; positive regulation of apoptotic process [GO:0043065]; programmed cell death [GO:0012501]CD40 receptor complex [GO:0035631]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]FUNCTION: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance. {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:14523016, ECO:0000269|PubMed:15200957}.P30405PPIF4Peptidyl-prolyl cis-trans isomerase F, mitochondrialCyp-DISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10406942}.~apoptotic mitochondrial changes [GO:0008637]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to calcium ion [GO:0071277]; cellular response to hydrogen peroxide [GO:0070301]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of ATPase activity [GO:0032780]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of oxidative phosphorylation [GO:0090324]; negative regulation of oxidative phosphorylation uncoupler activity [GO:2000276]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane permeability involved in programmed necrotic cell death [GO:1902445]; regulation of necrotic cell death [GO:0010939]; regulation of proton-transporting ATPase activity, rotational mechanism [GO:0010849]; response to ischemia [GO:0002931]membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis. {ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:22726440}.Q6UB35C1TM:Monofunctional C1-tetrahydrofolate synthase, mitochondrial One-carbon metabolismBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12937168}.embryonic neurocranium morphogenesis [GO:0048702]; embryonic viscerocranium morphogenesis [GO:0048703]; folic acid-containing compound biosynthetic process [GO:0009396]; folic acid-containing compound metabolic process [GO:0006760]; formate metabolic process [GO:0015942]; neural tube closure [GO:0001843]; one-carbon metabolic process [GO:0006730]; oxidation-reduction process [GO:0055114]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653]ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; protein homodimerization activity [GO:0042803]1membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2. {ECO:0000250}.Q9BQB6VKOR1-Vitamin K epoxide reductase complex subunit 1vSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}; Multi-pass membrane protein {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:15716279, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}.blood coagulation [GO:0007596]; bone development [GO:0060348]; cellular protein metabolic process [GO:0044267]; drug metabolic process [GO:0017144]; peptidyl-glutamic acid carboxylation [GO:0017187]; post-translational protein modification [GO:0043687]; regulation of blood coagulation [GO:0030193]; response to antibiotic [GO:0046677]; response to organic cyclic compound [GO:0014070]; response to organonitrogen compound [GO:0010243]; vitamin K metabolic process [GO:0042373]quinone binding [GO:0048038]; vitamin-K-epoxide reductase (warfarin-insensitive) activity [GO:0047058]; vitamin-K-epoxide reductase (warfarin-sensitive) activity [GO:0047057]FUNCTION: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxid< e reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development. {ECO:0000269|PubMed:14765194, ECO:0000269|PubMed:14765195, ECO:0000269|PubMed:15879509, ECO:0000269|PubMed:16270630, ECO:0000269|PubMed:20978134, ECO:0000269|PubMed:22923610}.Q6YN16HSDL2+Hydroxysteroid dehydrogenase-like protein 2?SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19703561}.Jmembrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]ZFUNCTION: Has apparently no steroid dehydrogenase activity. {ECO:0000269|PubMed:19703561}.O14735CDIPT6CDP-diacylglycerol--inositol 3-phosphatidyltransferase0SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:8110188}.CDP-diacylglycerol metabolic process [GO:0046341]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]alcohol binding [GO:0043178]; carbohydrate binding [GO:0030246]; CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity [GO:0003881]; diacylglycerol binding [GO:0019992]; manganese ion binding [GO:0030145]endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]UFUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme. {ECO:0000269|PubMed:8110188}.Q02978M2OM3Mitochondrial 2-oxoglutarate/malate carrier proteinalpha-ketoglutarate transport [GO:0015742]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]Voxoglutarate:malate antiporter activity [GO:0015367]; poly(A) RNA binding [GO:0044822]integral component of plasma membrane [GO:0005887]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]gFUNCTION: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism.P09914IFIT1;Interferon-induced protein with tetratricopeptide repeats 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:21642987}.cellular response to exogenous dsRNA [GO:0071360]; cellular response to type I interferon [GO:0071357]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; intracellular transport of viral protein in host cell [GO:0019060]; negative regulation of defense response to virus by host [GO:0050689]; negative regulation of helicase activity [GO:0051097]; negative regulation of protein binding [GO:0032091]; negative regulation of viral genome replication [GO:0045071]; positive regulation of viral genome replication [GO:0045070]; response to virus [GO:0009615]; type I interferon signaling pathway [GO:0060337]Dcytoplasm [GO:0005737]; cytosol [GO:0005829]; host cell [GO:0043657]FUNCTION: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses. {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420}.Q4G0N4NAKD2NAD kinase 2, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23212377}.JNAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741]kATP binding [GO:0005524]; NAD+ kinase activity [GO:0003951]; protein homodimerization activity [GO:0042803]PFUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo. {ECO:0000269|PubMed:23212377}.Q8NE86MCU(Calcium uniporter protein, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:24231807}; Multi-pass membrane protein {ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:24231807}.ocalcium ion transmembrane import into mitochondrion [GO:0036444]; calcium-mediated signaling [GO:0019722]; glucose homeostasis [GO:0042593]; mitochondrial calcium ion transport [GO:0006851]; positive regulation of insulin secretion [GO:0032024]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; protein complex oligomerization [GO:0035786]Fcalcium channel activity [GO:0005262]; uniporter activity [GO:0015292]calcium channel complex [GO:0034704]; integral component of mitochondrial inner membrane [GO:0031305]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; uniplex complex [GO:1990246]AFUNCTION: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Activity is regulated by MICU1 and MICU2 that stimulate and inhibit MCU activity, respectively. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes. {ECO:0000269|PubMed:21685886, ECO:0000269|PubMed:21685888, ECO:0000269|PubMed:22822213, ECO:0000269|PubMed:22829870, ECO:0000269|PubMed:22904319, ECO:0000269|PubMed:23101630, ECO:0000269|PubMed:23178883, ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24560927}.Q8WWX9SELMSelenoprotein MSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]xFUNCTION: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation. {ECO:0000250}.Q9HD45TM9S3$Transmembrane 9 superfamily member 3Q9NVH1DJC11"DnaJ homolog subfamily C member 11BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25997101}.P319373HIDH13-hydroxyisobutyrate dehydrogenase, mitochondrial< 3-hydroxyisobutyrate dehydrogenase activity [GO:0008442]; NAD binding [GO:0051287]; phosphogluconate dehydrogenase (decarboxylating) activity [GO:0004616]Q9H6B4CLMPCXADR-like membrane proteinSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:22155368}. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.(digestive tract development [GO:0048565]bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; cytoplasmic microtubule [GO:0005881]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886] FUNCTION: May be involved in the cell-cell adhesion. May play a role in adipocyte differentiation and development of obesity. Is required for normal small intestine development. {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:15563274, ECO:0000269|PubMed:22155368}.P11177ODPB?Pyruvate dehydrogenase E1 component subunit beta, mitochondrialTacetyl-CoA biosynthetic process from pyruvate [GO:0006086]; cellular metabolic process [GO:0044237]; glucose metabolic process [GO:0006006]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]ppyruvate dehydrogenase (acetyl-transferring) activity [GO:0004739]; pyruvate dehydrogenase activity [GO:0004738]extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pyruvate dehydrogenase complex [GO:0045254]FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.Q5JTJ3COA6.Cytochrome c oxidase assembly factor 6 homologLcytochrome-c oxidase activity [GO:0004129]; poly(A) RNA binding [GO:0044822]Q9NNW7TRXR2&Thioredoxin reductase 2, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10215850}.~cell redox homeostasis [GO:0045454]; response to oxygen radical [GO:0000305]; response to reactive oxygen species [GO:0000302]gflavin adenine dinucleotide binding [GO:0050660]; thioredoxin-disulfide reductase activity [GO:0004791]FUNCTION: Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.P53007TXTP/Tricarboxylate transport protein, mitochondrial\carbohydrate metabolic process [GO:0005975]; cellular lipid metabolic process [GO:0044255]; citrate transport [GO:0015746]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]7citrate transmembrane transporter activity [GO:0015137]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]FUNCTION: Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway.P12757SKILSki-like proteinblastocyst formation [GO:0001825]; cell cycle arrest [GO:0007050]; gene expression [GO:0010467]; lens fiber cell differentiation [GO:0070306]; lymphocyte homeostasis [GO:0002260]; negative regulation of cell differentiation [GO:0045596]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of axonogenesis [GO:0050772]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902231]; protein heterotrimerization [GO:0070208]; protein homotrimerization [GO:0070207]; regulation of apoptotic process [GO:0042981]; response to antibiotic [GO:0046677]; response to cytokine [GO:0034097]; response to growth factor [GO:0070848]; skeletal muscle tissue development [GO:0007519]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]chromatin binding [GO:0003682]; protein complex binding [GO:0032403]; protein domain specific binding [GO:0019904]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; SMAD binding [GO:0046332]; transcription corepressor activity [GO:0003714]acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; protein complex [GO:0043234]lFUNCTION: May have regulatory role in cell division or differentiation in response to extracellular signals.Q9NU23LYRM2LYR motif-containing protein 2Q14165MLECMalectincellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]>carbohydrate binding [GO:0030246]; enzyme binding [GO:0019899]FUNCTION: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity). {ECO:0000250}.P42765THIM&3-ketoacyl-CoA thiolase, mitochondrialsSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18371312}. Note=Colocalizes with BNIP3 in the mitochondria.ecellular response to hypoxia [GO:0071456]; cholesterol biosynthetic process [GO:0006695]; fatty acid metabolic process [GO:0006631]; negative regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902109]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]Tacetyl-CoA C-acyltransferase activity [GO:0003988]; poly(A) RNA binding [GO:0044822]eFUNCTION: Abolishes BNIP3-mediated apoptosis and mitochondrial damage. {ECO:0000269|PubMed:18371312}.Q9Y3B3TMED7/Transmembrane emp24 domain-containing protein 7<SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway.COPII vesicle coat [GO:0030127]; COPI vesicle coat [GO:0030126]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Appears to play a role in the biosynthesis of secreted cargo including processing and post-translational modifications.O60674JAK2Tyrosine-protein kinase JAK2SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:19783980}. Nucleus {ECO:0000269|PubMed:19783980}.actin filament polymerization [GO:0030041]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; a< ctivation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of JAK2 kinase activity [GO:0042977]; activation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to lipopolysaccharide [GO:0071222]; chromatin organization [GO:0006325]; cytokine-mediated signaling pathway [GO:0019221]; enzyme linked receptor protein signaling pathway [GO:0007167]; erythrocyte differentiation [GO:0030218]; extrinsic apoptotic signaling pathway [GO:0097191]; G-protein coupled receptor signaling pathway [GO:0007186]; growth hormone receptor signaling pathway [GO:0060396]; histone H3-Y41 phosphorylation [GO:0035409]; hormone-mediated signaling pathway [GO:0009755]; host programmed cell death induced by symbiont [GO:0034050]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; interleukin-12-mediated signaling pathway [GO:0035722]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; JAK-STAT cascade [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; mammary gland epithelium development [GO:0061180]; mesoderm development [GO:0007498]; mineralocorticoid receptor signaling pathway [GO:0031959]; movement of cell or subcellular component [GO:0006928]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cell proliferation [GO:0008285]; negative regulation of DNA binding [GO:0043392]; negative regulation of heart contraction [GO:0045822]; negative regulation of neuron apoptotic process [GO:0043524]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of cell activation [GO:0050867]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA binding [GO:0043388]; positive regulation of growth hormone receptor signaling pathway [GO:0060399]; positive regulation of inflammatory response [GO:0050729]; positive regulation of insulin secretion [GO:0032024]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of Stat3 protein [GO:0042517]; positive regulation of tyrosine phosphorylation of Stat5 protein [GO:0042523]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of cell proliferation [GO:0042127]; regulation of inflammatory response [GO:0050727]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; response to antibiotic [GO:0046677]; response to hydroperoxide [GO:0033194]; response to interleukin-12 [GO:0070671]; response to lipopolysaccharide [GO:0032496]; response to tumor necrosis factor [GO:0034612]; signal transduction [GO:0007165]; STAT protein import into nucleus [GO:0007262]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; tyrosine phosphorylation of Stat1 protein [GO:0042508]; tyrosine phosphorylation of Stat3 protein [GO:0042503]; tyrosine phosphorylation of Stat5 protein [GO:0042506]; tyrosine phosphorylation of STAT protein [GO:0007260]ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; heme binding [GO:0020037]; histone binding [GO:0042393]; histone kinase activity (H3-Y41 specific) [GO:0035401]; interleukin-12 receptor binding [GO:0005143]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; SH2 domain binding [GO:0042169],caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome lumen [GO:0031904]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane raft [GO:0045121]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:19783980, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21423214}.P30042ES1"ES1 protein homolog, mitochondrialP08648ITA5Integrin alpha-5angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-substrate adhesion [GO:0031589]; cell-substrate junction assembly [GO:0007044]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; memory [GO:0007613]; negative regulation of anoikis [GO:2000811]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; viral process [GO:0016032]; wound healing, spread< ing of epidermal cells [GO:0035313]metal ion binding [GO:0046872]; platelet-derived growth factor receptor binding [GO:0005161]; vascular endothelial growth factor receptor 2 binding [GO:0043184]ialphav-beta3 integrin-vitronectin complex [GO:0071062]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; synapse [GO:0045202] FUNCTION: Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.Q9NX63MIC19MICOS complex subunit MIC19LSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9CRB9}; Lipid-anchor {ECO:0000250|UniProtKB:Q9CRB9}; Intermembrane side {ECO:0000250|UniProtKB:Q9CRB9}. Cytoplasm {ECO:0000269|PubMed:22567091}. Nucleus {ECO:0000269|PubMed:22567091}. Mitochondrion {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.cristae formation [GO:0042407]; inner mitochondrial membrane organization [GO:0007007]; mitochondrial fusion [GO:0008053]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]phosphatase binding [GO:0019902]; protein complex scaffold [GO:0032947]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; MICOS complex [GO:0061617]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]8FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:25781180). {ECO:0000269|PubMed:22567091, ECO:0000269|PubMed:25781180}.P09622DLDH*Dihydrolipoyl dehydrogenase, mitochondrialQ2-oxoglutarate metabolic process [GO:0006103]; acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; aging [GO:0007568]; branched-chain amino acid catabolic process [GO:0009083]; cell redox homeostasis [GO:0045454]; cellular metabolic process [GO:0044237]; cellular nitrogen compound metabolic process [GO:0034641]; dihydrolipoamide metabolic process [GO:0051068]; gastrulation [GO:0007369]; lipoate metabolic process [GO:0009106]; lysine catabolic process [GO:0006554]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proteolysis [GO:0006508]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; regulation of membrane potential [GO:0042391]; small molecule metabolic process [GO:0044281]; sperm capacitation [GO:0048240]; tricarboxylic acid cycle [GO:0006099]dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660]; lipoamide binding [GO:0043544]; NAD binding [GO:0051287]acrosomal matrix [GO:0043159]; cilium [GO:0005929]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; oxoglutarate dehydrogenase complex [GO:0045252]; pyruvate dehydrogenase complex [GO:0045254]FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.Q9P291ARMX1.Armadillo repeat-containing X-linked protein 1P30084ECHM"Enoyl-CoA hydratase, mitochondrial)enoyl-CoA hydratase activity [GO:0004300]aextracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.O75844FACE1CAAX prenyl protease 1 homologSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}.CAAX-box protein processing [GO:0071586]; nuclear envelope organization [GO:0006998]; prenylated protein catabolic process [GO:0030327]; proteolysis [GO:0006508]umetal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metalloexopeptidase activity [GO:0008235]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]lFUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C.Q9ULX7CAH14Carbonic anhydrase 14Nitrogen metabolisQbicarbonate transport [GO:0015701]; small molecule metabolic process [GO:0044281]Kcarbonate dehydratase activity [GO:0004089]; metal ion binding [GO:0046872]Iintegral component of membrane [GO:0016021]; plasma membrane [GO:0005886]1FUNCTION: Reversible hydration of carbon dioxide.P01137TGFB1!Transforming growth factor beta-1ligandhSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17827158}.!"active induction of host immune response by virus [GO:0046732]; adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains [GO:0002460]; aging [GO:0007568]; ATP biosynthetic process [GO:0006754]; blood coagulation [GO:0007596]; branch elongation involved in mammary gland duct branching [GO:0060751]; cell-cell junction organization [GO:0045216]; cell cycle arrest [GO:0007050]; cell development [GO:0048468]; cell growth [GO:0016049]; cellular calcium ion homeostasis [GO:0006874]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to organic cyclic compound [GO:0071407]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; common-partner SMAD protein phosphorylation [GO:0007182]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; defense response to fungus, incompatible interaction [GO:0009817]; digestive tract development [GO:0048565]; endoderm development [GO:0007492]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial to mesenchymal transition [GO:0001837]; evasion or tolerance of host defenses by virus [GO:0019049]; extracellular matrix assembly [GO:0085029]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway [GO:0097191]; face morphogenesis [GO:0060325]; female pregnancy [GO:0007565]; frontal suture morphogenesis [GO:0060364]; germ cell migration [GO:0008354]; hematopoietic progenitor cell differentiation [GO:0002244]; hyaluronan catabolic process [GO:0030214]; inflammatory response [GO:0006954]; inner ear development [GO:0048839]; lens fiber cell differentiation [GO:0070306]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; lymph node development [GO:0048535]; macrophage derived foam cell differentiation [GO:0010742]; mammary gland branching involved in thelarche [GO:0060744]; MAPK cascade [GO:0000165]; mitotic cell cycle checkpoint [GO:0007093]; modulation by virus of host morphology or physiology [GO:0019048]; mononuclear cell proliferation [GO:0032943]; myelination [GO:0042552]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-cell adhesion [GO:0022< 408]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell differentiation [GO:0045596]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of DNA replication [GO:0008156]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of gene silencing by miRNA [GO:0060965]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of ossification [GO:0030279]; negative regulation of phagocytosis [GO:0050765]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of release of sequestered calcium ion into cytosol [GO:0051280]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; oligodendrocyte development [GO:0014003]; organ regeneration [GO:0031100]; ossification involved in bone remodeling [GO:0043932]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; phosphate-containing compound metabolic process [GO:0006796]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of bone mineralization [GO:0030501]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of gene expression [GO:0010628]; positive regulation of histone acetylation [GO:0035066]; positive regulation of histone deacetylation [GO:0031065]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NAD+ ADP-ribosyltransferase activity [GO:1901666]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of odontogenesis [GO:0042482]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of protein complex assembly [GO:0031334]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein secretion [GO:0050714]; positive regulation of SMAD protein import into nucleus [GO:0060391]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; positive regulation of vascular endothelial growth factor production [GO:0010575]; protein export from nucleus [GO:0006611]; protein import into nucleus, translocation [GO:0000060]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; receptor catabolic process [GO:0032801]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of apoptotic process [GO:0042981]; regulation of binding [GO:0051098]; regulation of blood vessel remodeling [GO:0060312]; regulation of branching involved in mammary gland duct morphogenesis [GO:0060762]; regulation of cartilage development [GO:0061035]; regulation of cell migration [GO:0030334]; regulation of DNA binding [GO:0051101]; regulation of interleukin-23 production [GO:0032667]; regulation of protein import into nucleus [GO:0042306]; regulation of sodium ion transport [GO:0002028]; regulation of striated muscle tissue development [GO:0016202]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulatory T cell differentiation [GO:0045066]; response to cholesterol [GO:0070723]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to laminar fluid shear stress [GO:0034616]; response to progesterone [GO:0032570]; response to radiation [GO:0009314]; response to vitamin D [GO:0033280]; response to wounding [GO:0009611]; salivary gland morphogenesis [GO:0007435]; SMAD protein complex assembly [GO:0007183]; SMAD protein import into nucleus [GO:0007184]; SMAD protein signal transduction [GO:0060395]; T cell homeostasis [GO:0043029]; tolerance induction to self antigen [GO:0002513]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; viral life cycle [GO:0019058]Qantigen binding [GO:0003823]; cytokine activity [GO:0005125]; enzyme binding [GO:0019899]; glycoprotein binding [GO:0001948]; type III transforming growth factor beta receptor binding [GO:0034714]; type II transforming growth factor beta receptor binding [GO:0005114]; type I transforming growth factor beta receptor binding [GO:0034713]vaxon [GO:0030424]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; proteinaceous extracellular matrix [GO:0005578]zFUNCTION: Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells. {ECO:0000250|UniProtKB:P04202}.P11234RALBRas-related protein Ral-B,SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}; Lipid-anchor {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}; Cytoplasmic side {ECO:0< 000269|PubMed:17875936, ECO:0000269|PubMed:18756269}. Note=During late cytokinesis localizes at the midbody.apoptotic process [GO:0006915]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to starvation [GO:0009267]; cytokinesis [GO:0000910]; negative regulation of protein binding [GO:0032091]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of protein binding [GO:0032092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; Ras protein signal transduction [GO:0007265]; regulation of exocyst assembly [GO:0001928]; regulation of exocyst localization [GO:0060178]; signal transduction [GO:0007165]ATPase binding [GO:0051117]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; ubiquitin protein ligase binding [GO:0031625]rextracellular exosome [GO:0070062]; intracellular [GO:0005622]; midbody [GO:0030496]; plasma membrane [GO:0005886]FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. {ECO:0000269|PubMed:18756269}.Q02083NAAA+N-acylethanolamine-hydrolyzing acid amidaseZSUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:10610717, ECO:0000305|PubMed:15655246}.}hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; transcription factor binding [GO:0008134]Qcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine. {ECO:0000269|PubMed:15655246}.Q9Y2Q3GSTK1!Glutathione S-transferase kappa 1?SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14742434}.epithelial cell differentiation [GO:0030855]; glutathione metabolic process [GO:0006749]; oxidation-reduction process [GO:0055114]glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; protein disulfide oxidoreductase activity [GO:0015035]; receptor binding [GO:0005102]extracellular exosome [GO:0070062]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; peroxisome [GO:0005777]FUNCTION: Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).O95477ABCA1*ATP-binding cassette sub-family A member 1Fat digestion and absorptionSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522}; Multi-pass membrane protein {ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522}.apolipoprotein A-I-mediated signaling pathway [GO:0038027]; cellular lipid metabolic process [GO:0044255]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to retinoic acid [GO:0071300]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; endosomal transport [GO:0016197]; G-protein coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle assembly [GO:0034380]; interleukin-1 beta secretion [GO:0050702]; intracellular cholesterol transport [GO:0032367]; lipoprotein metabolic process [GO:0042157]; lysosome organization [GO:0007040]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; peptide secretion [GO:0002790]; phagocytosis, engulfment [GO:0006911]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; phospholipid translocation [GO:0045332]; platelet dense granule organization [GO:0060155]; positive regulation of cAMP biosynthetic process [GO:0030819]; positive regulation of cholesterol efflux [GO:0010875]; protein lipidation [GO:0006497]; regulation of Cdc42 protein signal transduction [GO:0032489]; response to laminar fluid shear stress [GO:0034616]; response to low-density lipoprotein particle [GO:0055098]; reverse cholesterol transport [GO:0043691]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]Aanion transmembrane transporter activity [GO:0008509]; apolipoprotein A-I binding [GO:0034186]; apolipoprotein A-I receptor activity [GO:0034188]; apolipoprotein binding [GO:0034185]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATPase binding [GO:0051117]; ATP binding [GO:0005524]; cholesterol binding [GO:0015485]; cholesterol transporter activity [GO:0017127]; phospholipid binding [GO:0005543]; phospholipid transporter activity [GO:0005548]; receptor binding [GO:0005102]; small GTPase binding [GO:0031267]; syntaxin binding [GO:0019905](endocytic vesicle [GO:0030139]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport.P45880VDAC23Voltage-dependent anion-selective channel protein 2PSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:7539795}.anion transport [GO:0006820]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of protein polymerization [GO:0032272]; regulation of anion transmembrane transport [GO:1903959]onucleotide binding [GO:0000166]; porin activity [GO:0015288]; voltage-gated anion channel activity [GO:0008308]"extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; pore complex [GO:0046930]TFUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective.Q5T9L3WLSProtein wntless homolog Ligands(20)SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein {ECO:0000269|PubMed:16678095}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16678095}; Multi-pass membrane protein {ECO:0000269|PubMed:16678095}.anterior/posterior axis specification [GO:0009948]; mesoderm formation [GO:0001707]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; Wnt signaling pathway [GO:0016055]cytoplasmic vesicle membrane [GO:0030659]; dendrite cytoplasm [GO:0032839]; dendrite membrane [GO:0032590]; early endosome membrane [GO:0031901]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction pl< ays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity). {ECO:0000250}.O60216RAD210Double-strand-break repair protein rad21 homologMSUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by separase/ESPL1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Once cleaved by caspase-3, the C-terminal 64 kDa cleavage product translocates to the cytoplasm, where it may trigger apoptosis."apoptotic process [GO:0006915]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; chromosome segregation [GO:0007059]; DNA recombination [GO:0006310]; double-strand break repair [GO:0006302]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; post-translational protein modification [GO:0043687]; protein localization to chromatin [GO:0071168]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131]; regulation of transcription from RNA polymerase II promoter [GO:0006357]RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear meiotic cohesin complex [GO:0034991]; nucleoplasm [GO:0005654]uFUNCTION: Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway. {ECO:0000269|PubMed:11875078, ECO:0000269|PubMed:12417729}.O14495LPP3"Lipid phosphate phosphohydrolase 3SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.Bergmann glial cell differentiation [GO:0060020]; blood vessel development [GO:0001568]; canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion [GO:0044329]; canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration [GO:0044328]; canonical Wnt signaling pathway involved in positive regulation of wound healing [GO:0044330]; dephosphorylation [GO:0016311]; gastrulation with mouth forming second [GO:0001702]; germ cell migration [GO:0008354]; homotypic cell-cell adhesion [GO:0034109]; lipid metabolic process [GO:0006629]; negative regulation of protein phosphorylation [GO:0001933]; phospholipid metabolic process [GO:0006644]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein stabilization [GO:0050821]; regulation of sphingolipid mediated signaling pathway [GO:1902068]; regulation of Wnt signaling pathway [GO:0030111]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]lipid phosphatase activity [GO:0042577]; phosphatidate phosphatase activity [GO:0008195]; phosphoprotein phosphatase activity [GO:0004721]; sphingosine-1-phosphate phosphatase activity [GO:0042392]adherens junction [GO:0005912]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]LFUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.O95967FBLN4:EGF-containing fibulin-like extracellular matrix protein 2.extracellular matrix organization [GO:0030198]Zcalcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]Q15155NOMO1Nodal modulator 18FUNCTION: May antagonize Nodal signaling. {ECO:0000250}.Q96BQ5CC127)Coiled-coil domain-containing protein 127Q9H4K7MTG2*Mitochondrial ribosome-associated GTPase 2lSUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.regulation of mitochondrial translation [GO:0070129]; regulation of respiratory system process [GO:0044065]; ribosome biogenesis [GO:0042254]qmitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial ribosome [GO:0005761]FUNCTION: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays GTPase activity. Involved in the ribosome maturation process. {ECO:0000269|PubMed:17054726, ECO:0000269|PubMed:23396448}.P17152TMM11'Transmembrane protein 11, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21274005}; Multi-pass membrane protein {ECO:0000269|PubMed:21274005}.'mitochondrion organization [GO:0007005]sintegral component of mitochondrial inner membrane [GO:0031305]; integral component of plasma membrane [GO:0005887]UFUNCTION: Plays a role in mitochondrial morphogenesis. {ECO:0000269|PubMed:21274005}.Q8N684CPSF79Cleavage and polyadenylation specificity factor subunit 7<SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20695905}.(gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; protein tetramerization [GO:0051262]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]pmembrane [GO:0016020]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Binds to cleavage and polyadenylation RNA substrates. {ECO:0000269|PubMed:8626397}.Q9NZV5SELNSelenoprotein NqSUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane {ECO:0000305}. Note=Probably membrane-associated.Ocellular response to caffeine [GO:0071313]; cellular response to oxidative stress [GO:0034599]; lung alveolus development [GO:0048286]; mitochondrion organization [GO:0007005]; multicellular organismal response to stress [GO:0033555]; positive regulation of skeletal muscle cell proliferation [GO:0014858]; respiratory system process [GO:0003016]; response to muscle activity involved in regulation of muscle adaptation [GO:0014873]; skeletal muscle fiber development [GO:0048741]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle tissue regeneration [GO:0043403]+endoplasmic reticulum membrane [GO:0005789]Q15363TMED2/Transmembrane emp24 domain-containing protein 2:SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane< ; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Note=Cycles between compartments of the early secretatory pathway.cargo loading into vesicle [GO:0035459]; COPI coating of Golgi vesicle [GO:0048205]; COPII vesicle coating [GO:0048208]; embryonic morphogenesis [GO:0048598]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; labyrinthine layer blood vessel development [GO:0060716]; maternal placenta development [GO:0001893]; negative regulation of GTPase activity [GO:0034260]; protein targeting to plasma membrane [GO:0072661]COPI-coated vesicle [GO:0030137]; COPI-coated vesicle membrane [GO:0030663]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; zymogen granule membrane [GO:0042589]FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing. {ECO:0000269|PubMed:10761932, ECO:0000269|PubMed:17693410, ECO:0000269|PubMed:20361938, ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.Q9H7F0AT133(Probable cation-transporting ATPase 13A3Q04837SSBP2Single-stranded DNA-binding protein, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18063578}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18063578}.DNA replication [GO:0006260]; mitochondrion morphogenesis [GO:0070584]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; positive regulation of helicase activity [GO:0051096]jchromatin binding [GO:0003682]; poly(A) RNA binding [GO:0044822]; single-stranded DNA binding [GO:0003697]extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA.O95202LETM1<LETM1 and EF-hand domain-containing protein 1, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14706454, ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:18628306}; Single-pass membrane protein {ECO:0000269|PubMed:14706454, ECO:0000269|PubMed:15138253, ECO:0000269|PubMed:18628306}.cristae formation [GO:0042407]FUNCTION: Crucial for the maintenance of mitochondrial tubular networks and for the assembly of the supercomplexes of the respiratory chain. Required for the maintenance of the tubular shape and cristae organization. {ECO:0000269|PubMed:18628306}.P49755TMEDA0Transmembrane emp24 domain-containing protein 10SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Melanosome. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Cycles between compartments of the early secretatory pathway.gcargo loading into vesicle [GO:0035459]; COPI-coated vesicle budding [GO:0035964]; COPI coating of Golgi vesicle [GO:0048205]; COPII vesicle coating [GO:0048208]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; kidney development [GO:0001822]; protein oligomerization [GO:0051259]; regulated secretory pathway [GO:0045055]; regulation of beta-amyloid formation [GO:1902003]; response to alkaloid [GO:0043279]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; vesicle targeting, to, from or within Golgi [GO:0048199]cis-Golgi network [GO:0005801]; COPI-coated vesicle [GO:0030137]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; gamma-secretase complex [GO:0070765]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; melanosome [GO:0042470]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; trans-Golgi network transport vesicle [GO:0030140]; transport vesicle membrane [GO:0030658]; zymogen granule membrane [GO:0042589]FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus. {ECO:0000250, ECO:000026< 9|PubMed:10052452, ECO:0000269|PubMed:11726511, ECO:0000269|PubMed:16641999, ECO:0000269|PubMed:17288597, ECO:0000269|PubMed:19296914, ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.Q13219PAPP1 Pappalysin-1=SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077652}.qcell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; female pregnancy [GO:0007565]qmetalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]8extracellular region [GO:0005576]; membrane [GO:0016020]VFUNCTION: Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF. {ECO:0000269|PubMed:10077652, ECO:0000269|PubMed:10913121, ECO:0000269|PubMed:11522292}.Q15738NSDHL;Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14506130}; Single-pass membrane protein {ECO:0000269|PubMed:14506130}. Lipid droplet {ECO:0000269|PubMed:14506130}. Note=Trafficking through the Golgi is necessary for ER membrane localization.cholesterol biosynthetic process [GO:0006695]; hair follicle development [GO:0001942]; labyrinthine layer blood vessel development [GO:0060716]; small molecule metabolic process [GO:0044281]; smoothened signaling pathway [GO:0007224]3-beta-hydroxy-delta5-steroid dehydrogenase activity [GO:0003854]; sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity [GO:0047012]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]FUNCTION: Involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis. {ECO:0000269|PubMed:14506130}.O94826TOM70+Mitochondrial import receptor subunit TOM70cellular protein metabolic process [GO:0044267]; protein targeting to mitochondrion [GO:0006626]; protein transmembrane transport [GO:0071806]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]fFUNCTION: Receptor that accelerates the import of all mitochondrial precursor proteins. {ECO:0000250}.Q9H0V9LMA2LVIP36-like proteinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Predominantly found in the endoplasmic reticulum. Partly found in the Golgi.qER to Golgi vesicle-mediated transport [GO:0006888]; protein folding [GO:0006457]; protein transport [GO:0015031]<mannose binding [GO:0005537]; metal ion binding [GO:0046872]endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle [GO:0030134]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53. {ECO:0000269|PubMed:12878160}.Q86VU5CMTD18Catechol O-methyltransferase domain-containing protein 16FUNCTION: Putative O-methyltransferase. {ECO:0000305}.O43861ATP9B-Probable phospholipid-transporting ATPase IIBSUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.endocytosis [GO:0006897]; establishment of protein localization to Golgi [GO:0072600]; phospholipid translocation [GO:0045332]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]endosome [GO:0005768]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]Q9Y5L4TIM13=Mitochondrial import inner membrane translocase subunit Tim13SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896}; Peripheral membrane protein {ECO:0000269|PubMed:11489896}; Intermembrane side {ECO:0000269|PubMed:11489896}.cellular protein metabolic process [GO:0044267]; chaperone-mediated protein transport [GO:0072321]; protein targeting to mitochondrion [GO:0006626]; sensory perception of sound [GO:0007605]mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.O15270SPTC2Serine palmitoyltransferase 2endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]; serine C-palmitoyltransferase complex [GO:0017059]FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate. {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:20920666}.Q9H9S5FKRPFukutin-related proteinSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein. Secreted. Cell membrane, sarcolemma {ECO:0000250}. Rough endoplasmic reticulum. Note=According to some studies the N-terminal hydrophobic domain is cleaved after translocation to the Golgi apparatus and the protein is secreted. Localization at the cell membrane may require the presence of dystroglycan. At the Golgi apparatus localizes to the middle-to-trans-cisternae, as assessed by MG160 colocalization. Detected in rough endoplasmic reticulum in myocytes. In general, mutants associated with severe clinical phenotypes are retained within the endoplasmic reticulum.Lprotein O-linked mannosylation [GO:0035269]; protein processing [GO:0016485]dystrophin-associated glycoprotein complex [GO:0016010]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; rough endoplasmic reticulum [GO:0005791]; sarcolemma [GO:0042383]zFUNCTION: Transferase involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. {ECO:0000269|PubMed:25279699}.Q5C9Z4NOM1+Nucleolar MIF4G domain-containing protein 1dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15715967, ECO:0000269|PubMed:17965019}.[FUNCTION: Plays a role in targeting PPP1CA to the nucleolus. {ECO:0000269|PubMed:17965019}.Q9Y5J9TIM8B>Mitochondrial import inner membrane translocase subunit Tim8 Bextracellular space [GO:0005615]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space protein transporter complex [GO:0042719]FUNCTION: Probable mitochondrial< intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}.Q14517FAT1Protocadherin Fat 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15922730}; Single-pass type I membrane protein {ECO:0000269|PubMed:15922730}. Nucleus {ECO:0000269|PubMed:15922730}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15922730}.qactin filament organization [GO:0007015]; anatomical structure morphogenesis [GO:0009653]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cell migration [GO:0016477]; establishment or maintenance of cell polarity [GO:0007163]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; single organismal cell-cell adhesion [GO:0016337]+cell-cell junction [GO:0005911]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact. {ECO:0000250}.Q9NP64NO40Nucleolar protein of 40 kDaGSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12893261}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; positive regulation of defense response to virus by host [GO:0002230]intermediate filament cytoskeleton [GO:0045111]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]P06748NPM NucleophosminSUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Can shuttle between cytoplasm and nucleus. Co- localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis.cell aging [GO:0007569]; CENP-A containing nucleosome assembly [GO:0034080]; centrosome cycle [GO:0007098]; DNA repair [GO:0006281]; intracellular protein transport [GO:0006886]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of centrosome duplication [GO:0010826]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of protein kinase activity by regulation of protein phosphorylation [GO:0044387]; nucleocytoplasmic transport [GO:0006913]; nucleosome assembly [GO:0006334]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of translation [GO:0045727]; protein localization [GO:0008104]; protein oligomerization [GO:0051259]; regulation of centriole replication [GO:0046599]; regulation of eIF2 alpha phosphorylation by dsRNA [GO:0060735]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of endoribonuclease activity [GO:0060699]; response to stress [GO:0006950]; ribosome assembly [GO:0042255]; signal transduction [GO:0007165]; viral process [GO:0016032]histone binding [GO:0042393]; NF-kappaB binding [GO:0051059]; poly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]; ribosomal large subunit binding [GO:0043023]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; Tat protein binding [GO:0030957]; transcription coactivator activity [GO:0003713]; unfolded protein binding [GO:0051082]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; spindle pole centrosome [GO:0031616]FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. {ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061}.Q9UBM7DHCR77-dehydrocholesterol reductaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9878250}; Multi-pass membrane protein {ECO:0000269|PubMed:9878250}.blood vessel development [GO:0001568]; cell differentiation [GO:0030154]; cholesterol biosynthetic process [GO:0006695]; lung development [GO:0030324]; multicellular organism growth [GO:0035264]; post-embryonic development [GO:0009791]; regulation of cell proliferation [GO:0042127]; regulation of cholesterol biosynthetic process [GO:0045540]; small molecule metabolic process [GO:0044281]47-dehydrocholesterol reductase activity [GO:0047598]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear outer membrane [GO:0005640]fFUNCTION: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).Q9NPE2NGRNNeugrinTSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118320}. Secreted {ECO:0000305}.#neuron differentiation [GO:0030182]7extracellular region [GO:0005576]; nucleus [GO:0005634]6FUNCTION: May be involved in neuronal differentiation.Q9UG56PISD*Phosphatidylserine decarboxylase proenzymeglycerophospholipid biosynthetic process [GO:0046474]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]6phosphatidylserine decarboxylase activity [GO:0004609]Q16698DECR(2,4-dienoyl-CoA reductase, mitochondrialcellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; protein homotetramerization [GO:0051289]; small molecule metabolic process [GO:0044281]2,4-dienoyl-CoA reductase (NADPH) activity [GO:0008670]; NADPH binding [GO:0070402]; oxidoreductase activity, acting on NAD(P)H [GO:0016651]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent < reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.P23229ITA6Integrin alpha-6SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22314500}; Single-pass type I membrane protein {ECO:0000269|PubMed:22314500}. Cell membrane {ECO:0000269|PubMed:22314500}; Lipid-anchor {ECO:0000269|PubMed:22314500}.8amelogenesis [GO:0097186]; blood coagulation [GO:0007596]; brown fat cell differentiation [GO:0050873]; cell adhesion mediated by integrin [GO:0033627]; cell junction assembly [GO:0034329]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; cell-substrate junction assembly [GO:0007044]; cellular response to extracellular stimulus [GO:0031668]; digestive tract development [GO:0048565]; ectodermal cell differentiation [GO:0010668]; extracellular matrix organization [GO:0030198]; filopodium assembly [GO:0046847]; hemidesmosome assembly [GO:0031581]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; nail development [GO:0035878]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; renal system development [GO:0072001]; skin development [GO:0043588]basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; hemidesmosome [GO:0030056]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]FUNCTION: Integrin alpha-6/beta-1 is a receptor for laminin on platelets. Integrin alpha-6/beta-4 is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome. {ECO:0000269|PubMed:17303120}.Q9BVK6TMED9/Transmembrane emp24 domain-containing protein 9SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Cycles between compartments of the early secretatory pathway.COPI coating of Golgi vesicle [GO:0048205]; Golgi organization [GO:0007030]; positive regulation of organelle organization [GO:0010638]; protein transport [GO:0015031]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; trans-Golgi network transport vesicle [GO:0030140],FUNCTION: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB. {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:14600267, ECO:0000269|PubMed:16595549, ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:19296914}.Q12770SCAPESterol regulatory element-binding protein cleavage-activating proteinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. {ECO:0000250}.aging [GO:0007568]; cholesterol metabolic process [GO:0008203]; negative regulation of cholesterol biosynthetic process [GO:0045541]; positive regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045716]; regulation of fatty acid biosynthetic process [GO:0042304]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; small molecule metabolic process [GO:0044281]; SREBP signaling pathway [GO:0032933]Gcholesterol binding [GO:0015485]; unfolded protein binding [GO:0051082] endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; protein complex [GO:0043234]FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP/SREBF complex from the ER upon low cholesterol. Formation of a ternary complex with INSIG at high sterol concentrations leads to masking of an ER-export signal in SCAP and retention of the complex in the ER. Low sterol concentrations trigger release of INSIG, a conformational change in the SSC domain of SCAP, unmasking of the ER export signal, recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of SREBF in the Golgi, release of the transcription factor fragment of SREBF from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (By similarity). {ECO:0000250}.P98160PGBMDBasement membrane-specific heparan sulfate proteoglycan core protein]SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.pangiogenesis [GO:0001525]; brain development [GO:0007420]; carbohydrate metabolic process [GO:0005975]; cardiac muscle tissue development [GO:0048738]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; chondrocyte differentiation [GO:0002062]; chondroitin sulfate metabolic process [GO:0030204]; embryonic skeletal system morphogenesis [GO:0048704]; endochondral ossification [GO:0001958]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; lipoprotein metabolic process [GO:0042157]; phototransduction, visible light [GO:0007603]; protein localization [GO:0008104]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]Gmetal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]basal lamina [GO:0005605]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]FUNCTION: Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.; FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phospho< rylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.; FUNCTION: The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.Q9UHI8ATS1@A disintegrin and metalloproteinase with thrombospondin motifs 1XSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to vitamin D [GO:0071305]; heart trabecula formation [GO:0060347]; integrin-mediated signaling pathway [GO:0007229]; kidney development [GO:0001822]; negative regulation of cell proliferation [GO:0008285]; ovulation from ovarian follicle [GO:0001542]; positive regulation of neuron projection development [GO:0010976]; tooth eruption [GO:0044691]heparin binding [GO:0008201]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]Xbasement membrane [GO:0005604]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]hFUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture. {ECO:0000250, ECO:0000269|PubMed:10438512}.O43819SCO2#Protein SCO2 homolog, mitochondrial TCA regulatorcellular copper ion homeostasis [GO:0006878]; copper ion transport [GO:0006825]; eye development [GO:0001654]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; muscle system process [GO:0003012]; oxidation-reduction process [GO:0055114]; respiratory chain complex IV assembly [GO:0008535]; respiratory electron transport chain [GO:0022904]; response to activity [GO:0014823]; transcription initiation from RNA polymerase II promoter [GO:0006367]mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myofibril [GO:0030016]; nucleoplasm [GO:0005654]zFUNCTION: Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).Q96MT1RN145RING finger protein 145P27105STOM,Erythrocyte band 7 integral membrane proteinSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Melanosome. Cytoplasmic vesicle {ECO:0000250}. Note=Exposed on the cytoplasmic surface of the membrane. Associated with lipid rafts. Concentrates preferentially in plasma membrane protrusions and in a juxta-nuclear region which may represent Golgi-derived vesicles. Colocalizes with actin. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of protein targeting to membrane [GO:0090314]; protein homooligomerization [GO:0051260]; regulation of acid-sensing ion channel activity [GO:1901585]#RNA polymerase binding [GO:0070063]blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; vesicle [GO:0031982]uFUNCTION: Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.Q00325MPCP(Phosphate carrier protein, mitochondrialgeneration of precursor metabolites and energy [GO:0006091]; phosphate ion transmembrane transport [GO:0035435]; transport [GO:0006810]rphosphate ion carrier activity [GO:0015320]; protein complex binding [GO:0032403]; symporter activity [GO:0015293]extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: Transport of phosphate groups from the cytosol to the mitochondrial matrix. Phosphate is cotransported with H(+). May play a role regulation of the mitochondrial permeability transition pore (mPTP).Q8IVS2FABD<Malonyl-CoA-acyl carrier protein transacylase, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12882974}.Lfatty acid biosynthetic process [GO:0006633]; metabolic process [GO:0008152][acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; poly(A) RNA binding [GO:0044822]; transferase activity [GO:0016740]FUNCTION: Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias. {ECO:0000269|PubMed:12882974}.Q6IAN0DRS7B,Dehydrogenase/reductase SDR family member 7B1FUNCTION: Putative oxidoreductase. {ECO:0000305}.P56589PEX3Peroxisomal biogenesis factor 3SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11390669}; Multi-pass membrane protein {ECO:0000269|PubMed:11390669}.wactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; amino acid transmembrane transport [GO:0003333]; peroxisome membrane biogenesis [GO:0016557]; peroxisome organization [GO:0007031]; positive regulation of defense response to virus by host [GO:0002230]; protein import into peroxisome membrane [GO:0045046]; transmembrane transport [GO:0055085]amino acid transmembrane transporter activity [GO:0015171]; lipid binding [GO:0008289]; protein dimerization activity [GO:0046983]Wcytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; integral component of peroxisomal membrane [GO:0005779]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein complex [GO:0043234]; protein-lipid complex [GO:0032994]1FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes. {ECO:0000269|PubMed:10848631, ECO:0000269|PubMed:15007061}.P10620MGST1&Microsomal glutathione S-transferase 1SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.cellular response to lipid hydroperoxide [GO:0071449]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; Leydig cell differentiation [GO:0033327]; oxidation-reduction process [GO:0055114]; protein homotrimerization [GO:0070207]; response to drug [GO:0042493]; response to lipopolysaccharide [GO:0032496]; response to organonitrogen compound [GO:0010243]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]}glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]Iapical part of cell [GO:0045177]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity.Q8N682DRAM12DNA damage-regulated autophagy modulator protein 1< SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16839881}; Multi-pass membrane protein {ECO:0000269|PubMed:16839881}.\apoptotic process [GO:0006915]; autophagy [GO:0006914]; regulation of autophagy [GO:0010506]{cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]FUNCTION: Lysosomal modulator of autophagy that plays a central role in p53/TP53-mediated apoptosis. Not involved in p73/TP73-mediated autophagy. {ECO:0000269|PubMed:16839881, ECO:0000269|PubMed:17304243}.Q9BRQ6MIC25MICOS complex subunit MIC25SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:22228767}; Lipid-anchor {ECO:0000305|PubMed:22228767}. Mitochondrion {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.Ucellular response to DNA damage stimulus [GO:0006974]; cristae formation [GO:0042407]aMICOS complex [GO:0061617]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000269|PubMed:22228767}.Q9Y5J7TIM9<Mitochondrial import inner membrane translocase subunit Tim9SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral membrane protein {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Intermembrane side {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.cellular protein metabolic process [GO:0044267]; chaperone-mediated protein transport [GO:0072321]; protein import into mitochondrial inner membrane [GO:0045039]; protein targeting to mitochondrion [GO:0006626]; sensory perception of sound [GO:0007605]chaperone binding [GO:0051087]; protein homodimerization activity [GO:0042803]; transporter activity [GO:0005215]; zinc ion binding [GO:0008270]mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}.Q13530SERC3Serine incorporator 3]SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.L-serine transport [GO:0015825]; phosphatidylserine metabolic process [GO:0006658]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; sphingolipid metabolic process [GO:0006665]8L-serine transmembrane transporter activity [GO:0015194]gGolgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]5FUNCTION: May be involved in cellular transformation.Q969X5ERGI1>Endoplasmic reticulum-Golgi intermediate compartment protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Golgi apparatus membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Note=Cycles between the endoplasmic reticulum and the Golgi.3ER to Golgi vesicle-mediated transport [GO:0006888]endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]lFUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000303|PubMed:15308636}.Q9Y320TMX2+Thioredoxin-related transmembrane protein 2>cell [GO:0005623]; integral component of membrane [GO:0016021]Q9UKA9PTBP2&Polypyrimidine tract-binding protein 2mRNA splice site selection [GO:0006376]; negative regulation of RNA splicing [GO:0033119]; regulation of neural precursor cell proliferation [GO:2000177]!spliceosomal complex [GO:0005681]FUNCTION: RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA. {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:12667457}.O00142KITM!Thymidine kinase 2, mitochondrialdeoxycytidine metabolic process [GO:0046092]; deoxyribonucleotide metabolic process [GO:0009262]; DNA biosynthetic process [GO:0071897]; mitochondrial DNA replication [GO:0006264]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside salvage [GO:0043097]; small molecule metabolic process [GO:0044281]; thymidine metabolic process [GO:0046104]lATP binding [GO:0005524]; deoxycytidine kinase activity [GO:0004137]; thymidine kinase activity [GO:0004797]Lmitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]FUNCTION: Deoxyribonucleoside kinase that phosphorylates thymidine, deoxycytidine, and deoxyuridine. Also phosphorylates anti-viral and anti-cancer nucleoside analogs.Q13454TUSC3Tumor suppressor candidate 3Wcell redox homeostasis [GO:0045454]; cellular protein metabolic process [GO:0044267]; cognition [GO:0050890]; magnesium ion transport [GO:0015693]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; transmembrane transport [GO:0055085]=magnesium ion transmembrane transporter activity [GO:0015095]endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; mitochondrion [GO:0005739]; oligosaccharyltransferase complex [GO:0008250]; plasma membrane [GO:0005886]FUNCTION: Magnesium transporter (PubMed:19717468). May be involved in N-glycosylation through its association with N-oligosaccharyl transferase (PubMed:24685145). {ECO:0000269|PubMed:19717468, ECO:0000303|PubMed:12887896, ECO:0000303|PubMed:24685145}.P09110THIK$3-ketoacyl-CoA thiolase, peroxisomalalpha-linolenic acid metabolic process [GO:0036109]; bile acid metabolic process [GO:0008206]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; small molecule metabolic process [GO:0044281]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid metabolic process [GO:0000038]_acetyl-CoA C-acyltransferase activity [GO:0003988]; palmitoyl-CoA oxidase activity [GO:0016401]intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]Q9Y3E5PTH2(Peptidyl-tRNA hydrolase 2, mitochondrialapoptotic process [GO:0006915]; negative regulation of anoikis [GO:2000811]; negative regulation of gene expression [GO:0010629]; positive regulation of anoikis [GO:2000210].aminoacyl-tRNA hydrolase activity [GO:0004045]Gcytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]'FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000250}.; FUNCTION: Promotes caspase-indepen< dent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1. {ECO:0000269|PubMed:15006356}.P30536TSPOATranslocator proteinSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:1847678}; Multi-pass membrane protein {ECO:0000269|PubMed:1847678}."adrenal gland development [GO:0030325]; aging [GO:0007568]; anion transport [GO:0006820]; apoptotic process [GO:0006915]; behavioral response to pain [GO:0048266]; cell proliferation [GO:0008283]; cellular hypotonic response [GO:0071476]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to zinc ion [GO:0071294]; chloride transport [GO:0006821]; contact inhibition [GO:0060242]; glial cell migration [GO:0008347]; heme biosynthetic process [GO:0006783]; lipid transport [GO:0006869]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of tumor necrosis factor production [GO:0032720]; peripheral nervous system axon regeneration [GO:0014012]; positive regulation of apoptotic process [GO:0043065]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of necrotic cell death [GO:0010940]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; protein targeting to mitochondrion [GO:0006626]; regulation of cholesterol transport [GO:0032374]; regulation of steroid biosynthetic process [GO:0050810]; response to drug [GO:0042493]; response to manganese ion [GO:0010042]; response to progesterone [GO:0032570]; response to testosterone [GO:0033574]; response to vitamin B1 [GO:0010266]; steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202]nandrogen binding [GO:0005497]; benzodiazepine receptor activity [GO:0008503]; cholesterol binding [GO:0015485]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]-FUNCTION: Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism (PubMed:24814875), but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides (PubMed:1847678). {ECO:0000250, ECO:0000269|PubMed:1847678, ECO:0000269|PubMed:24814875}.P25445TNR63Tumor necrosis factor receptor superfamily member 6Fas0SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.; SUBCELLULAR LOCATION: Isoform 3: Secreted.; SUBCELLULAR LOCATION: Isoform 4: Secreted.; SUBCELLULAR LOCATION: Isoform 5: Secreted.; SUBCELLULAR LOCATION: Isoform 6: Secreted.activation-induced cell death of T cells [GO:0006924]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; B cell mediated immunity [GO:0019724]; cell surface receptor signaling pathway [GO:0007166]; cellular response to hyperoxia [GO:0071455]; cellular response to lithium ion [GO:0071285]; cellular response to mechanical stimulus [GO:0071260]; circadian rhythm [GO:0007623]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; hepatocyte apoptotic process [GO:0097284]; immunoglobulin production [GO:0002377]; inflammatory cell apoptotic process [GO:0006925]; motor neuron apoptotic process [GO:0097049]; necroptotic process [GO:0070266]; necroptotic signaling pathway [GO:0097527]; negative regulation of apoptotic process [GO:0043066]; negative regulation of B cell activation [GO:0050869]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative thymic T cell selection [GO:0045060]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of protein homooligomerization [GO:0032464]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein complex assembly [GO:0006461]; protein homooligomerization [GO:0051260]; regulation of apoptotic process [GO:0042981]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of lymphocyte differentiation [GO:0045619]; regulation of myeloid cell differentiation [GO:0045637]; regulation of necrotic cell death [GO:0010939]; renal system process [GO:0003014]; response to glucocorticoid [GO:0051384]; response to toxic substance [GO:0009636]; signal transduction [GO:0007165]; spleen development [GO:0048536]; transformed cell apoptotic process [GO:0006927]identical protein binding [GO:0042802]; kinase binding [GO:0019900]; receptor activity [GO:0004872]; signal transducer activity [GO:0004871]; transmembrane signaling receptor activity [GO:0004888]zCD95 death-inducing signaling complex [GO:0031265]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]?FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). {ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:7533181}.Q96PD2DCBD23Discoidin, CUB and LCCL domain-containing protein 2SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11973641}; Single-pass type I membrane protein {ECO:0000269|PubMed:11973641}.intracellular receptor signaling pathway [GO:0030522]; negative regulation of cell growth [GO:0030308]; wound healing [GO:0042060]Mcell surface [GO:0009986]; integral component of plasma membrane [GO:0005887]Q9UFN0NPS3AProtein NipSnap homolog 3ASUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12427096}. Note=May be part of some vesicular structure distinct from lysosomal vesicles.P53985MOT1Monocarboxylate transporter 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:24390345}; Multi-pass membrane protein {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:24390345}.behavioral response to nutrient [GO:0051780]; blood coagulation [GO:0007596]; cellular metabolic process [GO:0044237]; cellular response to organic cyclic compound [GO:0071407]; centrosome organization [GO:0051297]; glucose homeostasis [GO:0042593]; leukocyte migration [GO:0050900]; lipid metabolic process [GO:0006629]; mevalonate transport [GO:0015728]; monocarboxylic acid transport [GO:0015718]; plasma membrane lactate transport [GO:0035879]; pyruvate metabolic process [GO:0006090]; regulation of insulin secretion [GO:0050796]; response to food [GO:0032094]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]lactate transmembrane transporter activity [GO:0015129]; mevalonate transmembrane < transporter activity [GO:0015130]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; organic cyclic compound binding [GO:0097159]; symporter activity [GO:0015293]centrosome [GO:0005813]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]]FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis. {ECO:0000269|PubMed:17701893}.Q86TM6SYVN1&E3 ubiquitin-protein ligase synoviolin<SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510}; Multi-pass membrane protein {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16186510}.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; IRE1-mediated unfolded protein response [GO:0036498]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; protein K48-linked ubiquitination [GO:0070936]; protein N-linked glycosylation via asparagine [GO:0018279]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; retrograde protein transport, ER to cytosol [GO:0030970]JATPase binding [GO:0051117]; chaperone binding [GO:0051087]; ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase activity involved in ERAD pathway [GO:1904264]; ubiquitin-specific protease binding [GO:1990381]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; Hrd1p ubiquitin ligase complex [GO:0000836]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; smooth endoplasmic reticulum [GO:0005790]tFUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. {ECO:0000269|PubMed:12459480, ECO:0000269|PubMed:12646171, ECO:0000269|PubMed:12975321, ECO:0000269|PubMed:14593114, ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16847254, ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:17141218, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:22607976}.P24593IBP5,Insulin-like growth factor-binding protein 5cellular protein metabolic process [GO:0044267]; cellular response to cAMP [GO:0071320]; cellular response to organic cyclic compound [GO:0071407]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; hair follicle morphogenesis [GO:0031069]; intracellular signal transduction [GO:0035556]; mammary gland involution [GO:0060056]; negative regulation of cell migration [GO:0030336]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of translation [GO:0017148]; osteoblast differentiation [GO:0001649]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of protein kinase B signaling [GO:0051897]; regulation of cell growth [GO:0001558]; regulation of glucose metabolic process [GO:0010906]; response to growth hormone [GO:0060416]; signal transduction [GO:0007165]; skeletal muscle tissue growth [GO:0048630]; striated muscle cell differentiation [GO:0051146]; type B pancreatic cell proliferation [GO:0044342]fibronectin binding [GO:0001968]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]extracellular region [GO:0005576]; extracellular space [GO:0005615]; insulin-like growth factor binding protein complex [GO:0016942]; insulin-like growth factor ternary complex [GO:0042567]; intracellular [GO:0005622]FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.O76095JTB Protein JTBpSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250}. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Detected at the centrosome and along spindle fibers during prophase and metaphase. Detected at the midbody during telophase.apoptotic mitochondrial changes [GO:0008637]; cytokinesis [GO:0000910]; mitotic nuclear division [GO:0007067]; positive regulation of protein kinase activity [GO:0045860]; regulation of cell proliferation [GO:0042127]#protein kinase binding [GO:0019901]cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; mitochondrion [GO:0005739]; spindle [GO:0005819]vFUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1 (By similarity). Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential (By similarity). {ECO:0000250}.O43759SNG1Synaptogyrin-1/SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17081065}; Multi-pass membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Cell junction, synapse {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.protein targeting [GO:0006605]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of short-term neuronal synaptic plasticity [GO:0048172]cell junction [GO:0030054]; integral component of membrane [GO:0016021]; m< elanosome [GO:0042470]; neuromuscular junction [GO:0031594]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]dFUNCTION: Involved in the regulation of short-term and long-term synaptic plasticity. {ECO:0000250}.Q07065CKAP4!Cytoskeleton-associated protein 4 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Note=Translocates to the perinuclear region upon APF-stimulation.;cytoskeleton [GO:0005856]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: High-affinity epithelial cell surface receptor for APF.; FUNCTION: Mediates the anchoring of the endoplasmic reticulum to microtubules.Q9P0B6CC167)Coiled-coil domain-containing protein 167Q9BXK5B2L13Bcl-2-like protein 13SUBCELLULAR LOCATION: Isoform 2: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000305}.}activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]Ycysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]@FUNCTION: May promote the activation of caspase-3 and apoptosis.P19823ITIH2,Inter-alpha-trypsin inhibitor heavy chain H2protease inhibitorehyaluronan metabolic process [GO:0030212]; negative regulation of endopeptidase activity [GO:0010951]hendopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867]gblood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]*FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.O14786NRP1 Neuropilin-1 apolipoprotein(PC00052);cell adhesion molecule(PC00069);enzyme modulator(PC00095);extracellular matrix protein(PC00102);membrane-bound signaling molecule(PC00152);metalloprotease(PC00153);oxidase(PC00175);receptor(PC00197);serine protease(PC00203);transporter(PC00227)uSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.angiogenesis [GO:0001525]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; artery morphogenesis [GO:0048844]; axonal fasciculation [GO:0007413]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axonogenesis involved in innervation [GO:0060385]; branchiomotor neuron axon guidance [GO:0021785]; cell-cell signaling [GO:0007267]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; commissural neuron axon guidance [GO:0071679]; coronary artery morphogenesis [GO:0060982]; dendrite development [GO:0016358]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; endothelial cell chemotaxis [GO:0035767]; endothelial tip cell fate specification [GO:0097102]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; ganglion morphogenesis [GO:0061552]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neuron migration [GO:0001764]; organ morphogenesis [GO:0009887]; otic placode formation [GO:0043049]; patterning of blood vessels [GO:0001569]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive chemotaxis [GO:0050918]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of cytokine activity [GO:0060301]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of retinal ganglion cell axon guidance [GO:1902336]; positive regulation of smooth muscle cell migration [GO:0014911]; protein localization to early endosome [GO:1902946]; regulation of retinal ganglion cell axon guidance [GO:0090259]; regulation of vesicle-mediated transport [GO:0060627]; renal artery morphogenesis [GO:0061441]; retinal ganglion cell axon guidance [GO:0031290]; retina vasculature morphogenesis in camera-type eye [GO:0061299]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; semaphorin-plexin signaling pathway involved in neuron projection guidance [GO:1902285]; sensory neuron axon guidance [GO:0097374]; signal transduction [GO:0007165]; sprouting angiogenesis [GO:0002040]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; toxin transport [GO:1901998]; trigeminal ganglion development [GO:0061551]; trigeminal nerve structural organization [GO:0021637]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; VEGF-activated neuropilin signaling pathway [GO:0038190]; VEGF-activated neuropilin signaling pathway involved in axon guidance [GO:1902378]; ventral trunk neural crest cell migration [GO:0036486]; vestibulocochlear nerve structural organization [GO:0021649]Rcoreceptor activity [GO:0015026]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor-activated receptor activity [GO:0005021]; vascular endothelial growth factor binding [GO:0038085]taxon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; neurofilament [GO:0005883]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; semaphorin receptor complex [GO:0002116]; sorting endosome [GO:0097443]FUNCTION: The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis.; FUNCTION: The soluble isoform 2 binds VEGF-165 and appears to inhibit its binding to cells. It may also induce apoptosis by sequestering VEGF-165. May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity.O75127PTCD1<Pentatricopeptide repeat-containing protein 1, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19651879, ECO:0000269|PubMed:21857155}. Mitochondrion matrix {ECO:0000250}.#tRNA 3'-end processing [< GO:0042780];poly(A) RNA binding [GO:0044822]; tRNA binding [GO:0000049]FUNCTION: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs. {ECO:0000269|PubMed:21857155}.Q13286CLN3BatteninSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17286803, ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:17286803, ECO:0000269|PubMed:17897319}. Late endosome {ECO:0000269|PubMed:17286803}.Daction potential [GO:0001508]; amyloid precursor protein catabolic process [GO:0042987]; arginine transport [GO:0015809]; associative learning [GO:0008306]; autophagosome fusion [GO:0000046]; cellular amino acid metabolic process [GO:0006520]; ceramide metabolic process [GO:0006672]; cytosolic calcium ion homeostasis [GO:0051480]; galactosylceramide metabolic process [GO:0006681]; globoside metabolic process [GO:0001575]; glucosylceramide metabolic process [GO:0006678]; ionotropic glutamate receptor signaling pathway [GO:0035235]; lysosomal lumen acidification [GO:0007042]; lysosomal lumen pH elevation [GO:0035752]; lysosome organization [GO:0007040]; macroautophagy [GO:0016236]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; negative regulation of catalytic activity [GO:0043086]; negative regulation of macroautophagy [GO:0016242]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of proteolysis [GO:0045861]; neuromuscular process controlling balance [GO:0050885]; neurotransmitter metabolic process [GO:0042133]; protein catabolic process [GO:0030163]; protein processing [GO:0016485]; receptor-mediated endocytosis [GO:0006898]; sphingomyelin metabolic process [GO:0006684]; vacuolar transport [GO:0007034]; vesicle transport along microtubule [GO:0047496]autophagosome [GO:0005776]; caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; trans-Golgi network [GO:0005802]FUNCTION: Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes. {ECO:0000269|PubMed:22261744}.O6061315 kDa selenoproteinSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:11278576}. Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum.7de novo' posttranslational protein folding [GO:0051084]Lendoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]FUNCTION: May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum (By similarity). {ECO:0000250}.P78363ABCA41Retinal-specific ATP-binding cassette transporterSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10075733}; Multi-pass membrane protein {ECO:0000269|PubMed:10075733}. Note=Localized to outer segment disk edges of rods and cones, with around one million copies/photoreceptor.Tcholesterol efflux [GO:0033344]; phospholipid efflux [GO:0033700]; phospholipid transfer to membrane [GO:0006649]; photoreceptor cell maintenance [GO:0045494]; phototransduction, visible light [GO:0007603]; retinoid metabolic process [GO:0001523]; transmembrane transport [GO:0055085]; transport [GO:0006810]; visual perception [GO:0007601]"ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; cholesterol transporter activity [GO:0017127]; phospholipid-translocating ATPase activity [GO:0004012]; phospholipid transporter activity [GO:0005548]; transporter activity [GO:0005215]integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]FUNCTION: In the visual cycle, acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans-retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. May play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery. {ECO:0000269|PubMed:10075733}.Q04721NOTC2(Neurogenic locus notch homolog protein 2qSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Notch 2 intracellular domain: Nucleus {ECO:0000269|PubMed:25985737}. Cytoplasm {ECO:0000269|PubMed:25985737}. Note=Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by C8orf4 (PubMed:25985737). {ECO:0000269|PubMed:25985737}.apoptotic process [GO:0006915]; atrial septum morphogenesis [GO:0060413]; bone remodeling [GO:0046849]; cell cycle arrest [GO:0007050]; cell fate determination [GO:0001709]; cell growth [GO:0016049]; gene expression [GO:0010467]; hemopoiesis [GO:0030097]; intracellular receptor signaling pathway [GO:0030522]; multicellular organismal development [GO:0007275]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; nervous system development [GO:0007399]; Notch receptor processing [GO:0007220]; Notch signaling involved in heart development [GO:0061314]; Notch signaling pathway [GO:0007219]; organ morphogenesis [GO:0009887]; positive regulation of Ras protein signal transduction [GO:0046579]; pulmonary valve morphogenesis [GO:0003184]; regulation of transcription, DNA-templated [GO:0006355]; stem cell maintenance [GO:0019827]; transcription initiation from RNA polymerase II promoter [GO:0006367]calcium ion binding [GO:0005509]; ligand-activated RNA polymerase II transcription factor binding transcription factor activity [GO:0038049]; receptor activity [GO:0004872]>cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells (PubMed:25985737). {ECO:0000250|UniProtKB:O35516, ECO:0000269|PubMed:21378985, ECO:0000269|PubMed:21378989, ECO:0000269|PubMed:25985737}.O14944EREG ProepiregulinSUBCELLULAR LOCATION: Epiregulin: Secreted, extracellular space.; SUBCELLULAR LOCATION: Proepiregulin: Cell membrane; Single-pass type I membrane protein.activation of MAPK activity [GO:0000187]; anatomical structure morphogenesis [GO:0009653]; angiogenesis [GO:0001525]; cell-cell signaling [GO:0007267]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon re< ceptor signaling pathway [GO:0038095]; female meiotic division [GO:0007143]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; luteinizing hormone signaling pathway [GO:0042700]; mRNA transcription [GO:0009299]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of smooth muscle cell differentiation [GO:0051151]; negative regulation of transcription, DNA-templated [GO:0045892]; neurotrophin TRK receptor signaling pathway [GO:0048011]; oocyte maturation [GO:0001556]; organ morphogenesis [GO:0009887]; ovarian cumulus expansion [GO:0001550]; ovulation [GO:0030728]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cytokine biosynthetic process [GO:0042108]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA replication [GO:0045740]; positive regulation of epidermal growth factor-activated receptor activity [GO:0045741]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of innate immune response [GO:0045089]; positive regulation of interleukin-6 biosynthetic process [GO:0045410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of smooth muscle cell proliferation [GO:0048661]; primary follicle stage [GO:0048160]; response to peptide hormone [GO:0043434]; wound healing [GO:0042060]Zepidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]extracellular region [GO:0005576]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]FUNCTION: Ligand of the EGF receptor/EGFR and ERBB4. May be a mediator of localized cell proliferation. As a mitogen it may stimulate cell proliferation and/or angiogenesis. {ECO:0000269|PubMed:9419975}.Q92581SL9A6Sodium/hydrogen exchanger 6 SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:11940519}; Multi-pass membrane protein {ECO:0000269|PubMed:11940519}. Note=Is present in the recycling compartments including early and recycling endosomes, and only appears transiently on the plasma membrane.axon extension [GO:0048675]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; dendrite extension [GO:0097484]; dendritic spine development [GO:0060996]; ion transport [GO:0006811]; neuron projection morphogenesis [GO:0048812]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386]; regulation of pH [GO:0006885]; sodium ion transmembrane transport [GO:0035725]; synapse organization [GO:0050808]; transmembrane transport [GO:0055085]; transport [GO:0006810].sodium:proton antiporter activity [GO:0015385]axonal spine [GO:0044308]; axon terminus [GO:0043679]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; synapse [GO:0045202]FUNCTION: Electroneutral exchange of protons for Na(+) and K(+) across the early and recycling endosome membranes. Contributes to calcium homeostasis.Q49B96COX19+Cytochrome c oxidase assembly protein COX19GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16212937}.baerobic respiration [GO:0009060]; mitochondrial respiratory chain complex IV assembly [GO:0033617]\cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]`FUNCTION: May be required for the assembly of mitochondrial cytochrome c oxidase. {ECO:0000250}.Q9P0P8CF203 Uncharacterized protein C6orf203O00767ACODAcyl-CoA desaturase'Biosynthesis of unsaturated fatty acidsSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:18765284, ECO:0000305}.,fatty acid biosynthetic process [GO:0006633]/stearoyl-CoA 9-desaturase activity [GO:0004768]FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity). {ECO:0000250|UniProtKB:P13516, ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:18765284}.P23434GCSH0Glycine cleavage system H protein, mitochondrialglycine catabolic process [GO:0006546]; glycine decarboxylation via glycine cleavage system [GO:0019464]; methylation [GO:0032259],aminomethyltransferase activity [GO:0004047]Aglycine cleavage complex [GO:0005960]; mitochondrion [GO:0005739]FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).P02751FINC Fibronectinacute-phase response [GO:0006953]; angiogenesis [GO:0001525]; blood coagulation [GO:0007596]; calcium-independent cell-matrix adhesion [GO:0007161]; cell adhesion [GO:0007155]; cell-substrate junction assembly [GO:0007044]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; integrin activation [GO:0033622]; leukocyte migration [GO:0050900]; negative regulation of transforming growth factor-beta secretion [GO:2001202]; peptide cross-linking [GO:0018149]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of axon extension [GO:0045773]; positive regulation of cell proliferation [GO:0008284]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of substrate-dependent cell migration, cell attachment to substrate [GO:1904237]; regulation of cell shape [GO:0008360]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of protein phosphorylation [GO:0001932]; response to wounding [GO:0009611]; substrate adhesion-dependent cell spreading [GO:0034446]collagen binding [GO:0005518]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; peptidase activator activity [GO:0016504]; protease binding [GO:0002020]{apical plasma membrane [GO:0016324]; basal lamina [GO:0005605]; blood microparticle [GO:0072562]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule lumen [GO:0031093]FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; FUNCTION: Anastellin binds fibronectin and induces fibril formation. This fibr< onectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.Q6P1X6CH082UPF0598 protein C8orf82Q9P2B2FPRP,Prostaglandin F2 receptor negative regulatorSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.(lipid particle organization [GO:0034389]cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]FUNCTION: Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur (By similarity). {ECO:0000250}.Q9HCU0CD248 Endosialin transmembraneanatomical structure regression [GO:0060033]; cell migration [GO:0016477]; lymph node development [GO:0048535]; positive regulation of cell proliferation [GO:0008284]; positive regulation of endothelial cell apoptotic process [GO:2000353]ncalcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; extracellular matrix binding [GO:0050840]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; proteinaceous extracellular matrix [GO:0005578]OFUNCTION: May play a role in tumor angiogenesis. {ECO:0000269|PubMed:15862292}.Q96DB5RMD1+Regulator of microtubule dynamics protein 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles.hcentrosome [GO:0005813]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; spindle pole [GO:0000922]Q9Y3Q3TMED3/Transmembrane emp24 domain-containing protein 38SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Probably cycles between compartments of the early secretatory pathway.oCOPI vesicle coat [GO:0030126]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]FUNCTION: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. {ECO:0000269|PubMed:10852829}.P33897ABCD1*ATP-binding cassette sub-family D member 1GSUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.~alpha-linolenic acid metabolic process [GO:0036109]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; linoleic acid metabolic process [GO:0043651]; long-chain fatty acid catabolic process [GO:0042758]; peroxisomal long-chain fatty acid import [GO:0015910]; peroxisomal membrane transport [GO:0015919]; peroxisome organization [GO:0007031]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid catabolic process [GO:0042760][ATPase activity [GO:0016887]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; peroxisomal fatty-acyl-CoA transporter activity [GO:0005325]; protein homodimerization activity [GO:0042803]; transporter activity [GO:0005215]cytoplasm [GO:0005737]; cytosol [GO:0005829]; integral component of peroxisomal membrane [GO:0005779]; membrane [GO:0016020]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. {ECO:0000269|PubMed:11248239}.P56557TM50BTransmembrane protein 50Bmendoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]Q92484ASM3A/Acid sphingomyelinase-like phosphodiesterase 3a,sphingomyelin catabolic process [GO:0006685]phydrolase activity, acting on glycosyl bonds [GO:0016798]; sphingomyelin phosphodiesterase activity [GO:0004767]Dextracellular exosome [GO:0070062]; extracellular space [GO:0005615]P49281NRAM22Natural resistance-associated macrophage protein 2kSUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:12475959, ECO:0000269|PubMed:25491917}; Multi-pass membrane protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:12475959}.; SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12475959, ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:25491917}; Multi-pass membrane protein {ECO:0000269|PubMed:18776082}. Mitochondrion outer membrane {ECO:0000269|PubMed:24448823}; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:12475959, ECO:0000269|PubMed:25326704, ECO:0000269|PubMed:25491917}; Multi-pass membrane protein {ECO:0000305}.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cadmium ion transmembrane transport [GO:0070574]; cation transmembrane transport [GO:0098655]; cellular copper ion homeostasis [GO:0006878]; cellular iron ion homeostasis [GO:0006879]; cellular response to hypoxia [GO:0071456]; cellular response to iron ion [GO:0071281]; cellular response to oxidative stress [GO:0034599]; cellular response to tumor necrosis factor [GO:0071356]; cobalt ion transport [GO:0006824]; copper ion import into cell [GO:1902861]; copper ion transmembrane transport [GO:0035434]; copper ion transport [GO:0006825]; dendrite morphogenesis [GO:0048813]; detection of oxygen [GO:0003032]; erythrocyte development [GO:0048821]; ferrous iron import [GO:0070627]; ferrous iron transmembrane transport [GO:1903874]; ferrous iron transport [GO:0015684]; heme biosynthetic process [GO:0006783]; lead ion transport [GO:0015692]; learning or memory [GO:0007611]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; multicellular organismal iron ion homeostasis [GO:0060586]; nickel cation transmembrane transport [GO:0035444]; nickel cation transport [GO:0015675]; response to cadmium ion [GO:0046686]; response to hypoxia [GO:0001666]; response to iron ion [GO:0010039]; response to lead ion [GO:0010288]; response to manganese ion [GO:0010042]; transmembrane transport [GO:0055085]; vanadium ion transport [GO:0015676]; zinc II ion transmembrane transport [GO:0071577]Ecadmium ion binding [GO:0046870]; cadmium ion transmembrane transporter activity [GO:0015086]; cobalt ion binding [GO:0050897]; cobalt ion transmembrane transporter activity [GO:0015087]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; ferrous iron transmembrane transporter activity [GO:0015093]; ferrous iron uptake transmembrane transporter activity [GO:0015639]; hydrogen ion transmembrane transporter activity [GO:0015078]; inorganic cation transmembrane transporter activity [GO:0022890]; iron ion binding [GO:0005506]; lead ion transmembrane transporter activity [G< O:0015094]; manganese ion binding [GO:0030145]; manganese ion transmembrane transporter activity [GO:0005384]; nickel cation binding [GO:0016151]; nickel cation transmembrane transporter activity [GO:0015099]; solute:proton symporter activity [GO:0015295]; transition metal ion transmembrane transporter activity [GO:0046915]; vanadium ion transmembrane transporter activity [GO:0015100]; zinc ion binding [GO:0008270]; zinc ion transmembrane transporter activity [GO:0005385]apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; brush border [GO:0005903]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; paraferritin complex [GO:0070826]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]; vacuole [GO:0005773] FUNCTION: Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria. {ECO:0000269|PubMed:17109629, ECO:0000269|PubMed:24448823, ECO:0000269|PubMed:25326704, ECO:0000269|PubMed:25491917}.Q9UNN8EPCREndothelial protein C receptorantigen processing and presentation [GO:0019882]; blood coagulation [GO:0007596]; immune response [GO:0006955]; leukocyte migration [GO:0050900]; negative regulation of coagulation [GO:0050819]receptor activity [GO:0004872]cell surface [GO:0009986]; centrosome [GO:0005813]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.O00748EST2Cocaine esterase@SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.catabolic process [GO:0009056]ncarboxylic ester hydrolase activity [GO:0052689]; methylumbelliferyl-acetate deacetylase activity [GO:0047374]nendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. {ECO:0000269|PubMed:9169443}.Q8NAN2FA73AProtein FAM73AQ99424ACOX2%Peroxisomal acyl-coenzyme A oxidase 2Wbile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; small molecule metabolic process [GO:0044281]3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity [GO:0033791]; acyl-CoA dehydrogenase activity [GO:0003995]; acyl-CoA oxidase activity [GO:0003997]; electron carrier activity [GO:0009055]; fatty acid binding [GO:0005504]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]; pristanoyl-CoA oxidase activity [GO:0016402]; receptor binding [GO:0005102]8peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]gFUNCTION: Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.Q9UI15TAGL3 Transgelin-3central nervous system development [GO:0007417]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]0myelin sheath [GO:0043209]; nucleus [GO:0005634]P26022PTX3Pentraxin-related protein PTX3cinflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation by host of viral exo-alpha-sialidase activity [GO:0044869]; negative regulation by host of viral glycoprotein metabolic process [GO:0044871]; negative regulation of exo-alpha-sialidase activity [GO:1903016]; negative regulation of glycoprotein metabolic process [GO:1903019]; negative regulation of viral entry into host cell [GO:0046597]; opsonization [GO:0008228]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phagocytosis [GO:0050766]; response to yeast [GO:0001878]u(1->3)-beta-D-glucan binding [GO:0001872]; complement component C1q binding [GO:0001849]; virion binding [GO:0046790]FUNCTION: Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. {ECO:0000250}.Q9UGH3S23A2!Solute carrier family 23 member 2}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19379732}; Multi-pass membrane protein {ECO:0000269|PubMed:19379732}.L-ascorbic acid metabolic process [GO:0019852]; L-ascorbic acid transport [GO:0015882]; molecular hydrogen transport [GO:0015993]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase transport [GO:0015851]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; transepithelial L-ascorbic acid transport [GO:0070904]; vitamin metabolic process [GO:0006766]; vitamin transmembrane transport [GO:0035461]; water-soluble vitamin metabolic process [GO:0006767]>L-ascorbate:sodium symporter activity [GO:0008520]; L-ascorbic acid transporter activity [GO:0015229]; nucleobase transmembrane transporter activity [GO:0015205]; sodium-dependent L-ascorbate transmembrane transporter activity [GO:0070890]; sodium-dependent multivitamin transmembrane transporter activity [GO:0008523]apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.Q9NP80PLPL8*Calcium-independent phospholipase A2-gammaSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.parachidonic acid metabolic process [GO:0019369]; arachidonic acid secretion [GO:0050482]; cell death [GO:0008219]; fatty acid metabolic process [GO:0006631]; glycerophospholipid biosynthetic process [GO:0046474]; linoleic acid metabolic process [GO:0043651]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152]; phosphatidylethanolamine catabolic process [GO:0046338]; phospholipid metabolic process [GO:0006644]; prostaglandin biosynthetic process [GO:0001516]; small molecule metabolic process [GO:0044281]}ATP binding [GO:0005524]; calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 posi< tion of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids. {ECO:0000269|PubMed:10744668, ECO:0000269|PubMed:15695510}.Q9Y2C4EXOGNuclease EXOG, mitochondrialQSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18187503}.3DNA catabolic process, endonucleolytic [GO:0000737]endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nuclease activity [GO:0004518]; nucleic acid binding [GO:0003676]Gmitochondrial inner membrane [GO:0005743]; protein complex [GO:0043234]FUNCTION: Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity. {ECO:0000269|PubMed:18187503}.Q15811ITSN1 Intersectin-10SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell projection, lamellipodium. Membrane, clathrin-coated pit. Note=Colocalizes with SGIP1 at the plasma membrane in structures corresponding most problably to clathrin-coated pits. {ECO:0000305}.}apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein kinase B signaling [GO:0051897]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; synaptic vesicle endocytosis [GO:0048488]calcium ion binding [GO:0005509]; guanyl-nucleotide exchange factor activity [GO:0005085]; kinase activator activity [GO:0019209]; proline-rich region binding [GO:0070064]; protein complex scaffold [GO:0032947]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]cell junction [GO:0030054]; coated pit [GO:0005905]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]FUNCTION: Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase (By similarity). Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. Inhibits ARHGAP31 activity toward RAC1. {ECO:0000250, ECO:0000269|PubMed:11744688, ECO:0000269|PubMed:22648170}.O75695XRP2 Protein XRP2SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, cilium. Note=Detected predominantly to the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus.cell morphogenesis [GO:0000902]; CTP biosynthetic process [GO:0006241]; cytoskeleton organization [GO:0007010]; GTP biosynthetic process [GO:0006183]; organelle organization [GO:0006996]; positive regulation of GTPase activity [GO:0043547]; post-Golgi vesicle-mediated transport [GO:0006892]; protein folding [GO:0006457]; protein transport [GO:0015031]; UTP biosynthetic process [GO:0006228]; visual perception [GO:0007601]ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; GTP binding [GO:0005525]; nucleoside diphosphate kinase activity [GO:0004550]; unfolded protein binding [GO:0051082]centriole [GO:0005814]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; periciliary membrane compartment [GO:1990075]; plasma membrane [GO:0005886]; primary cilium [GO:0072372]FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. {ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:20106869, ECO:0000269|PubMed:22085962}.P49959MRE11)Double-strand break repair protein MRE11ASUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250}.base-excision repair [GO:0006284]; cell proliferation [GO:0008283]; cellular response to DNA damage stimulus [GO:0006974]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; heart development [GO:0007507]; innate immune response [GO:0045087]; intra-S DNA damage checkpoint [GO:0031573]; mitotic G2 DNA damage checkpoint [GO:0007095]; negative regulation of DNA endoreduplication [GO:0032876]; negative regulation of viral entry into host cell [GO:0046597]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; positive regulation of kinase activity [GO:0033674]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of type I interferon production [GO:0032481]; reciprocal meiotic recombination [GO:0007131]; regulation of mitotic recombination [GO:0000019]; sister chromatid cohesion [GO:0007062]; synapsis [GO:0007129]; telomere maintenance via telomerase [GO:0007004]; viral process [GO:0016032],3'-5' exonuclease activity [GO:0008408]; double-stranded DNA binding [GO:0003690]; endodeoxyribonuclease activity [GO:0004520]; manganese ion binding [GO:0030145]; nuclease activity [GO:0004518]; protein C-terminus binding [GO:0008022]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]chromatin [GO:0000785]; condensed nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; Mre11 complex [GO:0030870]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; site of double-strand break [GO:0035861]#FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.Q7KZN9COX153Cytochrome c oxidase assembly protein COX15 homologSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:9878253}; Multi-pass membrane protein {ECO:0000269|PubMed:9878253}.cellular respiration [GO:0045333]; heme a biosynthetic process [GO:0006784]; heme biosynthetic process [GO:0006783]; hydrogen ion transmembrane transport [GO:1902600]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; oxidation-reduction process [GO:0055114]; porphyrin-containing compound metabolic process [GO:0006778]; respiratory chain complex IV assembly [GO:0008535]; respiratory gaseous exchange [GO:0007585]; small molecule metabolic process [GO:0044281]cytochrome-c oxidase activity [GO:0004129]; oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor [GO:0016653]; oxidor< eductase activity, acting on the CH-CH group of donors [GO:0016627]cytochrome complex [GO:0070069]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain [GO:0005746]; mitochondrion [GO:0005739]WFUNCTION: May be involved in the biosynthesis of heme A. {ECO:0000269|PubMed:12474143}.Q9NZN4EHD2EH domain-containing protein 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17233914}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8BH64}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8BH64}. Membrane, caveola {ECO:0000250|UniProtKB:Q8BH64}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8BH64}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8BH64}. Endosome membrane {ECO:0000250|UniProtKB:Q4V8H8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4V8H8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q4V8H8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BH64}. Note=Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes. {ECO:0000250|UniProtKB:Q8BH64}.5blood coagulation [GO:0007596]; cortical actin cytoskeleton organization [GO:0030866]; endocytic recycling [GO:0032456]; endocytosis [GO:0006897]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of myoblast fusion [GO:1901741]; protein localization to plasma membrane [GO:0072659]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; nucleic acid binding [GO:0003676]caveola [GO:0005901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (By similarity). Plays a role in membrane trafficking between the plasma membrane and endosomes (PubMed:17233914). Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q8BH64, ECO:0000269|PubMed:17233914}.P60228EIF3E4Eukaryotic translation initiation factor 3 subunit E3SUBCELLULAR LOCATION: Cytoplasm. Nucleus, PML body.cellular protein metabolic process [GO:0044267]; formation of translation preinitiation complex [GO:0001731]; gene expression [GO:0010467]; negative regulation of translational initiation [GO:0045947]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]~poly(A) RNA binding [GO:0044822]; protein N-terminus binding [GO:0047485]; translation initiation factor activity [GO:0003743]Ucytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins. {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:17310990, ECO:0000269|PubMed:17324924, ECO:0000269|PubMed:17468741}.Q969X1LFG3Protein lifeguard 3SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000269|PubMed:16607040}. Endosome membrane {ECO:0000269|PubMed:16607040}.vnegative regulation of establishment of protein localization to plasma membrane [GO:0090005]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of Fas signaling pathway [GO:1902045]; negative regulation of metalloenzyme activity [GO:0048553]; positive regulation of blood vessel remodeling [GO:2000504]endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]FUNCTION: Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling.Q6NYC8PPR18 PhostensinSUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24434620}.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17374523}.FUNCTION: Isoform 1: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000269|PubMed:24434620}.; FUNCTION: Isoform 4: May target protein phosphatase 1 to F-actin cytoskeleton. {ECO:0000269|PubMed:17374523}.P41240CSKTyrosine-protein kinase CSKSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Mainly cytoplasmic, also present in lipid rafts. {ECO:0000250}.adherens junction organization [GO:0034332]; blood coagulation [GO:0007596]; brain development [GO:0007420]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to peptide hormone stimulus [GO:0071375]; epidermal growth factor receptor signaling pathway [GO:0007173]; innate immune response [GO:0045087]; morphogenesis of an epithelium [GO:0002009]; negative regulation of bone resorption [GO:0045779]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of Golgi to plasma membrane protein transport [GO:0042997]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of kinase activity [GO:0033673]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of phagocytosis [GO:0050765]; oligodendrocyte differentiation [GO:0048709]; peptidyl-tyrosine autophosphorylation [GO:0038083]; platelet activation [GO:0030168]; positive regulation of MAP kinase activity [GO:0043406]; protein phosphorylation [GO:0006468]; regulation of cell proliferation [GO:0042127]; regulation of cytokine production [GO:0001817]; regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060368]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]5ATP binding [GO:0005524]; identical protein binding [GO:0042802]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein C-terminus binding [GO:0008022]; protein kinase A catalytic subunit binding [GO:0034236]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]nFUNCTION: Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail pho< sphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK. {ECO:0000269|PubMed:1639064, ECO:0000269|PubMed:9281320}.Q13247SRSF6&Serine/arginine-rich splicing factor 6Kalternative mRNA splicing, via spliceosome [GO:0000380]; gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cell death [GO:0060548]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of epithelial cell proliferation involved in lung morphogenesis [GO:0060501]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of keratinocyte proliferation [GO:0010837]; regulation of wound healing [GO:0061041]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]znucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723]4nuclear speck [GO:0016607]; nucleoplasm [GO:0005654] FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing. {ECO:0000269|PubMed:12549914, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:24440982}.Q9UPU7TBD2BTBC1 domain family member 2B@FUNCTION: May act as a GTPase-activating protein. {ECO:0000250}.Q9H4M9EHD1EH domain-containing protein 1XSUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:23596323}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:15020713}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9WVK4}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially associates with tubular recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:19864458, PubMed:23596323). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (By similarity). Localizes to the ciliary pocket from where the cilium protrudes (PubMed:25686250). {ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:23596323, ECO:0000269|PubMed:25686250}.$blood coagulation [GO:0007596]; cellular response to nerve growth factor stimulus [GO:1990090]; cholesterol homeostasis [GO:0042632]; endocytic recycling [GO:0032456]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; low-density lipoprotein particle clearance [GO:0034383]; neuron projection development [GO:0031175]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of myoblast fusion [GO:1901741]; protein homooligomerization [GO:0051260]uATP binding [GO:0005524]; calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; Rab GTPase binding [GO:0017137]early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; lipid particle [GO:0005811]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet dense tubular network membrane [GO:0031095]; recycling endosome membrane [GO:0055038]FUNCTION: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Also plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis (PubMed:25686250). {ECO:0000250|UniProtKB:Q641Z6, ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:20801876, ECO:0000269|PubMed:25686250}.Q9Y5A7NUB1NEDD8 ultimate buster 1XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11259415}. Note=Predominantly nuclear.positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein ubiquitination [GO:0016567]; response to interferon-gamma [GO:0034341]; response to tumor necrosis factor [GO:0034612]; ubiquitin-dependent protein catabolic process [GO:0006511]FUNCTION: Specific down-regulator of the NEDD8 conjugation system. Recruits NEDD8, UBD, and their conjugates to the proteasome for degradation. Isoform 1 promotes the degradation of NEDD8 more efficiently than isoform 2. {ECO:0000269|PubMed:16707496}.P40818UBP8'Ubiquitin carboxyl-terminal hydrolase 8SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein.cell proliferation [GO:0008283]; endosome organization [GO:0007032]; mitotic cytokinesis [GO:0000281]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; Ras protein signal transduction [GO:0007265]; regulation of proteasomal protein catabolic process [GO:0061136]dcysteine-type endopeptidase activity [GO:0004197]; ubiquitin-specific protease activity [GO:0004843]#acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extrinsic component of endosome membrane [GO:0031313]; extrinsic component of plasma membrane [GO:0019897]; Golgi apparatus [GO:0005794]; midbody [GO:0030496]; nucleoplasm [GO:0005654]FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. {ECO:0000269|PubMed:16520378, ECO:0000269|PubMed:17711858, ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:9628861}.Q9NTI5PDS5B0Sister chromatid cohesion protein PDS5 homolog B=SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.cell division [< GO:0051301]; cell proliferation [GO:0008283]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of cell proliferation [GO:0008285]; regulation of cell proliferation [GO:0042127]2ATP binding [GO:0005524]; DNA binding [GO:0003677]chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells. {ECO:0000269|PubMed:10963680, ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19696148}.Q13126MTAP'S-methyl-5'-thioadenosine phosphorylaseKSUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.cellular nitrogen compound metabolic process [GO:0034641]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; nucleobase-containing compound metabolic process [GO:0006139]; polyamine metabolic process [GO:0006595]; purine-containing compound salvage [GO:0043101]; purine ribonucleoside salvage [GO:0006166]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]aphosphorylase activity [GO:0004645]; S-methyl-5-thioadenosine phosphorylase activity [GO:0017061]FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. {ECO:0000255|HAMAP-Rule:MF_03155, ECO:0000269|PubMed:3091600}.P35555FBN1 Fibrillin-1iSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P98133}.anatomical structure morphogenesis [GO:0009653]; camera-type eye development [GO:0043010]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to transforming growth factor beta stimulus [GO:0071560]; embryonic eye morphogenesis [GO:0048048]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; heart development [GO:0007507]; metanephros development [GO:0001656]; post-embryonic eye morphogenesis [GO:0048050]; regulation of cellular response to growth factor stimulus [GO:0090287]; sequestering of BMP in extracellular matrix [GO:0035582]; sequestering of TGFbeta in extracellular matrix [GO:0035583]; skeletal system development [GO:0001501]calcium ion binding [GO:0005509]; extracellular matrix constituent conferring elasticity [GO:0030023]; extracellular matrix structural constituent [GO:0005201]; integrin binding [GO:0005178]; protein complex binding [GO:0032403]basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; microfibril [GO:0001527]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively. {ECO:0000269|PubMed:15062093}.Q8N1G2CMTR18Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18533109, ECO:0000269|PubMed:21310715}.n7-methylguanosine mRNA capping [GO:0006370]; cap1 mRNA methylation [GO:0097309]; mRNA methylation [GO:0080009]bmRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; nucleic acid binding [GO:0003676] FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. {ECO:0000269|PubMed:18533109, ECO:0000269|PubMed:20713356, ECO:0000269|PubMed:21310715}.P20839IMDH1(Inosine-5'-monophosphate dehydrogenase 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:14766016}.GMP biosynthetic process [GO:0006177]; lymphocyte proliferation [GO:0046651]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to cold [GO:0009409]; retina development in camera-type eye [GO:0060041]; small molecule metabolic process [GO:0044281]DNA binding [GO:0003677]; IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]xcell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.Q13619CUL4A Cullin-4Acell cycle arrest [GO:0007050]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; hemopoiesis [GO:0030097]; intrinsic apoptotic signaling pathway [GO:0097193]; in utero embryonic development [GO:0001701]; negative regulation of cell proliferation [GO:0008285]; negative regulation of granulocyte differentiation [GO:0030853]; positive regulation of cell proliferation [GO:0008284]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of DNA damage checkpoint [GO:2000001]; regulation of nucleotide-excision repair [GO:2000819]; regulation of protein metabolic process [GO:0051246]; somatic stem cell maintenance [GO:0035019]; translesion synthesis [GO:0019985]; viral process [GO:0016032]Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; nucleoplasm [GO:0005654]FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 fr< om ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL. {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:14609952, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15548678, ECO:0000269|PubMed:16537899, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24209620}.O60266ADCY3Adenylate cyclase type 3activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; female meiotic division [GO:0007143]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; neurotrophin TRK receptor signaling pathway [GO:0048011]; renal water homeostasis [GO:0003091]; sensory perception of smell [GO:0007608]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; water transport [GO:0006833]adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; metal ion binding [GO:0046872]cilium [GO:0005929]; cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]cFUNCTION: Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration.Q5XKP0QIL1 Protein QIL1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25997101}; Single-pass membrane protein {ECO:0000255}. Note=Enriched at crista junctions. {ECO:0000269|PubMed:25997101}.qMICOS complex [GO:0061617]; mitochondrial crista junction [GO:0044284]; mitochondrial inner membrane [GO:0005743]FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MINOS1/MIC10 into the MICOS complex. {ECO:0000269|PubMed:25997101}.Q9UBR2CATZ Cathepsin Zangiotensin maturation [GO:0002003]; cellular protein metabolic process [GO:0044267]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]`cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; plasma membrane [GO:0005886]QFUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity.Q8N573OXR1Oxidation resistance protein 1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15060142}.adult walking behavior [GO:0007628]; cellular response to hydroperoxide [GO:0071447]; negative regulation of neuron apoptotic process [GO:0043524]; response to oxidative stress [GO:0006979]2mitochondrion [GO:0005739]; nucleolus [GO:0005730]zFUNCTION: May be involved in protection from oxidative damage. {ECO:0000269|PubMed:11114193, ECO:0000269|PubMed:15060142}.Q9NTJ5SAC1&Phosphatidylinositide phosphatase SAC1phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]phosphatase activity [GO:0016791]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; phosphatidylinositol-4-phosphate phosphatase activity [GO:0043812]; phosphatidylinositol bisphosphate phosphatase activity [GO:0034593]alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [GO:0032281]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of endoplasmic reticulum membrane [GO:0030176]FUNCTION: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2 (By similarity). {ECO:0000250}.Q8TCD1CR032UPF0729 protein C18orf32WFUNCTION: May activate the NF-kappa-B signaling pathway. {ECO:0000269|PubMed:12761501}.Q9Y678COPG1Coatomer subunit gamma-19SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11056392}. Golgi apparatus membrane {ECO:0000269|PubMed:11056392}; Peripheral membrane protein {ECO:0000269|PubMed:11056392}; Cytoplasmic side {ECO:0000269|PubMed:11056392}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Predominantly located in the cis-Golgi apparatus. {ECO:0000250}.#COPI coating of Golgi vesicle [GO:0048205]; establishment of Golgi localization [GO:0051683]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; organelle transport along microtubule [GO:0072384]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]QCOPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi membrane [GO:0000139] FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity). {ECO:0000250}.Q9HAB8PPCS$Phosphopantothenate--cysteine ligasecoenzyme A biosynthetic process [GO:0015937]; coenzyme biosynthetic process [GO:0009108]; pantothenate metabolic process [GO:0015939]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]:phosphopantothenate--cysteine ligase activity [GO:0004632]FUNCTION: Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. {ECO:0000269|PubMed:11923312, ECO:0000269|PubMed:12906824}.O43242PSMD3.26S proteasome non-ATPase regulatory subunit 3vanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I,< TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032] cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.P98182ZN200Zinc finger protein 200Ametal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]/FUNCTION: Could have a role in spermatogenesis.Q9BRK0REEP2'Receptor expression-enhancing protein 2Nendoplasmic reticulum tubular network organization [GO:0071786]; positive regulation of defense response to virus by host [GO:0002230]; protein transport into membrane raft [GO:0032596]; regulation of intracellular transport [GO:0032386]; sensory perception of bitter taste [GO:0050913]; sensory perception of sweet taste [GO:0050916]cytoplasmic microtubule [GO:0005881]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]FUNCTION: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling. May enhance the cell surface expression of odorant receptors (By similarity). {ECO:0000250}.Q969M1TM40L,Mitochondrial import receptor subunit TOM40BlSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.:ion transport [GO:0006811]; protein transport [GO:0015031]porin activity [GO:0015288]bmitochondrial outer membrane [GO:0005741]; pore complex [GO:0046930]; protein complex [GO:0043234]xFUNCTION: Potential channel-forming protein implicated in import of protein precursors into mitochondria. {ECO:0000250}.O75448MED246Mediator of RNA polymerase II transcription subunit 24androgen receptor signaling pathway [GO:0030521]; gene expression [GO:0010467]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of transcription, DNA-templated [GO:0045893]; protein heterooligomerization [GO:0051291]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; stem cell maintenance [GO:0019827]; transcription initiation from RNA polymerase II promoter [GO:0006367]histone acetyltransferase activity [GO:0004402]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; receptor activity [GO:0004872]; RNA polymerase II transcription cofactor activity [GO:0001104]; thyroid hormone receptor binding [GO:0046966]; transcription cofactor activity [GO:0003712]; ubiquitin protein ligase activity [GO:0061630]; vitamin D receptor binding [GO:0042809]tmediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]DFUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:16595664}.P28845DHI1.Corticosteroid 11-beta-dehydrogenase isozyme 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10497248}; Single-pass type II membrane protein {ECO:0000269|PubMed:10497248}.glucocorticoid biosynthetic process [GO:0006704]; lung development [GO:0030324]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]11-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0070524]; 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity [GO:0003845]DFUNCTION: Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7-ketocholesterol to 7-beta-hydroxycholesterol (By similarity). {ECO:0000250}.Q12999TSN31Tetraspanin-316positive regulation of cell proliferation [GO:0008284]Iintegral component of plasma membrane [GO:0005887]; membrane [GO:0016020]Q9BVQ7SPA5L3Spermatogenesis-associated protein 5-like protein 1O75170PP6R2;Serine/threonine-protein phosphatase 6 regulatory subunit 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727}.Mcytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. {ECO:0000269|PubMed:16769727}.Q96I59SYNM/Probable asparagine--tRNA ligase, mitochondrialP53634CATCDipeptidyl peptidase 1"activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; aging [GO:0007568]; immune response [GO:0006955]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of peptidase activity [GO:0010952]; positive regulation of proteolysis involved in cellular protein catabolic process [GO:1903052]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; response to organic substance [GO:0010033]; T cell mediated cytotoxicity [GO:0001913]Qchaperone binding [GO:0051087]; chloride ion binding [GO:0031404]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; phosphatase binding [GO:0019902]; serine-type endopeptidase activity [GO:0004252]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane [GO:0016020]FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. {ECO:0000269|PubMed:1586157}.Q9H0W8SMG9 Protein SMG9ngene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO< :0000184]UFUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8. {ECO:0000269|PubMed:19417104}.P24752THIL+Acetyl-CoA acetyltransferase, mitochondrialadipose tissue development [GO:0060612]; brain development [GO:0007420]; branched-chain amino acid catabolic process [GO:0009083]; cellular ketone body metabolic process [GO:0046950]; cellular lipid metabolic process [GO:0044255]; cellular nitrogen compound metabolic process [GO:0034641]; ketone body biosynthetic process [GO:0046951]; ketone body catabolic process [GO:0046952]; liver development [GO:0001889]; metanephric proximal convoluted tubule development [GO:0072229]; protein homooligomerization [GO:0051260]; response to hormone [GO:0009725]; response to organic cyclic compound [GO:0014070]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]sacetyl-CoA C-acetyltransferase activity [GO:0003985]; coenzyme binding [GO:0050662]; metal ion binding [GO:0046872]7FUNCTION: Plays a major role in ketone body metabolism.Q9BVA6FICD0Adenosine monophosphate-protein transferase FICDWnegative regulation of GTPase activity [GO:0034260]; protein adenylylation [GO:0018117]KATP binding [GO:0005524]; protein adenylyltransferase activity [GO:0070733]FUNCTION: Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified. {ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:22266942}.P06400RB!Retinoblastoma-associated proteinProliferating regulator(2)<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255}.S androgen receptor signaling pathway [GO:0030521]; cell cycle arrest [GO:0007050]; cell cycle checkpoint [GO:0000075]; cell division [GO:0051301]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006338]; digestive tract development [GO:0048565]; enucleate erythrocyte differentiation [GO:0043353]; G1/S transition of mitotic cell cycle [GO:0000082]; glial cell apoptotic process [GO:0034349]; hepatocyte apoptotic process [GO:0097284]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; myoblast differentiation [GO:0045445]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter during mitosis [GO:0007070]; negative regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0071930]; neuron apoptotic process [GO:0051402]; neuron maturation [GO:0042551]; neuron projection development [GO:0031175]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein localization to chromosome, centromeric region [GO:0071459]; Ras protein signal transduction [GO:0007265]; regulation of centromere complex assembly [GO:0090230]; regulation of cohesin localization to chromatin [GO:0071922]; regulation of lipid kinase activity [GO:0043550]; regulation of mitotic cell cycle [GO:0007346]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; sister chromatid biorientation [GO:0031134]; skeletal muscle cell differentiation [GO:0035914]; striated muscle cell differentiation [GO:0051146]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]androgen receptor binding [GO:0050681]; core promoter binding [GO:0001047]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; phosphoprotein binding [GO:0051219]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Rb-E2F complex [GO:0035189]; spindle [GO:0005819]; SWI/SNF complex [GO:0016514][FUNCTION: Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. {ECO:0000250, ECO:0000269|PubMed:15084261}.Q05209PTN121Tyrosine-protein phosphatase non-receptor type 124SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35831}. Cell junction, focal adhesion {ECO:0000269|PubMed:18559503}. Cell projection, podosome {ECO:0000250|UniProtKB:P35831}. Note=Partial translocation to focal adhesion sites may be mediated by interaction with SORBS2. {ECO:0000269|PubMed:18559503}.zpeptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]; tissue regeneration [GO:0042246]inon-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; SH3 domain binding [GO:0017124]cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; podosome [GO:0002102]FUNCTION: Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. {ECO:0000269|PubMed:17329398}.Q9H1K1ISCU7Iron-sulfur cluster assembly enzyme ISCU, mitochondrialeSUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. [2Fe-2S] cluster assembly [GO:0044571]; cellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; nitrogen fixation [GO:0009399]; protein maturation by iron-sulfur cluster transfer [GO:0097428]; small molecule metabolic process [GO:0044281]2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; ferrous iron binding [GO:0008198]; iron ion binding [GO:0005506]; iron-sulfur transferase activity [GO:0036455]; protein complex scaffold [GO:0032947]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Involved in the assembly or repair < of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron. {ECO:0000269|PubMed:11060020}.Q8N108MIER1+Mesoderm induction early response protein 1SUBCELLULAR LOCATION: Isoform 1: Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Nucleus.; SUBCELLULAR LOCATION: Isoform 3: Nucleus.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.positive regulation of chromatin silencing [GO:0031937]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; transcription, DNA-templated [GO:0006351]ADNA binding [GO:0003677]; signal transducer activity [GO:0004871]`cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; transcriptional repressor complex [GO:0017053]FUNCTION: Transcriptional repressor regulating the expression of a number of genes including SP1 target genes. Probably functions through recruitment of HDAC1 a histone deacetylase involved in chromatin silencing. {ECO:0000269|PubMed:12482978}.Q9BW83IFT27+Intraflagellar transport protein 27 homologLSUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:25443296}.intracellular protein transport [GO:0006886]; intraciliary transport [GO:0042073]; organelle organization [GO:0006996]; Rab protein signal transduction [GO:0032482]; smoothened signaling pathway [GO:0007224]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514]; primary cilium [GO:0072372]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228]FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B that promotes the exit of the BBSome complex from cilia via its interaction with ARL6 (PubMed:25443296). Not involved in entry of the BBSome complex into cilium. Prevents aggregation of GTP-free ARL6 (PubMed:25443296). Required for hedgehog signaling. Forms a subcomplex within the IFT complex B with IFT25 (By similarity). {ECO:0000250|UniProtKB:A8HN58, ECO:0000269|PubMed:25443296}.Q6P1N0C2D1A/Coiled-coil and C2 domain-containing protein 1Anegative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]IFUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses (By similarity). Plays distinct roles depending on its localization. When cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway. Repressor of HTR1A when nuclear. In the centrosome, regulates spindle pole localization of the cohesin subunit SCC1/RAD21, thereby mediating centriole cohesion during mitosis. {ECO:0000250, ECO:0000269|PubMed:20171170}.Q16394EXT1 Exostosin-1SSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000269|PubMed:10679296}. Golgi apparatus membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000269|PubMed:10679296}. Note=The EXT1/EXT2 complex is localized in the Golgi apparatus. axon guidance [GO:0007411]; carbohydrate metabolic process [GO:0005975]; cellular polysaccharide biosynthetic process [GO:0033692]; embryonic skeletal joint development [GO:0072498]; endoderm development [GO:0007492]; gastrulation [GO:0007369]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; mesoderm development [GO:0007498]; olfactory bulb development [GO:0021772]; ossification [GO:0001503]; protein glycosylation [GO:0006486]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]2acetylglucosaminyltransferase activity [GO:0008375]; glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0050508]; glucuronosyltransferase activity [GO:0015020]; heparan sulfate N-acetylglucosaminyltransferase activity [GO:0042328]; metal ion binding [GO:0046872]; N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity [GO:0050509]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; transferase activity, transferring glycosyl groups [GO:0016757]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. {ECO:0000269|PubMed:11518722}.Q13948CASP Protein CASPSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12429822}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12429822}.3intra-Golgi vesicle-mediated transport [GO:0006891]1integral component of Golgi membrane [GO:0030173]]FUNCTION: May be involved in intra-Golgi retrograde transport. {ECO:0000269|PubMed:15718469}.Q92945FUBP2&Far upstream element-binding protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19198587}. Cytoplasm {ECO:0000269|PubMed:19198587}. Note=A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites. {ECO:0000250}.mgene expression [GO:0010467]; mRNA catabolic process [GO:0006402]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; regulation of miRNA metabolic process [GO:2000628]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; transcription, DNA-templated [GO:0006351]UDNA binding [GO:0003677]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]ncytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs. {ECO:0000250, ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:8940189, ECO:0000269|PubMed:9136930}.P39656OST48MDolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunitZSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; innate immune response [GO:0045087]; pos< t-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; response to cytokine [GO:0034097]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; T cell activation [GO:0042110]; translation [GO:0006412]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]; protein complex [GO:0043234]Q9NWS0PIHD1 PIH1 domain-containing protein 1(box C/D snoRNP assembly [GO:0000492]; epithelial cell differentiation [GO:0030855]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]:pre-snoRNP complex [GO:0070761]; R2TP complex [GO:0097255]HFUNCTION: Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles (PubMed:17636026). Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription (PubMed:22368283, PubMed:24036451). Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1 (PubMed:20864032). Positively regulates the assembly and activity of the mTORC1 complex (PubMed:24036451). {ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:22368283, ECO:0000269|PubMed:24036451}.Q8NBN7RDH13Retinol dehydrogenase 13eye photoreceptor cell development [GO:0042462]; response to high light intensity [GO:0009644]; retina layer formation [GO:0010842])mitochondrial inner membrane [GO:0005743]IFUNCTION: Does not exhibit retinol dehydrogenase (RDH) activity in vitro.Q6PML9ZNT9Zinc transporter 9SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10409434}.nucleotide-excision repair [GO:0006289]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]; zinc II ion transport [GO:0006829]cation transmembrane transporter activity [GO:0008324]; chromatin binding [GO:0003682]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; sequence-specific DNA binding transcription factor activity [GO:0003700]\cytoskeleton [GO:0005856]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]FUNCTION: Plays a role in the p160 coactivator signaling pathway that mediates transcriptional activation by nuclear receptors. Plays a role in transcriptional activation of Wnt-responsive genes. {ECO:0000250}.Q92545TM131Transmembrane protein 1310regulation of immune system process [GO:0002682]SFUNCTION: May play a role in the immune response to viral infection. {ECO:0000250}.Q92530PSMF1!Proteasome inhibitor PI31 subunitsSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18495667}. Endoplasmic reticulum {ECO:0000269|PubMed:18495667}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of proteasomal protein catabolic process [GO:1901799]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]Nendopeptidase inhibitor activity [GO:0004866]; proteasome binding [GO:0070628]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; proteasome core complex [GO:0005839]FUNCTION: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28. {ECO:0000269|PubMed:10764772}.Q9BRK5CAB4545 kDa calcium-binding proteinSUBCELLULAR LOCATION: Isoform 1: Golgi apparatus lumen {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Cell projection, bleb. Note=Isoform 5 colocalizes with STX3 and STXBP1 isoform 2 at the plasma membrane and cell surface blebs.calcium ion-dependent exocytosis [GO:0017156]; cerebellum development [GO:0021549]; fat cell differentiation [GO:0045444]; response to ethanol [GO:0045471]; UV protection [GO:0009650]; zymogen granule exocytosis [GO:0070625]Hcalcium ion binding [GO:0005509]; identical protein binding [GO:0042802]bleb [GO:0032059]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]; late endosome [GO:0005770]; membrane [GO:0016020]FUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. {ECO:0000250}.; FUNCTION: Isoform 5 may be involved in the exocytosis of zymogens by pancreatic acini.P49674KC1ECasein kinase I isoform epsiloncellular protein localization [GO:0034613]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA repair [GO:0006281]; endocytosis [GO:0006897]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; negative regulation of Wnt signaling pathway [GO:0030178]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; regulation of circadian rhythm [GO:0042752]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]jcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation. {ECO:0000269|PubMed:12556519, ECO:0000269|PubMed:15070676, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:16790549}.Q7Z6Z7HUWE1!E3 ubiquitin-protein ligase HUWE1jSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|P< ubMed:19713937}. Nucleus {ECO:0000269|PubMed:19713937}. Note=Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells (By similarity). Predominantly cytosolic or perinuclear in some colorectal carcinoma cells. {ECO:0000250|UniProtKB:Q7TMY8}.bbase-excision repair [GO:0006284]; cell differentiation [GO:0030154]; histone ubiquitination [GO:0016574]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]DNA binding [GO:0003677]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of isoform 2 of PA2G4. {ECO:0000269|PubMed:15567145, ECO:0000269|PubMed:15767685, ECO:0000269|PubMed:15989956, ECO:0000269|PubMed:15989957, ECO:0000269|PubMed:17567951, ECO:0000269|PubMed:18488021, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19713937}.O15027SC16A Protein transport protein Sec16A6SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation.COPII vesicle coating [GO:0048208]; endoplasmic reticulum organization [GO:0007029]; protein transport [GO:0015031]; substantia nigra development [GO:0021762]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]FUNCTION: Defines endoplasmic reticulum exit sites (ERES) and is required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for normal transitional endoplasmic reticulum (tER) organization. {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411}.O75954TSN9 Tetraspanin-9SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalizes with GP6 in tetraspanin microdomains on the platelet surface. {ECO:0000250}.focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197]Q24JP5T132ATransmembrane protein 132ASUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity). {ECO:0000250}.Q12888TP53B&Tumor suppressor p53-binding protein 1 Other related}SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores. Both nuclear and cytoplasmic in some cells. Recruited to sites of DNA damage, such as double stand breaks. H4K20me2 is required for efficient localization to double strand breaks and removal of proteins that have a high affinity for H4K20me2 such as L3MBTL1 and KDM4A is needed.cellular response to DNA damage stimulus [GO:0006974]; cellular response to X-ray [GO:0071481]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]damaged DNA binding [GO:0003684]; methylated histone binding [GO:0035064]; p53 binding [GO:0002039]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II transcription cofactor activity [GO:0001104]; telomeric DNA binding [GO:0042162]condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; nuclear chromosome, telomeric region [GO:0000784]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]FUNCTION: Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53-mediated transcriptional activation. {ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835}.O43488ARK72(Aflatoxin B1 aldehyde reductase member 2\SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:9576847}.carbohydrate metabolic process [GO:0005975]; cellular aldehyde metabolic process [GO:0006081]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; electron carrier activity [GO:0009055]; phenanthrene-9,10-epoxide hydrolase activity [GO:0019119]rcytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]FUNCTION: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:17591773, ECO:0000269|PubMed:9576847}.O00506STK25"Serine/threonine-protein kinase 25SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15037601}. Golgi apparatus {ECO:0000269|PubMed:15037601}. Note=Localizes to the Golgi apparatus.Mactivation of protein kinase activity [GO:0032147]; establishment of Golgi localization [GO:0051683]; establishment or maintenance of cell polarity [GO:0007163]; Golgi localization [GO:0051645]; Golgi reassembly [GO:0090168]; intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:0036481]; positive regulation of axonogenesis [GO:0050772]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; response to hydrogen peroxide [GO:0042542]; response to oxidative stress [GO:0006979]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; str< ess-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]Wcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]1FUNCTION: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration. {ECO:0000269|PubMed:15037601}.Q8NCC3PAG15Group XV phospholipase A2 lipases(2)USUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Secreted {ECO:0000269|PubMed:10092508}.ceramide metabolic process [GO:0006672]; fatty acid catabolic process [GO:0009062]; phosphatidylcholine metabolic process [GO:0046470]calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]; O-acyltransferase activity [GO:0008374]; phospholipid binding [GO:0005543]Uextracellular exosome [GO:0070062]; lysosome [GO:0005764]; mitochondrion [GO:0005739]FUNCTION: Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N-acetylsphingosine and the concomitant release of a lyso-phospholipid (By similarity). May have weak lysophospholipase activity. {ECO:0000250}.P07910HNRPC.Heterogeneous nuclear ribonucleoproteins C1/C2ASUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.3'-UTR-mediated mRNA stabilization [GO:0070935]; ATP-dependent chromatin remodeling [GO:0043044]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; RNA splicing [GO:0008380]identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; N6-methyladenosine-containing RNA binding [GO:1990247]; nucleosomal DNA binding [GO:0031492]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980] catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; spliceosomal complex [GO:0005681]FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs that affects mRNA splicing, processing and stability. M6A alters the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch' to facilitate binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). {ECO:0000269|PubMed:12509468, ECO:0000269|PubMed:16010978, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:7567451, ECO:0000269|PubMed:8264621}.P15311EZRIEzrinSUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cell projection {ECO:0000269|PubMed:18046454}. Cell projection, microvillus membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cell projection, ruffle membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18046454}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18046454}. Note=Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side). {ECO:0000250}.actin cytoskeleton reorganization [GO:0031532]; actin filament bundle assembly [GO:0051017]; astral microtubule organization [GO:0030953]; axon guidance [GO:0007411]; cellular protein complex localization [GO:0034629]; cellular response to cAMP [GO:0071320]; cortical microtubule organization [GO:0043622]; cytoskeletal anchoring at plasma membrane [GO:0007016]; establishment of centrosome localization [GO:0051660]; establishment of endothelial barrier [GO:0061028]; establishment of protein localization to plasma membrane [GO:0090002]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; filopodium assembly [GO:0046847]; intestinal D-glucose absorption [GO:0001951]; leukocyte cell-cell adhesion [GO:0007159]; membrane to membrane docking [GO:0022614]; microvillus assembly [GO:0030033]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-2 secretion [GO:1900041]; negative regulation of p38MAPK cascade [GO:1903753]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of gene expression [GO:0010628]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of protein localization to early endosome [GO:1902966]; positive regulation of protein secretion [GO:0050714]; protein kinase A signaling [GO:0010737]; protein localization to cell cortex [GO:0072697]; receptor internalization [GO:0031623]; regulation of cell shape [GO:0008360]; regulation of microvillus length [GO:0032532]; regulation of organelle assembly [GO:1902115]; sphingosine-1-phosphate signaling pathway [GO:0003376]; terminal web assembly [GO:1902896]actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATPase binding [GO:0051117]; cell adhesion molecule binding [GO:0050839]; microtubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; S100 protein binding [GO:0044548]actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; astrocyte projection [GO:0097449]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; cell body [GO:0044297]; cell periphery [GO:0071944]; cell projection [GO:0042995]; cell tip [GO:0051286]; ciliary basal body [GO:0036064]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; cytoplasmic side of apical plasma membrane [GO:0098592]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of membrane [GO:0019898]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; membrane [GO:0016020]; microspike [GO:0044393]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; Schwann cell microvillus [GO:0097454]; T-tubule [GO:0030315]; uropod [GO:0001931]; vesicle [GO:0031982]]FUNCTION: Probably involved in conn< ections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. {ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:18270268, ECO:0000269|PubMed:19111582}.Q14677EPN4Clathrin interactor 1RSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Note=Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network.pendocytosis [GO:0006897]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]9clathrin binding [GO:0030276]; lipid binding [GO:0008289]clathrin-coated vesicle [GO:0030136]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}.Q8ND24RN214RING finger protein 214P06730IF4E+Eukaryotic translation initiation factor 4E_SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:20616046}. Cytoplasm {ECO:0000250}.behavioral fear response [GO:0001662]; cellular protein metabolic process [GO:0044267]; cytokine-mediated signaling pathway [GO:0019221]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; mRNA export from nucleus [GO:0006406]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of mitotic cell cycle [GO:0045931]; regulation of translation [GO:0006417]; stem cell maintenance [GO:0019827]; translation [GO:0006412]; translational initiation [GO:0006413]; viral process [GO:0016032]enzyme binding [GO:0019899]; eukaryotic initiation factor 4G binding [GO:0031370]; poly(A) RNA binding [GO:0044822]; repressing transcription factor binding [GO:0070491]; RNA cap binding [GO:0000339]; translation initiation factor activity [GO:0003743]xchromatoid body [GO:0033391]; cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; extracellular exosome [GO:0070062]; mRNA cap binding complex [GO:0005845]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap. {ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813}.Q96BZ9TBC20TBC1 domain family member 20cacrosome assembly [GO:0001675]; cargo loading into COPII-coated vesicle [GO:0090110]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; lens fiber cell morphogenesis [GO:0070309]; lipid particle organization [GO:0034389]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation by virus of viral protein levels in host cell [GO:0046726]; positive regulation of ER to Golgi vesicle-mediated transport [GO:1902953]; positive regulation of GTPase activity [GO:0043547]; seminiferous tubule development [GO:0072520]; virion assembly [GO:0019068]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of Golgi membrane [GO:0030173]; nuclear membrane [GO:0031965]FUNCTION: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude.Q9HAN9NMNA11Nicotinamide mononucleotide adenylyltransferase 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11248244, ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:22842230}.NAD biosynthetic process [GO:0009435]; NAD metabolic process [GO:0019674]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; nicotinamide-nucleotide adenylyltransferase activity [GO:0000309]; nicotinate-nucleotide adenylyltransferase activity [GO:0004515]FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following mechanical or toxic insults. {ECO:0000269|PubMed:17402747}.Q9BQ39DDX50 ATP-dependent RNA helicase DDX50.RNA secondary structure unwinding [GO:0010501]Kmembrane [GO:0016020]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]Q8IZV5RDH10Retinol dehydrogenase 10 Cofactor metabolismSUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.bud elongation involved in lung branching [GO:0060449]; ear development [GO:0043583]; embryonic camera-type eye development [GO:0031076]; embryonic forelimb morphogenesis [GO:0035115]; embryonic viscerocranium morphogenesis [GO:0048703]; gonad development [GO:0008406]; in utero embryonic development [GO:0001701]; metanephros development [GO:0001656]; neural crest cell development [GO:0014032]; nose development [GO:0043584]; phototransduction, visible light [GO:0007603]; primary lung bud formation [GO:0060431]; retinal metabolic process [GO:0042574]; retinoic acid biosynthetic process [GO:0002138]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; visual perception [GO:0007601]cell body [GO:0044297]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]FUNCTION: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol. {ECO:0000269|PubMed:12407145}.Q13586STIM1Stromal interaction molecule 1STIMSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. Associated with the microtubule network at the growing distal tip of microtubules.activation of store-operated calcium channel activity [GO:0032237]; blood coagulation [GO:0007596]; calcium ion transport [GO:0006816]; detection of calcium ion [GO:0005513]; enamel mineralization [GO:0070166]; regulation of calcium ion transport [GO:0051924]calcium channel regulator acti< vity [GO:0005246]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; microtubule plus-end binding [GO:0051010]; protease binding [GO:0002020] cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of plasma membrane [GO:0005887]; microtubule [GO:0005874]EFUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1. Involved in enamel formation. {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671}.Q9BU61NDUF3DNADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3hSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion inner membrane {ECO:0000269|PubMed:19463981}.?mitochondrial respiratory chain complex I assembly [GO:0032981]?mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]FUNCTION: Essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000269|PubMed:19463981}.P07437TBB5Tubulin beta chaincell division [GO:0051301]; cellular process [GO:0009987]; cytoskeleton-dependent intracellular transport [GO:0030705]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; movement of cell or subcellular component [GO:0006928]; natural killer cell mediated cytotoxicity [GO:0042267]; organelle organization [GO:0006996]; protein polymerization [GO:0051258]; spindle assembly [GO:0051225]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; MHC class I protein binding [GO:0042288]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]; ubiquitin protein ligase binding [GO:0031625]cell body [GO:0044297]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; nuclear envelope lumen [GO:0005641]; nucleus [GO:0005634]Q16666IF16%Gamma-interferon-inducible protein 16%SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Localizes in the nucleus during human herpes simplex virus 1 (HHV-1) infection.activation of cysteine-type endopeptidase activity [GO:0097202]; activation of innate immune response [GO:0002218]; autophagy [GO:0006914]; cell proliferation [GO:0008283]; cellular response to glucose starvation [GO:0042149]; cellular response to ionizing radiation [GO:0071479]; defense response to virus [GO:0051607]; hemopoiesis [GO:0030097]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; monocyte differentiation [GO:0030224]; myeloid cell differentiation [GO:0030099]; negative regulation of cysteine-type endopeptidase activity [GO:2000117]; negative regulation of DNA binding [GO:0043392]; negative regulation of innate immune response [GO:0045824]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of viral genome replication [GO:0045071]; positive regulation of cytokine production [GO:0001819]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of autophagy [GO:0010506]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]core promoter binding [GO:0001047]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:24198334, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9642285}.Q92692PVRL2Nectin-2ISUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.acrosome assembly [GO:0001675]; adherens junction organization [GO:0034332]; adhesion of symbiont to host [GO:0044406]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell part morphogenesis [GO:0032990]; cell recognition [GO:0008037]; cilium organization [GO:0044782]; coreceptor-mediated virion attachment to host cell [GO:0046814]; cytoskeleton organization [GO:0007010]; establishment of mitochondrion localization [GO:0051654]; fertilization [GO:0009566]; fusion of virus membrane with host plasma membrane [GO:0019064]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molec< ules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of immunoglobulin mediated immune response [GO:0002891]; positive regulation of mast cell activation [GO:0033005]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002860]; regulation of immune response [GO:0050776]; regulation of viral entry into host cell [GO:0046596]; signal transduction [GO:0007165]; spermatid development [GO:0007286]; spermatid nucleus differentiation [GO:0007289]; sperm mitochondrion organization [GO:0030382]; susceptibility to natural killer cell mediated cytotoxicity [GO:0042271]; susceptibility to T cell mediated cytotoxicity [GO:0060370]cell adhesion molecule binding [GO:0050839]; coreceptor activity [GO:0015026]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; virus receptor activity [GO:0001618]Bcell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; zonula adherens [GO:0005915]GFUNCTION: Probable cell adhesion protein. {ECO:0000269|PubMed:9657005}.Q8NAF0ZN579Zinc finger protein 579ZDNA binding [GO:0003677]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]P30414NKTRNK-tumor recognition proteinnSUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Note=Attached to the membrane via its N-terminus.bFUNCTION: Component of a putative tumor-recognition complex. Involved in the function of NK cells.Q9GZT6CC90B8Coiled-coil domain-containing protein 90B, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11256614}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.O75157T22D2TSC22 domain family protein 2'response to osmotic stress [GO:0006970]Hsequence-specific DNA binding transcription factor activity [GO:0003700]Q92896GSLG1Golgi apparatus protein 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:2355176}; Single-pass type I membrane protein {ECO:0000269|PubMed:2355176}.1blood coagulation [GO:0007596]; bone morphogenesis [GO:0060349]; leukocyte migration [GO:0050900]; negative regulation of protein processing [GO:0010955]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; regulation of chondrocyte differentiation [GO:0032330]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils).P20073ANXA7 Annexin A7autophagy [GO:0006914]; cell proliferation [GO:0008283]; cellular calcium ion homeostasis [GO:0006874]; cellular water homeostasis [GO:0009992]; epithelial cell differentiation [GO:0030855]; hemostasis [GO:0007599]; membrane fusion [GO:0061025]; negative regulation of gene expression [GO:0010629]; regulation of cell shape [GO:0008360]; response to calcium ion [GO:0051592]; response to organic cyclic compound [GO:0014070]; response to salt stress [GO:0009651]; social behavior [GO:0035176]calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; poly(A) RNA binding [GO:0044822]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]lFUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.Q96ER9CCD51(Coiled-coil domain-containing protein 51aintegral component of membrane [GO:0016021]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]P38646GRP75 Stress-70 protein, mitochondrialtSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.:cellular protein metabolic process [GO:0044267]; cellular response to interleukin-1 [GO:0071347]; negative regulation of apoptotic process [GO:0043066]; protein export from nucleus [GO:0006611]; protein folding [GO:0006457]; protein targeting to mitochondrion [GO:0006626]; response to toxic substance [GO:0009636]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]FUNCTION: Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. {ECO:0000269|PubMed:23501103}.Q9H444CHM4B&Charged multivesicular body protein 4bzSUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; maintenance of lens transparency [GO:0036438]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of cell death [GO:0060548]; negative regulation of neuron death [GO:1901215]; nucleus organization [GO:0006997]; positive regulation of viral release from host cell [GO:1902188]; posttranslational protein targeting to membrane [GO:0006620]; protein homooligomerization [GO:0051260]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; regulation of viral process [GO:0050792]; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway [GO:0090611]; vacuolar transport [GO:0007034]; viral budding [GO:0046755]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]Videntical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]&cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endosome [GO:0005768]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane coat [GO:0030117]; midbody [GO:0030496]; nucleus [GO:0005634]FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569,< ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:18209100}.Q96D46NMD3!60S ribosomal export protein NMD3SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Shuttles between the nucleus/nucleolus and the cytoplasm in a XPO1/CRM1-dependent manner.Xprotein transport [GO:0015031]; ribosomal large subunit export from nucleus [GO:0000055]vpoly(A) RNA binding [GO:0044822]; protein binding, bridging [GO:0030674]; ribosomal large subunit binding [GO:0043023]ucytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit. {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}.Q13765NACA4Nascent polypeptide-associated complex subunit alphaSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus.cardiac ventricle development [GO:0003231]; heart trabecula morphogenesis [GO:0061384]; negative regulation of striated muscle cell apoptotic process [GO:0010664]; negative regulation of transcription from RNA polymerase II promoter involved in heart development [GO:1901227]; positive regulation of cell proliferation involved in heart morphogenesis [GO:2000138]; positive regulation of skeletal muscle tissue growth [GO:0048633]; positive regulation of transcription from RNA polymerase II promoter involved in heart development [GO:1901228]; protein transport [GO:0015031]; regulation of skeletal muscle fiber development [GO:0048742]; skeletal muscle tissue regeneration [GO:0043403]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; viral process [GO:0016032]IDNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nascent polypeptide-associated complex [GO:0005854]; nucleus [GO:0005634]FUNCTION: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters. {ECO:0000269|PubMed:10982809, ECO:0000269|PubMed:15784678, ECO:0000269|PubMed:9877153}.P11362FGFR1#Fibroblast growth factor receptor 1tSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus. angiogenesis [GO:0001525]; auditory receptor cell development [GO:0060117]; axon guidance [GO:0007411]; branching involved in salivary gland morphogenesis [GO:0060445]; cell maturation [GO:0048469]; cell migration [GO:0016477]; chondrocyte differentiation [GO:0002062]; chordate embryonic development [GO:0043009]; embryonic limb morphogenesis [GO:0030326]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development [GO:0035607]; innate immune response [GO:0045087]; inner ear morphogenesis [GO:0042472]; insulin receptor signaling pathway [GO:0008286]; in utero embryonic development [GO:0001701]; lung-associated mesenchyme development [GO:0060484]; MAPK cascade [GO:0000165]; mesenchymal cell differentiation [GO:0048762]; midbrain development [GO:0030901]; middle ear morphogenesis [GO:0042474]; motogenic signaling involved in postnatal olfactory bulb interneuron migration [GO:0021837]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron migration [GO:0001764]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ induction [GO:0001759]; outer ear morphogenesis [GO:0042473]; paraxial mesoderm development [GO:0048339]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway [GO:0090080]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of phospholipase activity [GO:0010518]; positive regulation of phospholipase C activity [GO:0010863]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling [GO:0060665]; regulation of cell differentiation [GO:0045595]; regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001239]; regulation of lateral mesodermal cell fate specification [GO:0048378]; regulation of sensory perception of pain [GO:0051930]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; skeletal system morphogenesis [GO:0048705]; stem cell maintenance [GO:0019827]; transcription, DNA-templated [GO:0006351]; ureteric bud development [GO:0001657]; ventricular zone neuroblast division [GO:0021847]/ATP binding [GO:0005524]; fibroblast growth factor-activated receptor activity [GO:0005007]; fibroblast growth factor binding [GO:0017134]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation. {ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:1379698, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409,< ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19261810, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:20139426, ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:8622701, ECO:0000269|PubMed:8663044}.P51692STA5B3Signal transducer and activator of transcription 5BSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocated into the nucleus in response to phosphorylation. {ECO:0000250}. 2-oxoglutarate metabolic process [GO:0006103]; allantoin metabolic process [GO:0000255]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hormone stimulus [GO:0032870]; citrate metabolic process [GO:0006101]; creatine metabolic process [GO:0006600]; creatinine metabolic process [GO:0046449]; development of secondary female sexual characteristics [GO:0046543]; development of secondary male sexual characteristics [GO:0046544]; fatty acid metabolic process [GO:0006631]; female pregnancy [GO:0007565]; isoleucine metabolic process [GO:0006549]; JAK-STAT cascade [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; lactation [GO:0007595]; lipid storage [GO:0019915]; luteinization [GO:0001553]; mast cell migration [GO:0097531]; natural killer cell differentiation [GO:0001779]; negative regulation of apoptotic process [GO:0043066]; negative regulation of erythrocyte differentiation [GO:0045647]; oxaloacetate metabolic process [GO:0006107]; Peyer's patch development [GO:0048541]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-2 biosynthetic process [GO:0045086]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell proliferation [GO:0032819]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; progesterone metabolic process [GO:0042448]; prolactin signaling pathway [GO:0038161]; regulation of epithelial cell differentiation [GO:0030856]; regulation of multicellular organism growth [GO:0040014]; regulation of steroid metabolic process [GO:0019218]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to estradiol [GO:0032355]; response to interleukin-15 [GO:0070672]; response to interleukin-2 [GO:0070669]; response to interleukin-4 [GO:0070670]; succinate metabolic process [GO:0006105]; taurine metabolic process [GO:0019530]; T cell differentiation in thymus [GO:0033077]; T cell homeostasis [GO:0043029]; valine metabolic process [GO:0006573]chromatin binding [GO:0003682]; glucocorticoid receptor binding [GO:0035259]; protein dimerization activity [GO:0046983]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871] FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. {ECO:0000269|PubMed:11773439}.P61218RPAB2:DNA-directed RNA polymerases I, II, and III subunit RPABC2;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.)7-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of type I interferon production [GO:0032481]; positive regulation of viral transcription [GO:0050434]; regulation of gene expression, epigenetic [GO:0040029]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; termination of RNA polymerase III transcription [GO:0006386]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase III promoter [GO:0006383]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]cytosol [GO:0005829]; DNA-directed RNA polymerase I complex [GO:0005736]; DNA-directed RNA polymerase II, core complex [GO:0005665]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250}.Q9H2H9S38A1/Sodium-coupled neutral amino acid transporter 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15054072}; Multi-pass membrane protein {ECO:0000269|PubMed:15054072}. Note=Restricted to the somatodendritic compartment of neurons. Found in the cellular processes of neurons in the developing brain (By similarity). {ECO:0000250}. amino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; ion transport [GO:0006811]; neurotransmitter uptake [GO:0001504]; neutral amino acid transport [GO:0015804]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]amino acid transmembrane transporter activity [GO:0015171]; neutral amino acid transmembrane transporter activity [GO:0015175]; sodium:amino acid symporter activity [GO:0005283]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of glutamine and sodium ions with a stoichiometry of 1:1. May also transport small zwitterionic and aliphatic amino acids with a lower affinity. May supply glutamatergic and GABAergic neurons with glutamine which is required for the synthesis of the neurotransmitters glutamate and GABA. {ECO:0000269|PubMed:10891391}.P00367DHE3(Glutamate dehydrogenase 1, mitochondrialcellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; glutamate biosynthetic process [GO:0006537]; glutamate catabolic process [GO:0006538]; glutamine metabolic process [GO:0006541]; positive regulation of insulin secretion [GO:0032024]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]; tricarboxylic acid metabolic process [GO:0072350]ADP binding [GO:0043531]; ATP binding [GO:0005524]; glutamate dehydrogenase (NAD+) activity [GO:0004352]< ; glutamate dehydrogenase [NAD(P)+] activity [GO:0004353]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; leucine binding [GO:0070728]; NAD+ binding [GO:0070403]FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). {ECO:0000250}.Q07352TISB(Zinc finger protein 36, C3H1 type-like 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.apoptotic process [GO:0006915]; cell proliferation [GO:0008283]; chorio-allantoic fusion [GO:0060710]; gene expression [GO:0010467]; heart development [GO:0007507]; multicellular organism growth [GO:0035264]; neural tube development [GO:0021915]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; proepicardium development [GO:0003342]; regulation of mRNA stability [GO:0043488]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; spongiotrophoblast layer development [GO:0060712]; T cell differentiation in thymus [GO:0033077]; vasculogenesis [GO:0001570]AU-rich element binding [GO:0017091]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]\FUNCTION: Probable regulatory protein involved in regulating the response to growth factors.Q12933TRAF2 TNF receptor-associated factor 2[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:19150425}.A activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular protein complex assembly [GO:0043623]; cellular response to nitric oxide [GO:0071732]; death-inducing signaling complex assembly [GO:0071550]; extrinsic apoptotic signaling pathway [GO:0097191]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; necroptotic process [GO:0070266]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of neuron death [GO:1901215]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein homodimerization activity [GO:0090073]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein autoubiquitination [GO:0051865]; protein catabolic process [GO:0030163]; protein complex assembly [GO:0006461]; protein heterooligomerization [GO:0051291]; protein homotrimerization [GO:0070207]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of immunoglobulin secretion [GO:0051023]; regulation of necrotic cell death [GO:0010939]; response to endoplasmic reticulum stress [GO:0034976]; signal transduction [GO:0007165]; tumor necrosis factor-mediated signaling pathway [GO:0033209]CD40 receptor binding [GO:0005174]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; ligase activity [GO:0016874]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; signal transducer activity [GO:0004871]; sphingolipid binding [GO:0046625]; thioesterase binding [GO:0031996]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]fAIP1-IRE1 complex [GO:1990597]; CD40 receptor complex [GO:0035631]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; IRE1-TRAF2-ASK1 complex [GO:1990604]; membrane raft [GO:0045121]; TRAF2-GSTP1 complex [GO:0097057]; ubiquitin ligase complex [GO:0000151]; vesicle membrane [GO:0012506]FUNCTION: Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE. {ECO:0000269|PubMed:10346818, ECO:0000269|PubMed:11907583, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:18981220, ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082, ECO:0000269|PubMed:19810754, ECO:0000269|PubMed:19918265, ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20047764, ECO:0000269|PubMed:20064526, ECO:0000269|PubMed:20385093, ECO:0000269|PubMed:20577214, ECO:0000269|PubMed:23453969}.Q6ZXV5TMTC31Transmembrane and TPR repeat-containing protein 3bud outgrowth involved in lung branching [GO:0060447]; lung alveolus development [GO:0048286]; muscle fiber development [GO:0048747]; post-embryonic development [GO:0009791]; regulation of gene expression [GO:0010468]P14649MYL6BMyosin light chain 6Bvmuscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; skeletal muscle tissue development [GO:0007519]lcalcium ion binding [GO:0005509]; motor activity [GO:0003774]; structural constituent of muscle [GO:0008307]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle myosin complex [GO:0005859]; myosin complex [GO:0016459]; unconventional myosin complex [GO:0016461]P55786PSA"Puromycin-sensitive aminopeptidase^SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10978616}. Nucleus {ECO:0000305}.1antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular response to hypoxia [GO:0071456]; peptide catabolic process [GO:0043171]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently tha< n tau from Alzheimer disease brain. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:11062501, ECO:0000269|PubMed:17154549, ECO:0000269|PubMed:17318184, ECO:0000269|PubMed:19917696}.Q8NI36WDR36WD repeat-containing protein 36dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21051332, ECO:0000269|PubMed:22002106}.regulation of axon extension [GO:0030516]; response to stimulus [GO:0050896]; retina homeostasis [GO:0001895]; rRNA processing [GO:0006364]; visual perception [GO:0007601]znucleolus [GO:0005730]; Pwp2p-containing subcomplex of 90S preribosome [GO:0034388]; small-subunit processome [GO:0032040]FUNCTION: Involved in the nucleolar processing of SSU 18S rRNA. Involved in T-cell activation and highly coregulated with IL2. {ECO:0000269|PubMed:21051332}.Q9BWD1THIC'Acetyl-CoA acetyltransferase, cytosolic4acetyl-CoA C-acetyltransferase activity [GO:0003985]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q8NET6CHSTD Carbohydrate sulfotransferase 13'carbohydrate biosynthetic process [GO:0016051]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan metabolic process [GO:0030203]; small molecule metabolic process [GO:0044281]vchondroitin 4-sulfotransferase activity [GO:0047756]; N-acetylgalactosamine 4-O-sulfotransferase activity [GO:0001537]FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.Q9UNM6PSD13/26S proteasome non-ATPase regulatory subunit 13Ranaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; meiosis I [GO:0007127]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]O43824GTPB6Putative GTP-binding protein 68GTP binding [GO:0005525]; metal ion binding [GO:0046872]Q03405UPAR0Urokinase plasminogen activator surface receptorSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12376466}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466}. Note=Colocalized with FAP (seprase) preferentially at the cell surface of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin-dependent manner. {ECO:0000269|PubMed:12376466}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.attachment of GPI anchor to protein [GO:0016255]; blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; chemotaxis [GO:0006935]; C-terminal protein lipidation [GO:0006501]; fibrinolysis [GO:0042730]; movement of cell or subcellular component [GO:0006928]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; positive regulation of DNA binding [GO:0043388]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; post-translational protein modification [GO:0043687]; regulation of proteolysis [GO:0030162]; signal transduction [GO:0007165]; urokinase plasminogen activator signaling pathway [GO:0038195]enzyme binding [GO:0019899]; protein domain specific binding [GO:0019904]; receptor activity [GO:0004872]; receptor binding [GO:0005102]; urokinase plasminogen activator receptor activity [GO:0030377]anchored component of membrane [GO:0031225]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; invadopodium membrane [GO:0071438]; plasma membrane [GO:0005886]0FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.Q9NRX4PHP14#14 kDa phosphohistidine phosphatasenegative regulation of ATP citrate synthase activity [GO:2000984]; negative regulation of lyase activity [GO:0051350]; negative regulation of T cell receptor signaling pathway [GO:0050860]; peptidyl-histidine dephosphorylation [GO:0035971]; positive regulation of cell motility [GO:2000147]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; protein dephosphorylation [GO:0006470]; regulation of actin cytoskeleton reorganization [GO:2000249]calcium channel inhibitor activity [GO:0019855]; ion channel binding [GO:0044325]; phosphohistidine phosphatase activity [GO:0008969]; phosphoprotein phosphatase activity [GO:0004721]9FUNCTION: Exhibits phosphohistidine phosphatase activity.Q8N4A0GALT4/Polypeptide N-acetylgalactosaminyltransferase 4SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:9804815}; Single-pass type II membrane protein {ECO:0000305|PubMed:9804815}.extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]7FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.P30419NMT1*Glycylpeptide N-tetradecanoyltransferase 1)SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952}. Cytoplasm, cytosol {ECO:0000269|PubMed:9353336}. Membrane {ECO:0000269|PubMed:9506952}; Peripheral memb< rane protein {ECO:0000269|PubMed:9506952}. Note=Copurifies with ribosomes. {ECO:0000269|PubMed:9353336}.apoptotic process [GO:0006915]; intrinsic apoptotic signaling pathway [GO:0097193]; in utero embryonic development [GO:0001701]; N-terminal peptidyl-glycine N-myristoylation [GO:0018008]; phototransduction, visible light [GO:0007603]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; rhodopsin mediated signaling pathway [GO:0016056]; viral process [GO:0016032]>glycylpeptide N-tetradecanoyltransferase activity [GO:0004379]actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952}.O75928PIAS2E3 SUMO-protein ligase PIAS2SUBCELLULAR LOCATION: Nucleus speckle. Nucleus, PML body. Note=Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs).Zandrogen receptor signaling pathway [GO:0030521]; cellular protein metabolic process [GO:0044267]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of osteoblast differentiation [GO:0045667]; transcription, DNA-templated [GO:0006351]androgen receptor binding [GO:0050681]; DNA binding [GO:0003677]; ligase activity [GO:0016874]; SUMO ligase activity [GO:0061665]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]anuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]RFUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'. {ECO:0000269|PubMed:15920481, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:22406621}.P49588SYAC!Alanine--tRNA ligase, cytoplasmicBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.alanyl-tRNA aminoacylation [GO:0006419]; cerebellar Purkinje cell layer development [GO:0021680]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; hair follicle development [GO:0001942]; negative regulation of neuron apoptotic process [GO:0043524]; neuromuscular process controlling balance [GO:0050885]; protein folding [GO:0006457]; response to amino acid [GO:0043200]; tRNA aminoacylation for protein translation [GO:0006418]; tRNA modification [GO:0006400]; tRNA processing [GO:0008033]alanine-tRNA ligase activity [GO:0004813]; aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]Q5T8P6RBM26RNA-binding protein 26VmRNA processing [GO:0006397]; negative regulation of phosphatase activity [GO:0010923]ametal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]Q9UMS4PRP19Pre-mRNA-processing factor 19SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20176811}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11082287}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11082287}. Cytoplasm {ECO:0000269|PubMed:11435423}. Lipid droplet {ECO:0000250|UniProtKB:Q99KP6}. Note=Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Recruited on damaged DNA at sites of double-strand break. {ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:18263876}.xcellular protein localization [GO:0034613]; double-strand break repair via nonhomologous end joining [GO:0006303]; gene expression [GO:0010467]; generation of catalytic spliceosome for first transesterification step [GO:0000349]; inner cell mass cell proliferation [GO:0001833]; lipid biosynthetic process [GO:0008610]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of neuron differentiation [GO:0045665]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; proteasomal protein catabolic process [GO:0010498]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; RNA splicing [GO:0008380]; signal transduction involved in DNA damage checkpoint [GO:0072422]; spliceosomal complex assembly [GO:0000245]; spliceosomal tri-snRNP complex assembly [GO:0000244]identical protein binding [GO:0042802]; ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-ubiquitin ligase activity [GO:0034450]Pcatalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; lipid particle [GO:0005811]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Prp19 complex [GO:0000974]; site of double-strand break [GO:0035861]; spindle [GO:0005819]; U2-type catalytic step 1 spliceosome [GO:0071006]% FUNCTION: Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor S< ETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity). {ECO:0000250|UniProtKB:Q99KP6, ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000269|PubMed:11082287, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:12960389, ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:16223718, ECO:0000269|PubMed:16332694, ECO:0000269|PubMed:16388800, ECO:0000269|PubMed:17349974, ECO:0000269|PubMed:18263876, ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:24332808, ECO:0000303|PubMed:17981804, ECO:0000303|PubMed:20595234}.Q5TDH0DDI2Protein DDI1 homolog 21aspartic-type endopeptidase activity [GO:0004190]Q9NUM4T106BTransmembrane protein 106BSUBCELLULAR LOCATION: Late endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein._dendrite morphogenesis [GO:0048813]; lysosome localization [GO:0032418]; transport [GO:0006810]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]%FUNCTION: Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with MAP6. May act by inhibiting retrograde transport of lysosomes along dendrites. Required for dendrite branching. {ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:24357581}.O60341KDM1A&Lysine-specific histone demethylase 1ACoRESTYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:16079795}.+blood coagulation [GO:0007596]; cell proliferation [GO:0008283]; chromatin organization [GO:0006325]; granulocyte differentiation [GO:0030851]; histone H3-K4 demethylation [GO:0034720]; histone H3-K9 demethylation [GO:0033169]; in utero embryonic development [GO:0001701]; muscle cell development [GO:0055001]; negative regulation of DNA binding [GO:0043392]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of histone H3-K4 methylation [GO:0051572]; negative regulation of histone H3-K9 methylation [GO:0051573]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of protein binding [GO:0032091]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; pituitary gland development [GO:0021983]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of hormone biosynthetic process [GO:0046886]; positive regulation of megakaryocyte differentiation [GO:0045654]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein demethylation [GO:0006482]; regulation of primitive erythrocyte differentiation [GO:0010725]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351]androgen receptor binding [GO:0050681]; chromatin binding [GO:0003682]; demethylase activity [GO:0032451]; enzyme binding [GO:0019899]; flavin adenine dinucleotide binding [GO:0050660]; histone demethylase activity [GO:0032452]; histone demethylase activity (H3-dimethyl-K4 specific) [GO:0034648]; histone demethylase activity (H3-K4 specific) [GO:0032453]; histone demethylase activity (H3-K9 specific) [GO:0032454]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; MRF binding [GO:0043426]; oxidoreductase activity [GO:0016491]; p53 binding [GO:0002039]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]ynuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]aFUNCTION: Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. {ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20562920}.O14880MGST3&Microsomal glutathione S-transferase 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. glutathione derivative biosynthetic process [GO:1901687]; lipid metabolic process [GO:0006629]; response to organonitrogen compound [GO:0010243]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]}glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; peroxidase activity [GO:0004601]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear envelope [GO:0005635]5FUNCTION: Also functions as a glutathione peroxidase.Q8WV41SNX33Sorting nexin-33rSUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Primarily cytosolic, but a minor proportion is membrane-bound (PubMed:18353773). Not associated with membranes (PubMed:21048941). {ECO:0000269|PubMed:18353773, ECO:0000269|PubMed:21048941}.cleavage furrow formation [GO:0036089]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; intracellular protein transport [GO:0006886]; macropinocytosis [GO:0044351]; membran< e tubulation [GO:0097320]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0007067]; negative regulation of endocytosis [GO:0045806]; negative regulation of protein localization to cell surface [GO:2000009]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of protein localization to cell surface [GO:2000010]; protein import [GO:0017038]; vesicle organization [GO:0016050]cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endosome [GO:0005768]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020]FUNCTION: Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes. {ECO:0000269|PubMed:18353773, ECO:0000269|PubMed:18419754, ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:20964629, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.Q9NR30DDX21Nucleolar RNA helicase 2SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:8614622}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060}. Note=Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292). Interaction with WDR46 is required for localization to the nucleolus (PubMed:23848194). {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194}.osteoblast differentiation [GO:0001649]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; rRNA processing [GO:0006364]; transcription from RNA polymerase II promoter [GO:0006366]7SK snRNA binding [GO:0097322]; ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; snoRNA binding [GO:0030515]]membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Involved in rRNA processing (PubMed:14559904, PubMed:18180292). {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904, ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391, ECO:0000269|PubMed:9461305}.Q9ULV4COR1C Coronin-1CSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12377779}. Cell projection, lamellipodium {ECO:0000269|PubMed:12377779}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12377779}. Note=All isoforms localize in a diffuse and punctate pattern in the cytosol and are highly enriched in F-actin-rich areas. Isoform 3 colocalizes with the thin filaments of the sarcomere and with the postsynaptic area and the junctional sarcoplasm of motor end plates.actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; establishment of protein localization [GO:0045184]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of protein kinase activity by regulation of protein phosphorylation [GO:0044387]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; neural crest cell migration [GO:0001755]; phagocytosis [GO:0006909]; positive regulation of lamellipodium morphogenesis [GO:2000394]; regulation of epithelial cell migration [GO:0010632]; regulation of fibroblast migration [GO:0010762]; regulation of focal adhesion assembly [GO:0051893]; regulation of protein phosphorylation [GO:0001932]; regulation of ruffle assembly [GO:1900027]; regulation of substrate adhesion-dependent cell spreading [GO:1900024]; signal transduction [GO:0007165]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; flotillin complex [GO:0016600]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; lateral plasma membrane [GO:0016328]FUNCTION: May be involved in cytokinesis, motility, and signal transduction. {ECO:0000250}.; FUNCTION: Isoform 3: Involved in myogenic differentiation.P16949STMN1Stathminaxonogenesis [GO:0007409]; brain development [GO:0007420]; intracellular signal transduction [GO:0035556]; microtubule depolymerization [GO:0007019]; mitotic spindle organization [GO:0007052]; negative regulation of microtubule polymerization [GO:0031115]; neuron projection development [GO:0031175]; positive regulation of cellular component movement [GO:0051272]; regulation of cytoskeleton organization [GO:0051493]; response to virus [GO:0009615]; signal transduction [GO:0007165]Esignal transducer activity [GO:0004871]; tubulin binding [GO:0015631]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; membrane [GO:0016020]; microtubule [GO:0005874]; neuron projection [GO:0043005]PFUNCTION: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity). {ECO:0000250}.O75533SF3B1Splicing factor 3B subunit 1}SUBCELLULAR LOCATION: Nucleus speckle. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm.anterior/posterior pattern specification [GO:0009952]; blastocyst formation [GO:0001825]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]@chromatin binding [GO:0003682]; poly(A) RNA binding [GO:0044822]/catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]Q9Y697NFS1#Cysteine desulfurase, mitochondrial{SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.; SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. Nucleus.cysteine metabolic process [GO:0006534]; iron inc< orporation into metallo-sulfur cluster [GO:0018283]; molybdopterin cofactor biosynthetic process [GO:0032324]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein complex assembly [GO:0006461]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]cysteine desulfurase activity [GO:0031071]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor. {ECO:0000269|PubMed:18650437}.P02786TFR1Transferrin receptor protein 1TSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065}; Single-pass type II membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.; SUBCELLULAR LOCATION: Transferrin receptor protein 1, serum form: Secreted.Hacute-phase response [GO:0006953]; aging [GO:0007568]; cellular iron ion homeostasis [GO:0006879]; cellular response to drug [GO:0035690]; iron ion import [GO:0097286]; osteoclast differentiation [GO:0030316]; positive regulation of bone resorption [GO:0045780]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666]; response to iron ion [GO:0010039]; response to manganese ion [GO:0010042]; response to nutrient [GO:0007584]; response to retinoic acid [GO:0032526]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]; viral process [GO:0016032].double-stranded RNA binding [GO:0003725]; glycoprotein binding [GO:0001948]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; transferrin receptor activity [GO:0004998]; transferrin transmembrane transporter activity [GO:0033570]blood microparticle [GO:0072562]; cell surface [GO:0009986]; coated pit [GO:0005905]; cytoplasmic membrane-bounded vesicle [GO:0016023]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; HFE-transferrin receptor complex [GO:1990712]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]FUNCTION: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. {ECO:0000250, ECO:0000269|PubMed:3568132}.O14763TR10B5Tumor necrosis factor receptor superfamily member 10BTNFactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; necroptotic process [GO:0070266]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; regulation of apoptotic process [GO:0042981]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of necrotic cell death [GO:0010939]; response to endoplasmic reticulum stress [GO:0034976]:receptor activity [GO:0004872]; TRAIL binding [GO:0045569]cell surface [GO:0009986]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis. {ECO:0000269|PubMed:15322075}.O95749GGPPS%Geranylgeranyl pyrophosphate synthase4cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid metabolic process [GO:0006720]; small molecule metabolic process [GO:0044281]dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.Q13608PEX6Peroxisome assembly factor 2aSUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane. Note=Associated with peroxisomal membranes.peroxisome organization [GO:0007031]; protein import into peroxisome matrix, translocation [GO:0016561]; protein stabilization [GO:0050821]; protein targeting to peroxisome [GO:0006625]ATPase activity [GO:0016887]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; protein complex binding [GO:0032403]; protein C-terminus binding [GO:0008022]hcytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.P27707DCKDeoxycytidine kinase;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9342341}.deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide biosynthetic process [GO:0009165]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside salvage [GO:0043097]; pyrimidine nucleotide metabolic process [GO:0006220]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; deoxycytidine kinase activity [GO:0004137]; drug binding [GO:0008144]; nucleoside kinase activity [GO:0019206]; protein homodimerization activity [GO:0042803]FUNCTION: Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based< on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. {ECO:0000269|PubMed:18377927, ECO:0000269|PubMed:20614893}.O00160MYO1FUnconventional myosin-If5defense response to Gram-positive bacterium [GO:0050830]; negative regulation of cell adhesion [GO:0007162]; neutrophil degranulation [GO:0043312]; positive regulation of cell migration [GO:0030335]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of innate immune response [GO:0045088]Qactin binding [GO:0003779]; ATP binding [GO:0005524]; motor activity [GO:0003774]tcortical actin cytoskeleton [GO:0030864]; filamentous actin [GO:0031941]; unconventional myosin complex [GO:0016461]FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}.Q9BZJ0CRNL1Crooked neck-like protein 1SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=Colocalizes with core spliceosomal snRNP proteins. Also diffusely expressed in cytoplasm.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of defense response to virus by host [GO:0002230]; spliceosomal complex assembly [GO:0000245]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; spliceosomal complex [GO:0005681]0FUNCTION: Involved in pre-mRNA splicing process.P55795HNRH2*Heterogeneous nuclear ribonucleoprotein H2[nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]mmembrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).A0FGR8ESYT2Extended synaptotagmin-2SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Detected at sites of contact between the endoplasmic reticulum membrane and the cell membrane. Recruited to the cell membrane via the third C2 domain.6endocytosis [GO:0006897]; lipid transport [GO:0006869]calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; phosphatidylcholine binding [GO:0031210]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylinositol binding [GO:0035091](endoplasmic reticulum [GO:0005783]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; integral component of plasma membrane [GO:0005887]; intrinsic component of endoplasmic reticulum membrane [GO:0031227]; membrane [GO:0016020]; organelle membrane contact site [GO:0044232]%FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24847877}.P25391LAMA1Laminin subunit alpha-1Taxon guidance [GO:0007411]; branching involved in salivary gland morphogenesis [GO:0060445]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; establishment of epithelial cell apical/basal polarity [GO:0045198]; extracellular matrix organization [GO:0030198]; morphogenesis of an epithelial sheet [GO:0002011]; regulation of cell adhesion [GO:0030155]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]; retinal blood vessel morphogenesis [GO:0061304]`extracellular matrix structural constituent [GO:0005201]; glycosphingolipid binding [GO:0043208]basement membrane [GO:0005604]; cell-cell junction [GO:0005911]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-1 complex [GO:0005606]; laminin-3 complex [GO:0005608]; proteinaceous extracellular matrix [GO:0005578]Q9BYT8NEULNeurolysin, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm {ECO:0000250}.lregulation of gluconeogenesis [GO:0006111]; regulation of skeletal muscle fiber differentiation [GO:1902809]hmetal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptide binding [GO:0042277]Lmitochondrial intermembrane space [GO:0005758]; plasma membrane [GO:0005886]bFUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. {ECO:0000250}.Q07955SRSF1&Serine/arginine-rich splicing factor 1{SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle. Note=In nuclear speckles. Shuttles between the nucleus and the cytoplasm.cardiac muscle contraction [GO:0060048]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; mRNA 3'-end processing [GO:0031124]; mRNA 5'-splice site recognition [GO:0000395]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; regulation of mRNA splicing, via spliceosome [GO:0048024]; regulation of mRNA stability [GO:0043488]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]wFUNCTION: Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway. {ECO:0000269|PubMed:8139654}.P04049RAF12RAF proto-oncogene serine/threonine-protein kinaseSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Mitochondrion. Nucleus. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its mitochondrial localization. Retinoic acid-induced Ser-621 phosphorylated form of RAF1 is predominantly localized at the nucleus.eactivation of adenylate cyclase activity [GO:0007190]; activation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell proliferation [GO:0008283]; death-inducing signaling complex assembly [GO:0071550]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor si< gnaling pathway [GO:0008543]; heart development [GO:0007507]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; intermediate filament cytoskeleton organization [GO:0045104]; ion transmembrane transport [GO:0034220]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of protein complex assembly [GO:0031333]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of apoptotic process [GO:0042981]; regulation of cell differentiation [GO:0045595]; regulation of cell motility [GO:2000145]; regulation of Rho protein signal transduction [GO:0035023]; response to hypoxia [GO:0001666]; response to muscle stretch [GO:0035994]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; somatic stem cell maintenance [GO:0035019]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing [GO:0042060]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269|PubMed:11427728, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:15618521, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:16924233, ECO:0000269|PubMed:9360956}.O15260SURF4Surfeit locus protein 4"SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Cycles between the endoplasmic reticulum and the Golgi.[Golgi organization [GO:0007030]; positive regulation of organelle organization [GO:0010638]endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: May play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi. {ECO:0000269|PubMed:18287528}.Q9NX62IMPA3Inositol monophosphatase 3SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18695242}; Single-pass type II membrane protein {ECO:0000269|PubMed:18695242}.4chondrocyte development [GO:0002063]; chondroitin sulfate metabolic process [GO:0030204]; embryonic digit morphogenesis [GO:0042733]; endochondral ossification [GO:0001958]; inositol biosynthetic process [GO:0006021]; phosphatidylinositol phosphorylation [GO:0046854]; post-embryonic development [GO:0009791]43'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3'-nucleotidase activity [GO:0008254]; inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; metal ion binding [GO:0046872]`Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. {ECO:0000250}.Q9Y6I3EPN1Epsin-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). {ECO:0000250}.Membryonic organ development [GO:0048568]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; female pregnancy [GO:0007565]; in utero embryonic development [GO:0001701]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; Notch signaling pathway [GO:0007219]coated pit [GO:0005905]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195] FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis. {ECO:0000250, ECO:0000269|PubMed:10557078}.Q9HC52CBX8Chromobox protein homolog 8<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. cellular protein metabolic process [GO:0044267]; cellular response to hydrogen peroxide [GO:0070301]; histone ubiquitination [GO:0016574]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA repair [GO:0045739]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; transcription, DNA-templated [GO:0006351]methylated histone binding [GO:0035064]; single-stranded RNA binding [GO:0003727]; ubiquitin-protein transferase activator activ< ity [GO:0097027]heterochromatin [GO:0000792]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. {ECO:0000269|PubMed:21282530}.Q8TF72SHRM3Protein Shroom3SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with F-actin in stress fibers and adherens junctions. {ECO:0000250}.Tactin cytoskeleton organization [GO:0030036]; apical protein localization [GO:0045176]; cell morphogenesis [GO:0000902]; cellular pigment accumulation [GO:0043482]; columnar/cuboidal epithelial cell development [GO:0002066]; neural tube closure [GO:0001843]; pattern specification process [GO:0007389]; regulation of cell shape [GO:0008360]adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microtubule [GO:0005874]FUNCTION: Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers. Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity). {ECO:0000250}.Q8WUD6CHPT1Cholinephosphotransferase 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}.vCDP-choline pathway [GO:0006657]; glycerophospholipid biosynthetic process [GO:0046474]; lipid metabolic process [GO:0006629]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid metabolic process [GO:0006644]; platelet activating factor biosynthetic process [GO:0006663]; regulation of cell growth [GO:0001558]; small molecule metabolic process [GO:0044281]diacylglycerol binding [GO:0019992]; diacylglycerol cholinephosphotransferase activity [GO:0004142]; metal ion binding [GO:0046872]Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]FUNCTION: Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes.Q9Y3D7TIM16=Mitochondrial import inner membrane translocase subunit TIM16SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}; Peripheral membrane protein {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}; Matrix side {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}.cellular protein metabolic process [GO:0044267]; negative regulation of ATPase activity [GO:0032780]; ossification [GO:0001503]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626] extrinsic component of mitochondrial inner membrane [GO:0031314]; mitochondrial inner membrane presequence translocase complex [GO:0005744]; mitochondrial matrix [GO:0005759]; presequence translocase-associated import motor [GO:0001405]; protein complex [GO:0043234]FUNCTION: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity. {ECO:0000269|PubMed:20053669}.Q9UL33TPC2L;Trafficking protein particle complex subunit 2-like proteinSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19416478}. Endoplasmic reticulum {ECO:0000269|PubMed:19416478}. Golgi apparatus {ECO:0000269|PubMed:19416478}.cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]tFUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:19416478}.Q96A49SYAP1Synapse-associated protein 1rcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]P50502F10A1Hsc70-interacting proteinchaperone cofactor-dependent protein refolding [GO:0070389]; negative regulation of protein refolding [GO:0061084]; protein folding [GO:0006457]; protein homooligomerization [GO:0051260]AdATP binding [GO:0032564]; protein binding, bridging [GO:0030674]ncytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; protein complex [GO:0043234]jFUNCTION: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity). {ECO:0000250}.Q76M96CCD80(Coiled-coil domain-containing protein 80kextracellular matrix organization [GO:0030198]; positive regulation of cell-substrate adhesion [GO:0010811]heparin binding [GO:0008201]@basement membrane [GO:0005604]; interstitial matrix [GO:0005614]DFUNCTION: Promotes cell adhesion and matrix assembly. {ECO:0000250}.Q8IZP0ABI1Abl interactor 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus (By similarity). {ECO:0000250}.actin polymerization or depolymerization [GO:0008154]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; lamellipodium morphogenesis [GO:0072673]; megakaryocyte development [GO:0035855]; movement of cell or subcellular component [GO:0006928]; negative regulation of cell proliferation [GO:0008285]; peptidyl-tyrosine phosphorylation [GO:0018108]; small GTPase mediated signal transduction [GO:0007264]; somitogenesis [GO:0001756]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]cytoskeletal protein binding [GO:0008092]; protein complex binding [GO:0032403]; protein tyrosine kinase activator activity [GO:0030296]vcell junction [GO:0030054]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; growth cone [GO:0030426]; intracellular [GO:0005622]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; SCAR complex [GO:0031209]hFUNCTION: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of d< eveloping neurons. {ECO:0000269|PubMed:11003655, ECO:0000269|PubMed:18328268}.O76081RGS20#Regulator of G-protein signaling 20SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation. {ECO:0000250}.positive regulation of GTPase activity [GO:0043547]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; termination of G-protein coupled receptor signaling pathway [GO:0038032]lcytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity). {ECO:0000250}.Q9BRA2TXD17(Thioredoxin domain-containing protein 17>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14607844}.goxidation-reduction process [GO:0055114]; tumor necrosis factor-mediated signaling pathway [GO:0033209]{electron carrier activity [GO:0009055]; peroxidase activity [GO:0004601]; protein-disulfide reductase activity [GO:0047134]FUNCTION: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide. {ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}.Q14296FASTK%Fas-activated serine/threonine kinasewapoptotic signaling pathway [GO:0097190]; protein phosphorylation [GO:0006468]; regulation of RNA splicing [GO:0043484]ATP binding [GO:0005524]; Fas-activated serine/threonine kinase activity [GO:0033867]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Phosphorylates the splicing regulator TIA1, thereby promoting the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-apoptotic form of the receptor. {ECO:0000269|PubMed:17135269, ECO:0000269|PubMed:7544399}.P18615NELFENegative elongation factor EYgene expression [GO:0010467]; negative regulation of mRNA polyadenylation [GO:1900364]; negative regulation of transcription elongation from RNA polymerase II promoter [GO:0034244]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]{chromatin binding [GO:0003682]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]emitochondrion [GO:0005739]; NELF complex [GO:0032021]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]}FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:11940650, ECO:0000269|PubMed:12612062}.Q5T0F9C2D1B/Coiled-coil and C2 domain-containing protein 1B<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19423080}.aRNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]eintracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. {ECO:0000269|PubMed:19423080}.Q8IUF8MINAFBifunctional lysine-specific demethylase and histidyl-hydroxylase MINASUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}. Nucleus, nucleolus {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}.Kribosome biogenesis [GO:0042254]; transcription, DNA-templated [GO:0006351]dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]; RNA polymerase II transcription factor binding transcription repressor activity [GO:0001191]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles. {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14695334, ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15819408, ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:17317935, ECO:0000269|PubMed:19502796, ECO:0000269|PubMed:23103944}.Q9P2X3IMPCTProtein IMPACTdSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=May be associated with polysomes. {ECO:0000250}.pnegative regulation of protein phosphorylation [GO:0001933]; regulation of translational initiation [GO:0006446]4FUNCTION: Translational regulator that ensures constant high levels of translation under amino acid starvation. Acts by interacting with GCN1/GCN1L1, thereby preventing activation of GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis (By similarity). May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis (By similarity). Through its action on GCN2, may also facilitate neuritogenesis (By similarity). {ECO:0000250}.Q9NUJ1ABHDA:Mycophenolic acid acyl-glucuronide esterase, mitochondrial,glucuronoside catabolic process [GO:0019391]Ahydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]FUNCTION: Catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, a metabolite of the immunosuppressant drug mycophenolate. {ECO:0000269|PubMed:22294686}.P08559ODPANPyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialuacetyl-CoA biosynthetic process from pyruvate [GO:0006086]; cellular metabolic process [GO:0044237]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; pyruvate dehydrogenase complex [GO:0045254]FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. {ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}.Q14004CDK13Cyclin-dependent kinase 13DSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16721827}.Ralternative mRNA splicing, via spliceosome [GO:0000380]; hemopoiesis [GO:0030097]; multicellular organismal development [GO:0007275]; phosphorylation of RNA polymerase II< C-terminal domain [GO:0070816]; positive regulation of cell proliferation [GO:0008284]; regulation of mitotic nuclear division [GO:0007088]; viral process [GO:0016032] ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]cyclin K-CDK13 complex [GO:0002945]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef. {ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328, ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}.P06737PYGL"Glycogen phosphorylase, liver formY5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; carbohydrate metabolic process [GO:0005975]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; necroptotic process [GO:0070266]; small molecule metabolic process [GO:0044281]YAMP binding [GO:0016208]; ATP binding [GO:0005524]; bile acid binding [GO:0032052]; drug binding [GO:0008144]; glucose binding [GO:0005536]; glycogen phosphorylase activity [GO:0008184]; protein homodimerization activity [GO:0042803]; purine nucleobase binding [GO:0002060]; pyridoxal phosphate binding [GO:0030170]; vitamin binding [GO:0019842]FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.O43402EMC8%ER membrane protein complex subunit 8>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22119785}.cytoplasm [GO:0005737]; ER membrane protein complex [GO:0072546]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]Q13616CUL1Cullin-1kanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; circadian rhythm [GO:0007623]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; mitotic cell cycle [GO:0000278]; negative regulation of cell proliferation [GO:0008285]; Notch signaling pathway [GO:0007219]; organ morphogenesis [GO:0009887]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein monoubiquitination [GO:0006513]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]cullin-RING ubiquitin ligase complex [GO:0031461]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; Parkin-FBXW7-Cul1 ubiquitin ligase complex [GO:1990452]; SCF ubiquitin ligase complex [GO:0019005]FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2. {ECO:0000269|PubMed:15531760, ECO:0000269|PubMed:15640526, ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23263282, ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:9663463}.P78559MAP1A!Microtubule-associated protein 1A"activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; microtubule cytoskeleton organization [GO:0000226]; photoreceptor cell maintenance [GO:0045494]; positive regulation of defense response to virus by host [GO:0002230]; sensory perception of sound [GO:0007605]cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; neuronal postsynaptic density [GO:0097481]; photoreceptor outer segment [GO:0001750]yFUNCTION: Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.Q86X02CDR2L.Cerebellar degeneration-related protein 2-likeO60832DKC1)H/ACA ribonucleoprotein complex subunit 4SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Nucleus, Cajal body. Note=Also localized to Cajal bodies (coiled bodies).; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.box H/ACA snoRNA 3'-end processing [GO:0000495]; cell proliferation [GO:0008283]; mRNA pseudouridine synthesis [GO:1990481]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere maintenance via telomerase [GO:0032212]; RNA processing [GO:0006396]; rRNA processing [GO:0006364]; rRNA pseudouridine synthesis [GO:0031118]; snRNA pseudouridine synthesis [GO:0031120]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]poly(A) RNA binding [GO:0044822]; pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; telomerase activity [GO:0003720]box H/ACA snoRNP complex [GO:0031429]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]"FUNCTION: Isoform 1: Required for ribosome biogenesis and telomere maintenance. Probable< catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.; FUNCTION: Isoform 3: Promotes cell to cell and cell to substratum adhesion, increases the cell proliferation rate and leads to cytokeratin hyper-expression (when overexpressed in HeLa cells).Q14839CHD4+Chromodomain-helicase-DNA-binding protein 4 Mi-2_NuRD(20)SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17626165}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in interphase. {ECO:0000250|UniProtKB:Q6PDQ2}.ATP-dependent chromatin remodeling [GO:0043044]; chromatin organization [GO:0006325]; DNA duplex unwinding [GO:0032508]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spindle assembly [GO:0051225]; terminal button organization [GO:0072553]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; DNA binding [GO:0003677]; RNA polymerase II repressing transcription factor binding [GO:0001103]; zinc ion binding [GO:0008270]centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; protein complex [GO:0043234]FUNCTION: Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:9804427}.P26440IVD+Isovaleryl-CoA dehydrogenase, mitochondrial/branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; leucine catabolic process [GO:0006552]; lipid homeostasis [GO:0055088]; small molecule metabolic process [GO:0044281]electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]Wmitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q14849STAR3%StAR-related lipid transfer protein 3JSUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein.cholesterol metabolic process [GO:0008203]; lipid metabolic process [GO:0006629]; mitochondrial transport [GO:0006839]; progesterone biosynthetic process [GO:0006701]; steroid metabolic process [GO:0008202]Ocholesterol binding [GO:0015485]; cholesterol transporter activity [GO:0017127]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739][FUNCTION: Binds and transports cholesterol. Promotes steroidogenesis in placenta and brain.P631512ABAQSerine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoformG2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope reassembly [GO:0007084]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; protein dephosphorylation [GO:0006470]; regulation of protein phosphatase type 2A activity [GO:0034047]; response to morphine [GO:0043278]; signal transduction [GO:0007165]`cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein phosphatase type 2A complex [GO:0000159]Q86Y07VRK2$Serine/threonine-protein kinase VRK2SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.cellular response to oxidative stress [GO:0034599]; endocytosis [GO:0006897]; peptidyl-serine phosphorylation [GO:0018105]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; regulation of interleukin-1-mediated signaling pathway [GO:2000659]; regulation of MAPK cascade [GO:0043408]; viral process [GO:0016032]; Wnt signaling pathway [GO:0016055]ATP binding [GO:0005524]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant.; FUNCTION: Isoform 2 phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity.Q14152EIF3A4Eukaryotic translation initiation factor 3 subunit A^SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:9150439}.Fcellular protein metabolic process [GO:0044267]; formation of cytoplasmic translation initiation complex [GO:0001732]; formation of translation preinitiation complex [GO:0001731]; gene expression [GO:0010467]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]poly(A) RNA binding [GO:0044822]; structural molecule activity [GO:0005198]; translation initiation factor activity [GO:0003743]`cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. {ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:11169732}.Q8IWE2NXP20< Protein NOXP20FFUNCTION: May play a role in neuronal cell development. {ECO:0000250}.Q8TD30ALAT2Alanine aminotransferase 2"2-oxoglutarate metabolic process [GO:0006103]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; L-alanine catabolic process [GO:0042853]; L-alanine metabolic process [GO:0042851]; small molecule metabolic process [GO:0044281]iL-alanine:2-oxoglutarate aminotransferase activity [GO:0004021]; pyridoxal phosphate binding [GO:0030170]FUNCTION: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. {ECO:0000269|PubMed:11863375}.Q9UHQ4BAP29%B-cell receptor-associated protein 29apoptotic process [GO:0006915]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; osteoblast differentiation [GO:0001649]; protein localization to endoplasmic reticulum exit site [GO:0070973]FUNCTION: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity). {ECO:0000250}.P51116FXR27Fragile X mental retardation syndrome-related protein 2vnegative regulation of translation [GO:0017148]; positive regulation of defense response to virus by host [GO:0002230]}identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; polysome [GO:0005844]FUNCTION: RNA-binding protein.Q7Z4G1COMD6 COMM domain-containing protein 6SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:21778237}. Cytoplasm {ECO:0000269|PubMed:16573520}.vnegative regulation of NF-kappaB transcription factor activity [GO:0032088]; transcription, DNA-templated [GO:0006351]FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF-kappa-B. Inhibits TNF-induced NFKB1 activation. {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, ECO:0000305|PubMed:21778237}.Q99757THIOMThioredoxin, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052}.Vcell redox homeostasis [GO:0045454]; cellular response to nutrient levels [GO:0031669]; cellular response to oxidative stress [GO:0034599]; glycerol ether metabolic process [GO:0006662]; oxidation-reduction process [GO:0055114]; protein folding [GO:0006457]; response to axon injury [GO:0048678]; response to drug [GO:0042493]; response to glucose [GO:0009749]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to nutrient [GO:0007584]; response to organic cyclic compound [GO:0014070]; response to reactive oxygen species [GO:0000302]; sulfate assimilation [GO:0000103]oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; peptide-methionine (S)-S-oxide reductase activity [GO:0008113]; protein disulfide oxidoreductase activity [GO:0015035]cytoplasm [GO:0005737]; dendrite [GO:0030425]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]FUNCTION: Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity. {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052}.Q86UP2KTN1KinectinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=Vesicle membrane protein anchored to the endoplasmic reticulum._microtubule-based movement [GO:0007018]; small GTPase mediated signal transduction [GO:0007264]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin.P09012SNRPA$U1 small nuclear ribonucleoprotein AU1(15)wnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; snRNA binding [GO:0017069]cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs. {ECO:0000269|PubMed:9848648}.P56182RRP1,Ribosomal RNA processing protein 1 homolog AcSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:9192856}._nucleolus [GO:0005730]; nucleus [GO:0005634]; preribosome, small subunit precursor [GO:0030688]>FUNCTION: Plays a critical role in the generation of 28S rRNA.Q9Y385UB2J1"Ubiquitin-conjugating enzyme E2 J1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12082160}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12082160}.eER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; protein N-linked glycosylation via asparagine [GO:0018279]; protein ubiquitination [GO:0016567]; regulation of tumor necrosis factor biosynthetic process [GO:0042534]; spermatid development [GO:0007286]pcytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12082160, ECO:0000269|PubMed:22607976}.Q9BSU1CP070UPF0183 protein C16orf70P60842IF4A1!Eukaryotic initiation factor 4A-Icellular protein metabolic process [GO:0044267]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; organ regeneration [GO:0031100]; regulation of gene expression [GO:0010468]; RNA secondary structure unwinding [GO:0010501]; translation [GO:0006412]; translational initiation [GO:0006413]; viral process [GO:0016032][ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. {ECO:0000269|PubMed:19153607, ECO:0000269|PubMed:19204291}.P08758ANXA5 Annexin A5< ]activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; blood coagulation [GO:0007596]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood coagulation [GO:0030195]; negative regulation of catalytic activity [GO:0043086]; positive regulation of apoptotic process [GO:0043065]; positive regulation of defense response to virus by host [GO:0002230]; protein homooligomerization [GO:0051260]; regulation of sperm motility [GO:1901317]; response to calcium ion [GO:0051592]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; peptide hormone binding [GO:0017046]; phospholipase inhibitor activity [GO:0004859]; phospholipid binding [GO:0005543]ccell projection [GO:0042995]; cytoplasm [GO:0005737]; endothelial microparticle [GO:0072563]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.Q15388TOM203Mitochondrial import receptor subunit TOM20 homologSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101}; Single-pass membrane protein {ECO:0000255}.yP-P-bond-hydrolysis-driven protein transmembrane transporter activity [GO:0015450]; unfolded protein binding [GO:0051082]ER-mitochondrion membrane contact site [GO:0044233]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]|FUNCTION: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). {ECO:0000250}.Q9NRP0OSTC.Oligosaccharyltransferase complex subunit OSTC:protein N-linked glycosylation via asparagine [GO:0018279][integral component of membrane [GO:0016021]; oligosaccharyltransferase complex [GO:0008250]Q9UBB6NCDN NeurochondrinrSUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, dendrite. Note=Localizes to somatic regions of neurons.bone resorption [GO:0045453]; neuron projection development [GO:0031175]; regulation of neuronal synaptic plasticity [GO:0048168]ccytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; neuronal cell body [GO:0043025]jFUNCTION: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling (By similarity). Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth. {ECO:0000250, ECO:0000269|PubMed:16945926}.Q9Y657SPIN1 Spindlin-1chromatin modification [GO:0016568]; gamete generation [GO:0007276]; meiotic cell cycle [GO:0051321]; multicellular organismal development [GO:0007275]; positive regulation of Wnt signaling pathway [GO:0030177]; rRNA transcription [GO:0009303]; Wnt signaling pathway [GO:0016055]Bnucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption. {ECO:0000269|PubMed:21960006, ECO:0000269|PubMed:22258766, ECO:0000269|PubMed:24589551}.Q15427SF3B4Splicing factor 3B subunit 4gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]gnucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]FUNCTION: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.P61106RAB14Ras-related protein Rab-14SUBCELLULAR LOCATION: Recycling endosome. Early endosome membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to recycling endosomes by DENND6A. Recruited to phagosomes containing S.aureus or M.tuberculosis.papical protein localization [GO:0045176]; body fluid secretion [GO:0007589]; defense response to bacterium [GO:0042742]; embryo development [GO:0009790]; endocytic recycling [GO:0032456]; fibroblast growth factor receptor signaling pathway [GO:0008543]; Golgi to endosome transport [GO:0006895]; intracellular protein transport [GO:0006886]; intracellular transport [GO:0046907]; membrane organization [GO:0061024]; phagolysosome assembly involved in apoptotic cell clearance [GO:0090387]; Rab protein signal transduction [GO:0032482]; regulation of protein localization [GO:0032880]; vesicle-mediated transport [GO:0016192]Ralveolar lamellar body [GO:0097208]; apical plasma membrane [GO:0016324]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; nuclear outer membrane-endoplasmic reticulum membrane network [GO:0042175]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; rough endoplasmic reticulum [GO:0005791]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140]FUNCTION: Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by mod< ulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion. {ECO:0000250, ECO:0000269|PubMed:22595670}.P54136SYRC"Arginine--tRNA ligase, cytoplasmic[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:16430231}.arginyl-tRNA aminoacylation [GO:0006420]; gene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]~arginine binding [GO:0034618]; arginine-tRNA ligase activity [GO:0004814]; ATP binding [GO:0005524]; tRNA binding [GO:0000049]aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]"FUNCTION: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1. {ECO:0000269|PubMed:17443684}.Q9H6L2TM231Transmembrane protein 231SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to the transition zone of primary cilia; SEPT2 is required for localization to the transition zone. {ECO:0000250}.Gcilium assembly [GO:0042384]; smoothened signaling pathway [GO:0007224]ciliary membrane [GO:0060170]; ciliary transition zone [GO:0035869]; integral component of membrane [GO:0016021]; TCTN-B9D complex [GO:0036038]HFUNCTION: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling (By similarity). {ECO:0000250}.Q13976KGP1cGMP-dependent protein kinase 1Gap junction(89)qSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized with TRPC7 in the plasma membrane. {ECO:0000250}. actin cytoskeleton organization [GO:0030036]; activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; blood coagulation [GO:0007596]; cGMP-mediated signaling [GO:0019934]; dendrite development [GO:0016358]; forebrain development [GO:0030900]; negative regulation of platelet aggregation [GO:0090331]; neuron migration [GO:0001764]; protein phosphorylation [GO:0006468]; regulation of GTPase activity [GO:0043087]; relaxation of vascular smooth muscle [GO:0060087]; signal transduction [GO:0007165]ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]hcytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] FUNCTION: Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. {ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11162591, ECO:0000269|PubMed:11723116, ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:14608379, ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:8182057}.Q9H6K4OPA3Optic atrophy 3 proteingrowth [GO:0040007]; mitochondrion morphogenesis [GO:0070584]; neuromuscular process [GO:0050905]; regulation of lipid metabolic process [GO:0019216]; response to stimulus [GO:0050896]; visual perception [GO:0007601]8FUNCTION: May play some role in mitochondrial processes.P29536LMOD1 Leiomodin-1uSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11350761}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11350761}.actin filament organization [GO:0007015]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694] tropomyosin binding [GO:0005523]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]O75663TIPRLTIP41-like protein>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17944932}.lDNA damage checkpoint [GO:0000077]; negative regulation of protein phosphatase type 2A activity [GO:0034048]jFUNCTION: May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair. {ECO:0000269|PubMed:17384681}.Q9C0E8LNPProtein lunaparkSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22729086}; Multi-pass membrane protein {ECO:0000269|PubMed:22729086}. Note=Localizes to three-way ER tubule junctions.blood coagulation [GO:0007596]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; endoplasmic reticulum tubular network organization [GO:0071786]; limb development [GO:0060173]; regulation of chondrocyte differentiation [GO:0032330]endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum tubular network [GO:0071782]; integral component of membrane [GO:0016021]FUNCTION: Plays a role in tubular endoplasmic reticulum network formation and maintenance. May be involved in limb and central nervous system development. {ECO:0000250}.O60513B4GT4 Beta-1,4-galactosyltransferase 4SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; membrane lipid metabolic process [GO:0006643]; post-translati< onal protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]nGolgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed:9792633}.Q8IWV7UBR1 E3 ubiquitin-protein ligase UBR1GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16311597}.cellular response to leucine [GO:0071233]; negative regulation of TOR signaling [GO:0032007]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]leucine binding [GO:0070728]; ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]tcytoplasm [GO:0005737]; cytosol [GO:0005829]; proteasome complex [GO:0000502]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:20298436, ECO:0000269|PubMed:20835242}.P09661RU2A%U2 small nuclear ribonucleoprotein A'?poly(A) RNA binding [GO:0044822]; U2 snRNA binding [GO:0030620]catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]nFUNCTION: This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA.P36957ODO2pDihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial2-oxoglutarate metabolic process [GO:0006103]; cellular metabolic process [GO:0044237]; cellular nitrogen compound metabolic process [GO:0034641]; generation of precursor metabolites and energy [GO:0006091]; L-lysine catabolic process to acetyl-CoA via saccharopine [GO:0033512]; lysine catabolic process [GO:0006554]; NADH metabolic process [GO:0006734]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]Edihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252]; plasma membrane [GO:0005886]&FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).Q2M2I8AAK1AP2-associated protein kinase 1jSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250}.4endocytosis [GO:0006897]; positive regulation of Notch signaling pathway [GO:0045747]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of clathrin-mediated endocytosis [GO:2000369]; regulation of protein localization [GO:0032880]AP-2 adaptor complex binding [GO:0035612]; ATP binding [GO:0005524]; Notch binding [GO:0005112]; protein serine/threonine kinase activity [GO:0004674]cell leading edge [GO:0031252]; clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; extrinsic component of plasma membrane [GO:0019897]; terminal bouton [GO:0043195]0FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity. {ECO:0000269|PubMed:12952931, ECO:0000269|PubMed:17494869, ECO:0000269|PubMed:18657069, ECO:0000269|PubMed:21464124}.Q8TCZ2C99L2CD99 antigen-like protein 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250}.ffocal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]CFUNCTION: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity). {ECO:0000250}.Q70E73RAPH1CRas-associated and pleckstrin homology domains-containing protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15469845}; Peripheral membrane protein {ECO:0000269|PubMed:15469845}; Cytoplasmic side {ECO:0000269|PubMed:15469845}. Cell projection, lamellipodium {ECO:0000269|PubMed:15469845}. Cell projection, filopodium {ECO:0000269|PubMed:15469845}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15469845}. Note=Recruited to the membrane, via the PH domain, by the phosphoinositide, PI(3,4)P2. Colocalizes with ENAH/VASP at the tips of lamellipodia and filopodia. Also colocalizes with the pathogens, Vaccinia and Enteropathogenic E.coli (EPEC) at the interface between the pathogen and their actin.`axon extension [GO:0048675]; cell-matrix adhesion [GO:0007160]; signal transduction [GO:0007165]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]FUNCTION: Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.Q8TBR7FA57AProtein FAM57AASUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.Q9Y3B8ORN Oligoribonuclease, mitochondrialSUBCELLULAR LOCATION: Isoform 1: Mitochondrion intermembrane space. Mitochondrion matrix.; SUBCELLULAR LOCATION: Isoform 2: Nucleus.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.nucleic acid phosphodiester bond hydrolysis [GO:0090305]; nucleobase-containing compound metabolic process [GO:0006139]; nucleotide metabolic process [GO:0009117]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]w3'-5' exonuclease activity [GO:0008408]; 3'-5'-exoribonuclease activity [GO:0000175]; nucleic acid binding [GO:0003676]focal adhesion [GO:0005925]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. Active on small (primarily Putative cytochrome b-c1 complex subunit Rieske-like protein 1P78527PRKDC.DNA-dependent protein kinase catalytic subunitNon-homologous end-joiningB cell lineage commitment [GO:0002326]; brain development [GO:0007420]; cellular protein modification process [GO:0006464]; cellular response to insulin stimulus [GO:0032869]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; ectopic germ cell programmed cell death [GO:0035234]; heart development [GO:0007507]; immunoglobulin V(D)J recombination [GO:0033152]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cellular senescence [GO:2000773]; negative regulation of immunoglobulin production [GO:0002638]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of response to gamma radiation [GO:2001229]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental growth [GO:0048639]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of immune system process [GO:0002684]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; pro-B cell differentiation [GO:0002328]; protein destabilization [GO:0031648]; regulation of circadian rhythm [GO:0042752]; regulation of smooth muscle cell proliferation [GO:0048660]; response to activity [GO:0014823]; response to gamma radiation [GO:0010332]; rhythmic process [GO:0048511]; signal transduction involved in mitotic G1 DNA damage checkpoint [GO:0072431]; somitogenesis [GO:0001756]; spleen development [GO:0048536]; T cell differentiation in thymus [GO:0033077]; T cell lineage commitment [GO:0002360]; T cell receptor V(D)J recombination [GO:0033153]; telomere maintenance [GO:0000723]; thymus development [GO:0048538] ATP binding [GO:0005524]; DNA-dependent protein kinase activity [GO:0004677]; double-stranded DNA binding [GO:0003690]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; transcription factor binding [GO:0008134]cytosol [GO:0005829]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; membrane [GO:0016020]; nonhomologous end joining complex [GO:0070419]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; transcription factor complex [GO:0005667]FUNCTION: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC< 6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect machanism. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation. {ECO:0000269|PubMed:12649176, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:9679063}.P51790CLCN3!H(+)/Cl(-) exchange transporter 3SUBCELLULAR LOCATION: Isoform 1: Membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Isoform 1 is localized mainly in early and late endosomes.; SUBCELLULAR LOCATION: Isoform 2: Membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Isoform 2 partially colocalized with isoform 1 but is mainly enriched in the Golgi.adult locomotory behavior [GO:0008344]; chloride transmembrane transport [GO:1902476]; endosomal lumen acidification [GO:0048388]; ion transmembrane transport [GO:0034220]; negative regulation of cell volume [GO:0045794]; phagocytosis, engulfment [GO:0006911]; photoreceptor cell maintenance [GO:0045494]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; regulation of anion transmembrane transport [GO:1903959]; regulation of anion transport [GO:0044070]; regulation of pH [GO:0006885]; synaptic transmission, GABAergic [GO:0051932]; synaptic transmission, glutamatergic [GO:0035249]; synaptic vesicle lumen acidification [GO:0097401]; transmembrane transport [GO:0055085]; transport [GO:0006810]Tantiporter activity [GO:0015297]; ATP binding [GO:0005524]; chloride channel activity [GO:0005254]; PDZ domain binding [GO:0030165]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; voltage-gated chloride channel activity [GO:0005247]; volume-sensitive chloride channel activity [GO:0072320]naxon terminus [GO:0043679]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; specific granule [GO:0042581]; synaptic vesicle [GO:0008021]; transport vesicle membrane [GO:0030658]; vesicle membrane [GO:0012506]FUNCTION: Mediates the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the endosome and synaptic vesicle lumen, and may thereby affect vesicle trafficking and exocytosis. May play an important role in neuronal cell function through regulation of membrane excitability by protein kinase C. It could help neuronal cells to establish short-term memory. {ECO:0000269|PubMed:11967229}.Q5BJH7YIF1B Protein YIF1BQ9UPN7PP6R1;Serine/threonine-protein phosphatase 6 regulatory subunit 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:18186651}.>regulation of phosphoprotein phosphatase activity [GO:0043666](protein phosphatase binding [GO:0019903]P09486SPRCSPARCSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:2306517, ECO:0000269|PubMed:3400777, ECO:0000269|PubMed:7495300, ECO:0000269|PubMed:9457905}. Note=In or around the basement membrane.>blood coagulation [GO:0007596]; bone development [GO:0060348]; cellular response to growth factor stimulus [GO:0071363]; extracellular matrix organization [GO:0030198]; heart development [GO:0007507]; inner ear development [GO:0048839]; lung development [GO:0030324]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; ossification [GO:0001503]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of endothelial cell migration [GO:0010595]; receptor-mediated endocytosis [GO:0006898]; regulation of cell morphogenesis [GO:0022604]; response to cadmium ion [GO:0046686]; response to calcium ion [GO:0051592]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]; response to ethanol [GO:0045471]; response to glucocorticoid [GO:0051384]; response to gravity [GO:0009629]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to lipopolysaccharide [GO:0032496]; response to peptide hormone [GO:0043434]; signal transduction [GO:0007165]jcalcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]Wbasement membrane [GO:0005604]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endocytic vesicle lumen [GO:0071682]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear matrix [GO:0016363]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]; platelet alpha granule membrane [GO:0031092]wFUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.Q8TB61S35B24Adenosine 3'-phospho 5'-phosphosulfate transporter 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12716889}; Multi-pass membrane protein {ECO:0000269|PubMed:12716889}.Z3'-phospho-5'-adenylyl sulfate transmembrane transport [GO:1902559]; 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; 3'-phosphoadenosine 5'-phosphosulfate transport [GO:0046963]; carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; xenobiotic metabolic process [GO:0006805]~3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity [GO:0046964]; signal transducer activity [GO:0004871]}Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020].FUNCTION: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF-kappa-B and MAPK pathways. {ECO:0000269|PubMed:12716889}.Q9BVS4RIOK2$Serine/threonine-protein kinase RIO2Ribosome biogenesis(56)P26038MOESMoesinSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Apical cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment. {ECO:0000250, ECO:0000269|PubMed:18586956}.Fcellular response to testosterone stimulus [GO:0071394]; establishment of endo< thelial barrier [GO:0061028]; establishment of epithelial cell apical/basal polarity [GO:0045198]; gland morphogenesis [GO:0022612]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; membrane to membrane docking [GO:0022614]; movement of cell or subcellular component [GO:0006928]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of gene expression [GO:0010628]; positive regulation of protein localization to early endosome [GO:1902966]; regulation of cell shape [GO:0008360]; regulation of cell size [GO:0008361]; regulation of lymphocyte migration [GO:2000401]; regulation of organelle assembly [GO:1902115]cell adhesion molecule binding [GO:0050839]; double-stranded RNA binding [GO:0003725]; protein kinase binding [GO:0019901]; receptor binding [GO:0005102]; structural constituent of cytoskeleton [GO:0005200]apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of membrane [GO:0019898]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]; uropod [GO:0001931]; vesicle [GO:0031982]FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. {ECO:0000269|PubMed:21549406}.Q8NE71ABCF1*ATP-binding cassette sub-family F member 1SSUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus, nucleoplasm. Nucleus envelope.inflammatory response [GO:0006954]; positive regulation of translation [GO:0045727]; translation [GO:0006412]; translational initiation [GO:0006413]; transmembrane transport [GO:0055085]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]; translation activator activity [GO:0008494]; translation factor activity, RNA binding [GO:0008135]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; polysomal ribosome [GO:0042788]; ribosome [GO:0005840]FUNCTION: Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis. {ECO:0000269|PubMed:19570978}.O75915PRAF3PRA1 family protein 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Also exists as a soluble form in the cytoplasm. Associated with microtubules (By similarity). {ECO:0000250}.intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; L-glutamate transport [GO:0015813]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of transport [GO:0051051]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of stress-activated MAPK cascade [GO:0032874]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Regulates intracellular concentrations of taurine and glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate. May be involved in membrane traffic (By similarity). {ECO:0000250}.Q6UXN9WDR82WD repeat-containing protein 82SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16253997, ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:20516061}. Note=Associates with chromatin.&histone H3-K4 methylation [GO:0051568]chromatin binding [GO:0003682]chromatin [GO:0000785]; histone methyltransferase complex [GO:0035097]; PTW/PP1 phosphatase complex [GO:0072357]; Set1C/COMPASS complex [GO:0048188]OFUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061}.Q8NB90SPAT5$Spermatogenesis-associated protein 5KSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}.2cytoplasm [GO:0005737]; mitochondrion [GO:0005739]~FUNCTION: May be involved in morphological and functional mitochondrial transformations during spermatogenesis. {ECO:0000250}.Q9NXW2DJB12"DnaJ homolog subfamily B member 12Q12972PP1R8*Nuclear inhibitor of protein phosphatase 1SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Primarily, but not exclusively, nuclear.; SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm. Note=Found mainly in the cytoplasm.Icell proliferation [GO:0008283]; mRNA processing [GO:0006397]; negative regulation of catalytic activity [GO:0043086]; regulation of transcription, DNA-templated [GO:0006355]; RNA catabolic process [GO:0006401]; RNA phosphodiester bond hydrolysis [GO:0090501]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; protein phosphatase type 1 regulator activity [GO:0008599]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; ribonuclease E activity [GO:0008995]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]dFUNCTION: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.; FUNCTION: Isoform Gamma is a site-specific single-strand endoribonuclease that cleaves single strand RNA 3' to purines and pyrimidines in A+U-rich regions. It generates 5'-phosphate termini at the site of cleavage. This isoform does not inhibit PP-1. May be implicated in mRNA splicing.P55287CAD11 Cadherin-11]adherens junction organization [GO:0034332]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; corticospinal tract morphogenesis [GO:0021957]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; ossification [GO:0001503]; skeletal system development [GO:0001501]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.O95273CCDB1Cyclin-D1-binding protein 1CDK inhibitors - inhibitor>cell cycle [GO:0007049]; regulation of cell cycle [GO:0051726]FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription. {ECO:0000269|PubMed:10801854}.Q8NC60NOA1!Nitric oxide-associated protein 1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:19103604}; Peripheral membrane protein {ECO< :0000269|PubMed:19103604}; Matrix side {ECO:0000269|PubMed:19103604}.apoptotic process [GO:0006915]; mitochondrial translation [GO:0032543]; regulation of cell death [GO:0010941]; regulation of cellular respiration [GO:0043457]; ribosome biogenesis [GO:0042254]FUNCTION: Involved in regulation of mitochondrial protein translation and respiration. Plays a role in mitochondria-mediated cell death. May act as a scaffolding protein or stabilizer of respiratory chain supercomplexes. Binds GTP. {ECO:0000269|PubMed:19103604}.O43719HTSF1HIV Tat-specific factor 1XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:8849451}.regulation of DNA-templated transcription, elongation [GO:0032784]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]; viral genome replication [GO:0019079]WFUNCTION: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:11780068, ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451, ECO:0000269|PubMed:9765201}.O00330ODPX9Pyruvate dehydrogenase protein X component, mitochondrial;transferase activity, transferring acyl groups [GO:0016746]Nmitochondrial matrix [GO:0005759]; pyruvate dehydrogenase complex [GO:0045254]FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.Q9BS40LXNLatexinydetection of temperature stimulus involved in sensory perception of pain [GO:0050965]; inflammatory response [GO:0006954]Rheparin binding [GO:0008201]; metalloendopeptidase inhibitor activity [GO:0008191]FUNCTION: Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4. May play a role in inflammation. {ECO:0000269|PubMed:15738388}.Q13347EIF3I4Eukaryotic translation initiation factor 3 subunit IBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.cellular protein metabolic process [GO:0044267]; formation of translation preinitiation complex [GO:0001731]; gene expression [GO:0010467]; regulation of translational initiation [GO:0006446]; translation [GO:0006412]; translational initiation [GO:0006413]'cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; extracellular exosome [GO:0070062]P36383CXG1Gap junction gamma-1 protein^SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.atrial cardiac muscle cell action potential [GO:0086014]; cardiac muscle tissue development [GO:0048738]; cell-cell junction assembly [GO:0007043]; cell development [GO:0048468]; gap junction assembly [GO:0016264]; membrane organization [GO:0061024]; muscle contraction [GO:0006936]; synaptic transmission [GO:0007268]; transport [GO:0006810]; vasculogenesis [GO:0001570]; visual perception [GO:0007601]Mgap junction channel activity [GO:0005243]; ion channel activity [GO:0005216]connexon complex [GO:0005922]; endoplasmic reticulum membrane [GO:0005789]; gap junction [GO:0005921]; integral component of membrane [GO:0016021]; intercalated disc [GO:0014704]; plasma membrane [GO:0005886]FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.Q8NB37PDDC1/Parkinson disease 7 domain-containing protein 1Q9UP38FZD1 Frizzled-1SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.autocrine signaling [GO:0035425]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation [GO:0044338]; canonical Wnt signaling pathway involved in osteoblast differentiation [GO:0044339]; cell-cell signaling [GO:0007267]; cellular response to growth factor stimulus [GO:0071363]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to vitamin D [GO:0071305]; epithelial cell differentiation [GO:0030855]; hard palate development [GO:0060022]; lung alveolus development [GO:0048286]; membranous septum morphogenesis [GO:0003149]; muscular septum morphogenesis [GO:0003150]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of catenin import into nucleus [GO:0035414]; negative regulation of transcription, DNA-templated [GO:0045892]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of osteoblast differentiation [GO:0045667]; response to drug [GO:0042493]frizzled binding [GO:0005109]; G-protein coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]; receptor binding [GO:0005102]; Wnt-activated receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]cell surface [GO:0009986]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]xFUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activated by Wnt3A, Wnt3, Wnt1 and to a lesser extent Wnt2, but not by Wnt4, Wnt5A, Wnt5B, Wnt6, Wnt7A or Wnt7B.P21266GSTM3Glutathione S-transferase Mu 3cellular detoxification of nitrogen compound [GO:0070458]; establishment of blood-nerve barrier [GO:0008065]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; nitrobenzene metabolic process [GO:0018916]; response to estrogen [GO:0043627]; small molecule metabolic process [GO:0044281]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]enzyme binding [GO:0019899]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686] FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers. {ECO:0000269|PubMed:10587441}.Q9NWS8RMND17Required for< meiotic nuclear division protein 1 homolog_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:23022099}.FUNCTION: Required for mitochondrial translation, possibly by coordinating the assembly or maintenance of the mitochondrial ribosome. {ECO:0000269|PubMed:23022098}.O60885BRD4 Bromodomain-containing protein 4SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with acetylated chromatin. Released from chromatin upon deacetylation of histones that can be triggered by different signals such as activation of the JNK pathway or nocodazole treatment.cellular response to DNA damage stimulus [GO:0006974]; chromatin remodeling [GO:0006338]; chromosome segregation [GO:0007059]; histone H3-K14 acetylation [GO:0044154]; histone H4-K12 acetylation [GO:0043983]; inner cell mass cell proliferation [GO:0001833]; negative regulation of DNA damage checkpoint [GO:2000002]; positive regulation of DNA binding [GO:0043388]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of inflammatory response [GO:0050727]; regulation of phosphorylation of RNA polymerase II C-terminal domain [GO:1901407]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039]chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; positive transcription elongation factor complex b [GO:0008024]TFUNCTION: Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters. {ECO:0000269|PubMed:22509028}.; FUNCTION: Isoform B: Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AFX/H2A.x phosphorylation.P78324SHPS1:Tyrosine-protein phosphatase non-receptor type substrate 1Osteoclast differentiationchemokine(PC00074)\blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; leukocyte migration [GO:0050900]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]=FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. {ECO:0000250, ECO:0000269|PubMed:10469599, ECO:0000269|PubMed:11509594}.Q9BV23ABHD6Monoacylglycerol lipase ABHD6SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion {ECO:0000250|UniProtKB:Q8R2Y0}.6acylglycerol catabolic process [GO:0046464]; long term synaptic depression [GO:0060292]; negative regulation of cell migration [GO:0030336]; phospholipid catabolic process [GO:0009395]; positive regulation of lipid biosynthetic process [GO:0046889]; regulation of endocannabinoid signaling pathway [GO:2000124]Nacylglycerol lipase activity [GO:0047372]; phospholipase activity [GO:0004620]alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [GO:0032281]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. May also have a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). {ECO:0000250|UniProtKB:Q8R2Y0, ECO:0000269|PubMed:22969151}.P15407FOSL1Fos-related antigen 1cellular defense response [GO:0006968]; cellular response to extracellular stimulus [GO:0031668]; chemotaxis [GO:0006935]; female pregnancy [GO:0007565]; in utero embryonic development [GO:0001701]; learning [GO:0007612]; negative regulation of cell proliferation [GO:0008285]; placenta blood vessel development [GO:0060674]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA-templated transcription, initiation [GO:2000144]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to cAMP [GO:0051591]; response to corticosterone [GO:0051412]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to gravity [GO:0009629]; response to hydrogen peroxide [GO:0042542]; response to mechanical stimulus [GO:0009612]; response to progesterone [GO:0032570]; response to virus [GO:0009615]; transcription from RNA polymerase II promoter [GO:0006366]; vitellogenesis [GO:0007296]ORNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytosol [GO:0005829]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynaptic membrane [GO:0042734]Q92769HDAC2Histone deacetylase 2!co-repressor(hairless-groucho)(6)eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24970816}. Cytoplasm {ECO:0000269|PubMed:24970816}. ATP-dependent chromatin remod< eling [GO:0043044]; behavioral response to ethanol [GO:0048149]; blood coagulation [GO:0007596]; cardiac muscle hypertrophy [GO:0003300]; cellular response to dopamine [GO:1903351]; cellular response to heat [GO:0034605]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; dendrite development [GO:0016358]; embryonic digit morphogenesis [GO:0042733]; epidermal cell differentiation [GO:0009913]; eyelid development in camera-type eye [GO:0061029]; fungiform papilla formation [GO:0061198]; gene expression [GO:0010467]; hair follicle placode formation [GO:0060789]; histone deacetylation [GO:0016575]; histone H3 deacetylation [GO:0070932]; histone H4 deacetylation [GO:0070933]; maintenance of chromatin silencing [GO:0006344]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell cycle [GO:0045786]; negative regulation of dendritic spine development [GO:0061000]; negative regulation of DNA binding [GO:0043392]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of neuron projection development [GO:0010977]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neurotrophin TRK receptor signaling pathway [GO:0048011]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of cell proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of proteolysis [GO:0045862]; positive regulation of receptor biosynthetic process [GO:0010870]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of Stat3 protein [GO:0042517]; regulation of gene expression, epigenetic [GO:0040029]; response to amphetamine [GO:0001975]; response to caffeine [GO:0031000]; response to cocaine [GO:0042220]; response to drug [GO:0042493]; response to hyperoxia [GO:0055093]; response to lipopolysaccharide [GO:0032496]; response to nicotine [GO:0035094]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; deacetylase activity [GO:0019213]; enzyme binding [GO:0019899]; histone deacetylase activity [GO:0004407]; NAD-dependent histone deacetylase activity (H3-K14 specific) [GO:0032041]; NF-kappaB binding [GO:0051059]; poly(A) RNA binding [GO:0044822]; protein deacetylase activity [GO:0033558]; RNA polymerase II repressing transcription factor binding [GO:0001103]; sequence-specific DNA binding [GO:0043565]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; ESC/E(Z) complex [GO:0035098]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; protein complex [GO:0043234]; Sin3 complex [GO:0016580]fFUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. {ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678}.P50583AP4A1Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]]apoptotic process [GO:0006915]; nucleobase-containing compound metabolic process [GO:0006139]bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity [GO:0004081]; bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity [GO:0008803]; GTP binding [GO:0005525]mFUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.Q96M69LRGUKBLeucine-rich repeat and guanylate kinase domain-containing protein6ATP binding [GO:0005524]; kinase activity [GO:0016301]P47755CAZA2'F-actin-capping protein subunit alpha-2barbed-end actin filament capping [GO:0051016]; blood coagulation [GO:0007596]; innate immune response [GO:0045087]; movement of cell or subcellular component [GO:0006928]; protein complex assembly [GO:0006461]actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; cortical cytoskeleton [GO:0030863]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; F-actin capping protein complex [GO:0008290]; membrane [GO:0016020]#FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.A1L188CQ089 Uncharacterized protein C17orf89Q9Y237PIN46Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Note=Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Mitochondrion matrix. Note=Imported in a time- and membrane potential-dependent manner to the mitochondrial matrix, but without concomitant processing of the protein. Directed to mitochondria by a novel N-terminal domain that functions as non-cleavable mitochondrial targeting peptide.bent DNA binding [GO:0003681]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; nucleolus [GO:0005730]; nucleus [GO:0005634]; preribosome [GO:0030684]; spindle [GO:0005819] FUNCTION: Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA. {ECO:0000269|PubMed:19369196}.; FUNCTION: Isoform 2 binds to double-stranded DNA. {ECO:0000269|PubMed:19369196}.Q9H3N1TMX1+Thioredoxin-related transmembrane protein 1SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly found in the endoplasmic reticulum. {ECO:0000269|PubMed:11152479}.xcell redox homeostasis [GO:0045454]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]adisulfide oxidoreductase activity [GO:0015036]; protein disulfide isomerase activity [GO:0003756]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; n< ucleolus [GO:0005730]FUNCTION: May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.Q9H063MAF1:Repressor of RNA polymerase III transcription MAF1 homolognegative regulation of transcription from RNA polymerase III promoter [GO:0016480]; transcription, DNA-templated [GO:0006351]; transcription factor TFIIIB complex assembly [GO:0070217]RNA polymerase III core binding [GO:0000994]; RNA polymerase III type 1 promoter DNA binding [GO:0001030]; RNA polymerase III type 2 promoter DNA binding [GO:0001031]; RNA polymerase III type 3 promoter DNA binding [GO:0001032]waxon [GO:0030424]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; inhibitory synapse [GO:0060077]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Element of the mTORC1 signaling pathway that acts as a mediator of diverse signals and that represses RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA. {ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138}.Q13325IFIT5;Interferon-induced protein with tetratricopeptide repeats 5SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000269|PubMed:23317505}. Note=Colocalized with DDX58/RIG-I at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.Kdefense response to virus [GO:0051607]; innate immune response [GO:0045087]poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]; tRNA binding [GO:0000049]_actin cytoskeleton [GO:0015629]; apical part of cell [GO:0045177]; ruffle membrane [GO:0032587]TFUNCTION: Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs. {ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:23334420}.Q9UMY4SNX12Sorting nexin-12xSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.endocytosis [GO:0006897]; negative regulation of early endosome to late endosome transport [GO:2000642]; negative regulation of gene expression [GO:0010629]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein processing [GO:0010955]; negative regulation of protein transport [GO:0051224]; protein transport [GO:0015031]; regulation of endocytosis [GO:0030100]; vesicle organization [GO:0016050]Fenzyme binding [GO:0019899]; phosphatidylinositol binding [GO:0035091]mearly endosome [GO:0005769]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]XFUNCTION: May be involved in several stages of intracellular trafficking. {ECO:0000250}.P61020RAB5BRas-related protein Rab-5BQSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065}; Lipid-anchor {ECO:0000269|PubMed:17081065}; Cytoplasmic side {ECO:0000269|PubMed:17081065}. Early endosome membrane {ECO:0000269|PubMed:17081065}; Lipid-anchor {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I melanosomes. antigen processing and presentation [GO:0019882]; endosome organization [GO:0007032]; intracellular protein transport [GO:0006886]; plasma membrane to endosome transport [GO:0048227]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]|GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]P62341SELTSelenoprotein TNcell redox homeostasis [GO:0045454]; selenocysteine incorporation [GO:0001514]cell [GO:0005623]O43809CPSF59Cleavage and polyadenylation specificity factor subunit 5igene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; protein tetramerization [GO:0051262]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]AU-rich element binding [GO:0017091]; histone deacetylase binding [GO:0042826]; hydrolase activity [GO:0016787]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]centrosome [GO:0005813]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; paraspeckles [GO:0042382]FUNCTION: Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export. {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.P49146NPY2RNeuropeptide Y receptor type 2adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; behavioral fear response [GO:0001662]; cardiac left ventricle morphogenesis [GO:0003214]; locomotory behavior [GO:0007626]; negative regulation of cAMP biosynthetic process [GO:0030818]; negative regulation of excitatory postsynaptic membrane potential [GO:0090394]; negative regulation of feeding behavior [GO:2000252]; negative regulation of neurological system process [GO:0031645]; negative regulation of secretion [GO:0051048]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; neuropeptide signaling pathway [GO:0007218]; nitric oxide mediated signal transduction [GO:0007263]; outflow tract morphogenesis [GO:0003151]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of circadian sleep/wake cycle, non-REM sleep [GO:0046010]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of dopamine secretion [GO:0033603]; positive regulation of peptide secretion [GO:0002793]; positive regulation of smooth muscle contraction [GO:0045987]; regulation of sensory perception of pain [GO:0051930]; secretion [GO:0046903]calcium channel regulator activity [GO:0005246]; neuropeptide Y receptor activity [GO:0004983]; peptide YY receptor activity [GO:0001601]; receptor activity [GO:0004872]cytosol [GO:0005829]; integral component of plasma membrane [GO:0005887]; nonmotile primary cilium [GO:0031513]; plasma membrane [GO:0005886]FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PYY > NPY > PYY (3-36) > NPY (2-36) > [Ile-31, Gln-34] PP > [Leu-31, Pro-34] NPY > PP, [Pro-34] PYY and NPY free acid.Q9P2E5CHPF2)Chondroitin sulfate glucuronyltransferase~SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondro< itin sulfate metabolic process [GO:0030204]; glycosaminoglycan metabolic process [GO:0030203]; small molecule metabolic process [GO:0044281]acetylgalactosaminyltransferase activity [GO:0008376]; N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity [GO:0050510]Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020] FUNCTION: Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N-acetylgalactosaminyltransferase activity. {ECO:0000269|PubMed:12145278, ECO:0000269|PubMed:18316376}.P49756RBM25RNA-binding protein 25SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=Colocalizes predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear speckles. Cytoplasmic localization is faint.mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of apoptotic process [GO:0042981]; RNA splicing [GO:0008380]ocytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]FUNCTION: RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure. {ECO:0000269|PubMed:18663000, ECO:0000269|PubMed:21859973}.Q9Y3B4SF3B6Splicing factor 3B subunit 6blastocyst formation [GO:0001825]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]Dnucleoplasm [GO:0005654]; U12-type spliceosomal complex [GO:0005689]FUNCTION: Necessary for the splicing of pre-mRNA. Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing. Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively. {ECO:0000269|PubMed:16432215}.Q6UWE0LRSM1"E3 ubiquitin-protein ligase LRSAM1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15256501}. Note=Displays a punctuate distribution and localizes to a submembranal ring.negative regulation of endocytosis [GO:0045806]; protein autoubiquitination [GO:0051865]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent endocytosis [GO:0070086]; viral budding [GO:0046755]Pcytoplasm [GO:0005737]; extracellular region [GO:0005576]; membrane [GO:0016020]FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. {ECO:0000269|PubMed:15256501}.O75879GATB<Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrialbSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:9878253}.glutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681]; mitochondrial translation [GO:0032543]; translation [GO:0006412]ATP binding [GO:0005524]; glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity [GO:0050567]; translation factor activity, RNA binding [GO:0008135]Tglutamyl-tRNA(Gln) amidotransferase complex [GO:0030956]; mitochondrion [GO:0005739]>FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:19805282}.O75886STAM2%Signal transducing adapter molecule 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane {ECO:0000269|PubMed:12551915}; Peripheral membrane protein {ECO:0000269|PubMed:12551915}; Cytoplasmic side {ECO:0000269|PubMed:12551915}. endosomal transport [GO:0016197]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]UFUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). {ECO:0000250}.Q9BZG1RAB34Ras-related protein Rab-34BSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.<antigen processing and presentation [GO:0019882]; Golgi to plasma membrane protein transport [GO:0043001]; lysosome localization [GO:0032418]; phagosome-lysosome fusion [GO:0090385]; phagosome maturation [GO:0090382]; protein localization to plasma membrane [GO:0072659]; Rab protein signal transduction [GO:0032482]WGTPase activity [GO:0003924]; GTP binding [GO:0005525]; Ral GTPase binding [GO:0017160]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi stack [GO:0005795]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; vesicle [GO:0031982]@FUNCTION: Protein transport. Involved in the redistribution of lysosomes to the peri-Golgi region (By similarity). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. {ECO:0000250, ECO:0000269|PubMed:21255211}.P40222TXLNA Alpha-taxilinactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; B cell activation [GO:0042113]; cell proliferation [GO:0008283]; exocytosis [GO:0006887]hcytokine activity [GO:0005125]; high molecular weight B cell growth factor receptor binding [GO:0030372]FUNCTION: May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.Q9Y3D2MSRB22Methionine-R-sulfoxide reductase B2, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18424444}.actin filament polymerization [GO:0030041]; protein repair [GO:0030091]; regulation of transcription, DNA-templated [GO:0006355]; response to oxidative stress [GO:0006979]actin binding [GO:0003779]; peptide-methionine (R)-S-oxide reductase activity [GO:0033743]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]LFUNCTION: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxi< de back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Upon oxidative stress, may play a role in the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance. {ECO:0000269|PubMed:18424444}.Q9H6W3NO66FBifunctional lysine-specific demethylase and histidyl-hydroxylase NO66SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli.histone H3-K36 demethylation [GO:0070544]; histone H3-K4 demethylation [GO:0034720]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]fhistone demethylase activity (H3-K36 specific) [GO:0051864]; histone demethylase activity (H3-K4 specific) [GO:0032453]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]Fnucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation. {ECO:0000250, ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053, ECO:0000269|PubMed:23103944}.Q92785REQUZinc finger protein ubi-d4LSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=30% nuclear. 70% cytoplasmic.apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]yRNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]BAF-type complex [GO:0090544]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]FUNCTION: May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells.Q9H857NT5D2+5'-nucleotidase domain-containing protein 2Q15233NONO1Non-POU domain-containing octamer-binding proteinSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus speckle. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.circadian rhythm [GO:0007623]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; mRNA processing [GO:0006397]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; negative regulation of transcription, DNA-templated [GO:0045892]; regulation of circadian rhythm [GO:0042752]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]membrane [GO:0016020]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; paraspeckles [GO:0042382]; RNA polymerase II transcription factor complex [GO:0090575]kFUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:22416126}.P78330SERBPhosphoserine phosphatasecellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; dephosphorylation [GO:0016311]; L-serine biosynthetic process [GO:0006564]; L-serine metabolic process [GO:0006563]; response to mechanical stimulus [GO:0009612]; response to nutrient levels [GO:0031667]; response to testosterone [GO:0033574]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; phosphoserine phosphatase activity [GO:0004647]; protein homodimerization activity [GO:0042803]Lcytoplasm [GO:0005737]; cytosol [GO:0005829]; neuron projection [GO:0043005]FUNCTION: Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. {ECO:0000269|PubMed:12777757}.O00401WASL'Neural Wiskott-Aldrich syndrome proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated. {ECO:0000250}.&actin polymerization or depolymerization [GO:0008154]; axon guidance [GO:0007411]; cell division [GO:0051301]; cellular protein complex localization [GO:0034629]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; membrane budding [GO:0006900]; mitotic nuclear division [GO:0007067]; movement of cell or subcellular component [GO:0006928]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of membrane tubulation [GO:1903526]; nitric oxide metabolic process [GO:0046209]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; positive regulation of clathrin-mediated endocytosis [GO:2000370]; positive regulation of filopodium assembly [GO:0051491]; protein complex assembly [GO:0006461]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of protein localization< [GO:0032880]; regulation of transcription, DNA-templated [GO:0006355]; response to bacterium [GO:0009617]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; spindle localization [GO:0051653]; transcription, DNA-templated [GO:0006351]; vesicle organization [GO:0016050]; vesicle transport along actin filament [GO:0030050]&GTPase regulator activity [GO:0030695]:actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. {ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:22847007, ECO:0000269|PubMed:22921828}.Q99519NEUR1 Sialidase-1&SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.Dcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; ganglioside catabolic process [GO:0006689]; glycosphingolipid metabolic process [GO:0006687]; oligosaccharide catabolic process [GO:0009313]; positive regulation of neuron projection development [GO:0010976]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; regulation of myoblast proliferation [GO:2000291]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308]Ncell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886].FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. {ECO:0000269|PubMed:8985184}.Q14376GALEUDP-glucose 4-epimerasecarbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; small molecule metabolic process [GO:0044281]coenzyme binding [GO:0050662]; protein homodimerization activity [GO:0042803]; UDP-glucose 4-epimerase activity [GO:0003978]; UDP-N-acetylglucosamine 4-epimerase activity [GO:0003974]FUNCTION: Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids. {ECO:0000269|PubMed:22654673, ECO:0000303|PubMed:23732289}.O15162PLS1Phospholipid scramblase 1}SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Membrane; Lipid-anchor; Cytoplasmic side. Nucleus.!acute-phase response [GO:0006953]; apoptotic process [GO:0006915]; defense response to virus [GO:0051607]; negative regulation of viral genome replication [GO:0045071]; phosphatidylserine biosynthetic process [GO:0006659]; phospholipid scrambling [GO:0017121]; platelet activation [GO:0030168]; positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity [GO:2000373]; positive regulation of gene expression [GO:0010628]; positive regulation of innate immune response [GO:0045089]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060368]; regulation of mast cell activation [GO:0033003]; response to interferon-beta [GO:0035456]; transcription from RNA polymerase II promoter [GO:0006366]calcium ion binding [GO:0005509]; CD4 receptor binding [GO:0042609]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; epidermal growth factor receptor binding [GO:0005154]; phospholipid scramblase activity [GO:0017128]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; SH3 domain binding [GO:0017124],cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; FUNCTION: May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation.Q9BR61ACBD6,Acyl-CoA-binding domain-containing protein 6>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18268358}.?fatty-acyl-CoA binding [GO:0000062]; lipid binding [GO:0008289]FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids. {ECO:0000269|PubMed:18268358}.P57723PCBP4Poly(rC)-binding protein 4>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14612387}.>cytoplasm [GO:0005737]; ribonucleoprotein complex [GO:0030529]lFUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. {ECO:0000250}.Q68CQ7GL8D11Glycosyltransferase 8 domain-containing protein 1Q9H5V9CX056UPF0428 protein CXorf56O43264ZW10+Centromere/kinetochore protein zw10 homologOSUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm. In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone.ccell division [GO:0051301]; ER to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; meiotic nuclear division [GO:0007126]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic metaphase plate congression [GO:0007080]; mitotic si< ster chromatid segregation [GO:0000070]; protein complex assembly [GO:0006461]; protein localization to kinetochore [GO:0034501]; protein transport [GO:0015031]; regulation of exit from mitosis [GO:0007096]; small GTPase mediated signal transduction [GO:0007264]$centromeric DNA binding [GO:0019237]jcondensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Dsl1p complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; membrane [GO:0016020]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle pole [GO:0000922] FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}.Q14558KPRA:Phosphoribosyl pyrophosphate synthase-associated protein 1negative regulation of kinase activity [GO:0033673]; nucleobase-containing compound metabolic process [GO:0006139]; nucleotide biosynthetic process [GO:0009165]enzyme inhibitor activity [GO:0004857]; magnesium ion binding [GO:0000287]; ribose phosphate diphosphokinase activity [GO:0004749]5ribose phosphate diphosphokinase complex [GO:0002189]^FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.P13716HEM2%Delta-aminolevulinic acid dehydratasecellular response to interleukin-4 [GO:0071353]; cellular response to lead ion [GO:0071284]; heme biosynthetic process [GO:0006783]; porphyrin-containing compound metabolic process [GO:0006778]; protein homooligomerization [GO:0051260]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to activity [GO:0014823]; response to aluminum ion [GO:0010044]; response to amino acid [GO:0043200]; response to arsenic-containing substance [GO:0046685]; response to cadmium ion [GO:0046686]; response to cobalt ion [GO:0032025]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to glucocorticoid [GO:0051384]; response to herbicide [GO:0009635]; response to hypoxia [GO:0001666]; response to ionizing radiation [GO:0010212]; response to iron ion [GO:0010039]; response to lipopolysaccharide [GO:0032496]; response to mercury ion [GO:0046689]; response to methylmercury [GO:0051597]; response to oxidative stress [GO:0006979]; response to platinum ion [GO:0070541]; response to selenium ion [GO:0010269]; response to vitamin B1 [GO:0010266]; response to vitamin E [GO:0033197]; response to zinc ion [GO:0010043]; small molecule metabolic process [GO:0044281]catalytic activity [GO:0003824]; identical protein binding [GO:0042802]; lead ion binding [GO:0032791]; porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270] FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. {ECO:0000269|PubMed:11032836, ECO:0000269|PubMed:19812033}.Q96EK5KBPKIF1-binding proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975, ECO:0000269|PubMed:23427148}.pcell differentiation [GO:0030154]; mitochondrial transport [GO:0006839]; nervous system development [GO:0007399]kinesin binding [GO:0019894]5cytoskeleton [GO:0005856]; mitochondrion [GO:0005739]FUNCTION: Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development. {ECO:0000269|PubMed:16225668, ECO:0000269|PubMed:20621975, ECO:0000269|PubMed:23427148}.Q16629SRSF7&Serine/arginine-rich splicing factor 7eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11336712}. Cytoplasm {ECO:0000269|PubMed:11336712}.gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]`nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]jcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific. {ECO:0000269|PubMed:11336712, ECO:0000269|PubMed:12667464, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:18364396}.Q92599Septin-8SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In platelets, found in areas surrounding alpha-granules. {ECO:0000269|PubMed:15116257}.Mcytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; myelin sheath [GO:0043209]FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion. {ECO:0000250, ECO:0000269|PubMed:15116257, ECO:0000305}.Q8NC54KCT2/Keratinocyte-associated transmembrane protein 2Q8NHP6MSPD2(Motile sperm domain-containing protein 2P83876TXN4AThioredoxin-like protein 4AU5(7)cell division [GO:0051301]; gene expression [GO:0010467]; mitotic nuclear division [GO:0007067]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]}nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]FUNCTION: Essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly. {ECO:0000269|PubMed:10610776}.Q8N9N8EIF1A#Probable RNA-binding protein EIF1ADYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20644585, ECO:0000269|PubMed:22095125}.intermediate filament cytoskeleton [GO:0045111]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]FUNCTION: Plays a role into cellular response to oxidative stress. Decreases cell proliferation. {ECO:0000269|PubMed:20644585, ECO:0000269|PubMed:22095125}.Q9H078CLPB(Caseinolytic peptidase B protein homologBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25597510}.&cellular response to heat [GO:0034605]fFUNCTION: May function as a regulatory ATPase and be related to secretion/protein trafficking process.O43310CTIF0CBP80/20-dependent translation initiation factorRSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19648179}.nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translational initiation [GO:0006446]FUNCTION: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subuni< t of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:19648179}.P09211GSTP1Glutathione S-transferase P+SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19269317}. Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus {ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.cellular response to lipopolysaccharide [GO:0071222]; central nervous system development [GO:0007417]; common myeloid progenitor cell proliferation [GO:0035726]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; negative regulation of acute inflammatory response [GO:0002674]; negative regulation of apoptotic process [GO:0043066]; negative regulation of biosynthetic process [GO:0009890]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of leukocyte proliferation [GO:0070664]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of monocyte chemotactic protein-1 production [GO:0071638]; negative regulation of nitric-oxide synthase biosynthetic process [GO:0051771]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of tumor necrosis factor production [GO:0032720]; nitric oxide storage [GO:0035732]; positive regulation of superoxide anion generation [GO:0032930]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of stress-activated MAPK cascade [GO:0032872]; response to reactive oxygen species [GO:0000302]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]dinitrosyl-iron complex binding [GO:0035731]; glutathione transferase activity [GO:0004364]; JUN kinase binding [GO:0008432]; kinase regulator activity [GO:0019207]; nitric oxide binding [GO:0070026]; S-nitrosoglutathione binding [GO:0035730]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular [GO:0005622]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; TRAF2-GSTP1 complex [GO:0097057]; vesicle [GO:0031982]FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000269|PubMed:21668448}.Q9P1Z2CACO1;Calcium-binding and coiled-coil domain-containing protein 1eSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.Kintracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; protein C-terminus binding [GO:0008022]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nucleus [GO:0005634]FFUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions (By similarity). In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000250|UniProtKB:Q8CGU1, ECO:0000269|PubMed:24245781}.; FUNCTION: Seems to enhance inorganic pyrphosphatase thus activating phosphogluomutase (PMG). Probably functions as component of the calphoglin complex, which is involved in linking cellular metabolism (phosphate and glucose metabolism) with other core functions including protein synthesis and degradation, calcium signaling and cell growth. {ECO:0000269|Ref.1}.Q00688FKBP3)Peptidyl-prolyl cis-trans isomerase FKBP3cchaperone-mediated protein folding [GO:0061077]; protein peptidyl-prolyl isomerization [GO:0000413]FK506 binding [GO:0005528]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]; receptor activity [GO:0004872]Ycytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634] FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.Q8TEA8DTD1D-tyrosyl-tRNA(Tyr) deacylase 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}. Cytoplasm {ECO:0000305}. Note=Associated with chromatin at some replication origins containing functional DNA-unwinding elements.D-amino acid catabolic process [GO:0019478]; DNA replication [GO:0006260]; regulation of translational fidelity [GO:0006450]; tRNA metabolic process [GO:0006399]aminoacyl-tRNA editing activity [GO:0002161]; DNA binding [GO:0003677]; D-tyrosyl-tRNA(Tyr) deacylase activity [GO:0051500]; metal ion binding [GO:0046872]4FUNCTION: ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine. {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}.Q9HCS7SYF1Pre-mRNA-splicing factor SYF1tSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Detected in the splicing complex carrying pre-mRNA. {ECO:0000250}.blastocyst development [GO:0001824]; DNA repair [GO:0006281]; mRNA splicing, via spliceosome [GO:0000398]; nucleotide-excision repair [GO:0006289]; transcription, DNA-templated [GO:0006351]; transcription-coupled nucleotide-excision repair [GO:0006283]FUNCTION: Involved in transcription-coupled repair (TCR), transcription and pre-mRNA splicing. {ECO:0000269|PubMed:10944529, ECO:0000269|PubMed:17981804}.Q9UL46PSME2&Proteasome activator complex subunit 2cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; proteasome activator complex [GO:0008537]; proteasome complex [GO:0000502]FUNCTION: Implicated in immun< oproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.P60981DESTDestrinactin filament depolymerization [GO:0030042]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; positive regulation of actin filament depolymerization [GO:0030836]mactin cytoskeleton [GO:0015629]; cortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.Q56VL3OCAD2 OCIA domain-containing protein 2-SUBCELLULAR LOCATION: Endosome {ECO:0000305}.@endosome [GO:0005768]; mitochondrial inner membrane [GO:0005743]P13984T2FB*General transcription factor IIF subunit 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454543}.7-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription initiation from RNA polymerase II promoter [GO:0060261]; positive regulation of viral transcription [GO:0050434]; RNA splicing [GO:0008380]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]ATP binding [GO:0005524]; core RNA polymerase II binding transcription factor activity [GO:0000991]; DNA binding [GO:0003677]; helicase activity [GO:0004386]holo TFIIH complex [GO:0005675]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor TFIIF complex [GO:0005674]'FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity. {ECO:0000269|PubMed:2477704}.Q8IWW6RHG12 Rho GTPase-activating protein 12morphogenesis of an epithelial sheet [GO:0002011]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]uFUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. {ECO:0000250}.O00443P3C2ALPhosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alphaSUBCELLULAR LOCATION: Cell membrane. Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus. Cytoplasm. Note=According to PubMed:10766823 and PubMed:11239472, it is found in the cell membrane, the Golgi apparatus and in clathrin-coated vesicles. According to PubMed:17038310 it inserts preferentially into membranes containing PtdIns(4,5)P2. According to PubMed:11606566, it is nuclear and cytoplasmic. Associated with RNA-containing structures. According to PubMed:14563213, it is mainly cytoplasmic.adaptive immune response [GO:0002250]; cell chemotaxis [GO:0060326]; clathrin coat assembly [GO:0048268]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; exocytosis [GO:0006887]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; negative regulation of zinc ion transmembrane transport [GO:0071583]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; platelet activation [GO:0030168]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; protein phosphorylation [GO:0006468]; small molecule metabolic process [GO:0044281]; vascular smooth muscle contraction [GO:0014829]1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol 3-kinase activity [GO:0035004]; phosphatidylinositol binding [GO:0035091])clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]; vesicle [GO:0031982]FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:12719431, ECO:0000269|PubMed:16215232, ECO:0000269|PubMed:21081650, ECO:0000269|PubMed:9337861}.P13804ETFA;Electron transfer flavoprotein subunit alpha, mitochondrialcellular metabolic process [GO:0044237]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]; respiratory electron transport chain [GO:0022904]; small molecule metabolic process [GO:0044281]7acyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]Q6P4E1CASC4 Protein CASC4IGolgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]Q5T447HECD3"E3 ubiquitin-protein ligase HECTD3proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]Qligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity). {ECO:0000250}.O00231PSD11/26S proteasome non-ATPase regulatory subunit 11anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presenta< tion of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome assembly [GO:0043248]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stem cell differentiation [GO:0048863]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269|PubMed:22972301}.Q9H910HN1L7Hematological and neurological expressed 1-like proteinJcytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q9NQS1AVENCell death regulator AvenuSUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Associated with intracellular membranes.Uapoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]Sendomembrane system [GO:0012505]; intracellular [GO:0005622]; membrane [GO:0016020]8FUNCTION: Protects against apoptosis mediated by Apaf-1.O43670ZN207:BUB3-interacting and GLEBS motif-containing protein ZNF207SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding.Oattachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint [GO:0007094]; protein stabilization [GO:0050821]; regulation of chromosome segregation [GO:0051983]; regulation of transcription, DNA-templated [GO:0006355]DNA binding [GO:0003677]; heparin binding [GO:0008201]; microtubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]condensed chromosome kinetochore [GO:0000777]; kinetochore [GO:0000776]; microtubule [GO:0005874]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Kinetochore-binding protein involved in spindle-assembly checkpoint signaling by regulating mitotic chromosome alignment and mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187). {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}.Q9NTJ4MA2C1Alpha-mannosidase 2C1Lmannose metabolic process [GO:0006013]; protein deglycosylation [GO:0006517]ialpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; zinc ion binding [GO:0008270]vacuole [GO:0005773]Q15366PCBP2Poly(rC)-binding protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19029303}. Cytoplasm {ECO:0000269|PubMed:19029303}. Note=Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.defense response to virus [GO:0051607]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mRNA metabolic process [GO:0016071]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of defense response to virus [GO:0050687]; negative regulation of type I interferon production [GO:0032480]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; RNA splicing [GO:0008380]DNA binding [GO:0003677]; enzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and degradation. {ECO:0000269|PubMed:19881509}.Q676U5A16L1Autophagy-related protein 16-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to omegasomes membranes by WIPI2. Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5. Localizes also to discrete punctae along the ciliary axoneme. {ECO:0000250|UniProtKB:Q8C0J2}.autophagosome assembly [GO:0000045]; negative stranded viral RNA replication [GO:0039689]; protein homooligomerization [GO:0051260]; protein transport [GO:0015031]autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane. {ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904}.Q9Y2G5OFUT2)GDP-fucose protein O-fucosyltransferase 2SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:15233996}. Golgi apparatus {ECO:0000269|PubMed:15233996}. Note=Mainly located in the endoplasmic reticulum.cellular protein metabolic process [GO:0044267]; fucose metabolic process [GO:0006004]; mesoderm formation [GO:0001707]; post-translational protein modification [GO:0043687]; protein O-linked fucosylation [GO:0036066]; protein O-linked glycosylation [GO:0006493]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gene expression [GO:0010468]; regulation of secretion [GO:0051046]2peptide-O-fucosyltransferase activity [GO:0046922]Iendoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]]FUNCTION: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin famili< es. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity). Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13. {ECO:0000250, ECO:0000269|PubMed:11067851, ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:17395588, ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:22588082}.O75382TRIM3%Tripartite motif-containing protein 3\SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000269|PubMed:15772161}.Gnervous system development [GO:0007399]; protein transport [GO:0015031]vprotein C-terminus binding [GO:0008022]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]3cytoplasm [GO:0005737]; early endosome [GO:0005769]FUNCTION: Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation.Q9H330TM245Transmembrane protein 245Q92925SMRD2]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2ATP-dependent chromatin remodeling [GO:0043044]; chromatin remodeling [GO:0006338]; nucleosome disassembly [GO:0006337]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]pnuclear chromatin [GO:0000790]; nucleus [GO:0005634]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology).Q96SN8CK5P2,CDK5 regulatory subunit-associated protein 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Golgi apparatus. Cytoplasm. Note=Found in the pericentriolar region adhering to the surface of the centrosome and in the region of the centrosomal appendages. Localizes to microtubule plus ends.brain development [GO:0007420]; centrosome organization [GO:0051297]; chromosome segregation [GO:0007059]; establishment of mitotic spindle orientation [GO:0000132]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; negative regulation of centriole replication [GO:0046600]; negative regulation of neuron differentiation [GO:0045665]; neurogenesis [GO:0022008]; organelle organization [GO:0006996]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of neuron differentiation [GO:0045664]; regulation of spindle checkpoint [GO:0090231]calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; transcription regulatory region DNA binding [GO:0044212]; tubulin binding [GO:0015631]Gcell junction [GO:0030054]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; pericentriolar material [GO:0000242]; perinuclear region of cytoplasm [GO:0048471]; spindle pole [GO:0000922]{FUNCTION: Potential regulator of CDK5 activity via its interaction with CDK5R1. Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation (By similarity). Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Together with MAPRE1, it may promote microtubule polymerization, bundle formation, growth and dynamics at the plus ends. {ECO:0000250, ECO:0000269|PubMed:17959831, ECO:0000269|PubMed:18042621, ECO:0000269|PubMed:19282672, ECO:0000269|PubMed:19553473}.Q9BWH2FUND2!FUN14 domain-containing protein 2&mitochondrion degradation [GO:0000422]qintegral component of mitochondrial outer membrane [GO:0031307]; mitochondrion [GO:0005739]; nucleus [GO:0005634]Q8IWA4MFN1 Mitofusin-1SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305|PubMed:11751411, ECO:0000305|PubMed:12759376}; Multi-pass membrane protein {ECO:0000305|PubMed:11751411, ECO:0000305|PubMed:12759376}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.!mitochondrial fusion [GO:0008053]rintegral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN1 acts independently of the cytoskeleton. Overexpression induces the formation of mitochondrial networks. {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:12475957, ECO:0000269|PubMed:12759376, ECO:0000269|PubMed:23921378}.Q7L8L6FAKD5'FAST kinase domain-containing protein 5!cellular respiration [GO:0045333]Fpoly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]Q6PK18OGFD3G2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]fextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]Q9NV35NUD15(Probable 8-oxo-dGTP diphosphatase NUDT15dGTP catabolic process [GO:0006203]; nucleobase-containing small molecule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; small molecule metabolic process [GO:0044281]8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; metal ion binding [GO:0046872]HFUNCTION: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. Its substrate specificity in vivo however remains unclear (By similarity). May have a role in DNA synthesis and cell cycle progression through the interaction with PCNA. {ECO:0000250, ECO:0000269|PubMed:19419956, ECO:0000269|PubMed:22556419}.Q8N474SFRP1#Secreted frizzled-related protein 1 InhibitorsSUBCELLULAR LOCATION: Secreted. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding.bone trabecula formation [GO:0060346]; canonical Wnt signaling pathway [GO:0060070]; cellular response to BMP stimulus [GO:0071773]; cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heparin [GO:0071504]; cellular response to hypoxia [GO:0071456]; cellular response to interleukin-1 [GO:0071347]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to starvation [GO:0009267]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin D [GO:0071305]; cellular response to X-ray [GO:0071481]; convergent extension involved in somitogenesis [GO:0090246]; digestive tract morphogenesis [GO:0048546]; dorsal/ventral axis specification [GO:0009950]; female gonad development [GO:0008585]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell differentiation [GO:0060218]; male gonad development [GO:0008584]; menstrual cycle phase [GO:0022601]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regu< lation of apoptotic process [GO:0043066]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of bone remodeling [GO:0046851]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation [GO:2000080]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of fibroblast apoptotic process [GO:2000270]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of gene expression [GO:0010629]; negative regulation of insulin secretion [GO:0046676]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of planar cell polarity pathway involved in axis elongation [GO:2000041]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of Wnt signaling pathway [GO:0030178]; negative regulation of Wnt signaling pathway involved in dorsal/ventral axis specification [GO:2000054]; neural crest cell fate commitment [GO:0014034]; non-canonical Wnt signaling pathway [GO:0035567]; osteoblast differentiation [GO:0001649]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cell proliferation [GO:0008284]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of non-canonical Wnt signaling pathway [GO:2000052]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of Wnt signaling pathway [GO:0030177]; prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis [GO:0060527]; proteolysis [GO:0006508]; regulation of angiogenesis [GO:0045765]; regulation of branching involved in prostate gland morphogenesis [GO:0060687]; regulation of cell cycle process [GO:0010564]; response to drug [GO:0042493]; response to organic cyclic compound [GO:0014070]; somatic stem cell maintenance [GO:0035019]; stromal-epithelial cell signaling involved in prostate gland development [GO:0044345]; ureteric bud development [GO:0001657]; Wnt signaling pathway involved in somitogenesis [GO:0090244]cysteine-type endopeptidase activity [GO:0004197]; drug binding [GO:0008144]; frizzled binding [GO:0005109]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; Wnt-protein binding [GO:0017147]&cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular [GO:0005622]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription. {ECO:0000250}.Q9NRL3STRN4 Striatin-4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=CTTNBP2-binding may regulate dendritic spine distribution. {ECO:0000250}.armadillo repeat domain binding [GO:0070016]; calmodulin binding [GO:0005516]; protein complex binding [GO:0032403]; protein phosphatase 2A binding [GO:0051721]icytoplasm [GO:0005737]; dendritic spine [GO:0043197]; membrane [GO:0016020]; protein complex [GO:0043234]kFUNCTION: Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.Q9UHR5S30BPSAP30-binding protein<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15496587}.Iapoptotic process [GO:0006915]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of cell death [GO:0010942]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]_intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Induces cell death. May act as a transcriptional corepressor of a gene related to cell survival. May be involved in the regulation of beta-2-microglobulin genes. {ECO:0000250|UniProtKB:Q02614, ECO:0000269|PubMed:15496587}.O95817BAG3*BAG family molecular chaperone regulator 36brain development [GO:0007420]; cellular response to heat [GO:0034605]; cellular response to mechanical stimulus [GO:0071260]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; negative regulation of apoptotic process [GO:0043066]; negative regulation of striated muscle cell apoptotic process [GO:0010664]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; regulation of cellular response to heat [GO:1900034]; spinal cord development [GO:0021510]cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; Z disc [GO:0030018]uFUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.Q5TBA9FRYProtein furry homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22753416}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22753416}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22753416}. Note=Distributed diffusely throughout the cytoplasm in interphase. Localizes to the separating centrosomes in prophase, to the spindle poles and spindle microtubules in prometaphase to metaphase, to spindle microtubules in anaphase and to the distal sections of the midbody in cytokinesis. Colocalizes with PLK1 to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle.wactin filament reorganization [GO:0090527]; cell morphogenesis [GO:0000902]; neuron projection development [GO:0031175]cell cortex [GO:0005938]; microtubule organizing center [GO:0005815]; site of polarized growth [GO:0030427]; spindle pole [GO:0000922]cFUNCTION: Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-< mediated PLK1 phosphorylation. {ECO:0000269|PubMed:22753416}.Q9BZC7ABCA2*ATP-binding cassette sub-family A member 2#SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:11309290}; Multi-pass membrane protein {ECO:0000269|PubMed:11309290}. Lysosome membrane {ECO:0000269|PubMed:11309290}; Multi-pass membrane protein {ECO:0000269|PubMed:11309290}. Note=Forms discrete, punctate intracellular vesicles.ycholesterol homeostasis [GO:0042632]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; regulation of intracellular cholesterol transport [GO:0032383]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to drug [GO:0042493]; response to steroid hormone [GO:0048545]; transmembrane transport [GO:0055085]; transport [GO:0006810]ATPase activity [GO:0016887]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; nucleotide binding [GO:0000166]MATP-binding cassette (ABC) transporter complex [GO:0043190]; cytoplasmic membrane-bounded vesicle [GO:0016023]; endosome [GO:0005768]; endosome membrane [GO:0010008]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]FUNCTION: Probable transporter, its natural substrate has not been found yet. May have a role in macrophage lipid metabolism and neural development.O14879IFIT3;Interferon-induced protein with tetratricopeptide repeats 3/SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.Mcellular response to interferon-alpha [GO:0035457]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; response to virus [GO:0009615]; type I interferon signaling pathway [GO:0060337]5FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exihibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2. {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20686046, ECO:0000269|PubMed:21190939, ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21813773}.Q16134ETFDGElectron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial cellular metabolic process [GO:0044237]; electron transport chain [GO:0022900]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; respiratory electron transport chain [GO:0022904]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; electron carrier activity [GO:0009055]; electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, oxidizing metal ions with flavin as acceptor [GO:0043783]; quinone binding [GO:0048038]; ubiquinone binding [GO:0048039]integral component of mitochondrial inner membrane [GO:0031305]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]<FUNCTION: Accepts electrons from ETF and reduces ubiquinone.P10768ESTDS-formylglutathione hydrolase5SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.+formaldehyde catabolic process [GO:0046294]carboxylic ester hydrolase activity [GO:0052689]; hydrolase activity, acting on ester bonds [GO:0016788]; methylumbelliferyl-acetate deacetylase activity [GO:0047374]; S-formylglutathione hydrolase activity [GO:0018738]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}.P30533AMRP1Alpha-2-macroglobulin receptor-associated proteinSUBCELLULAR LOCATION: Endoplasmic reticulum. Cytoplasm. Cell surface. Note=Intracellular and associated with cell surface receptors. Found in the endoplasmic reticulum.~extracellular negative regulation of signal transduction [GO:1900116]; negative regulation of beta-amyloid clearance [GO:1900222]; negative regulation of protein binding [GO:0032091]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; protein folding [GO:0006457]; receptor-mediated endocytosis [GO:0006898]; vesicle-mediated transport [GO:0016192]&asialoglycoprotein receptor activity [GO:0004873]; heparin binding [GO:0008201]; low-density lipoprotein particle receptor binding [GO:0050750]; receptor antagonist activity [GO:0048019]; unfolded protein binding [GO:0051082]; very-low-density lipoprotein particle receptor binding [GO:0070326]cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; rough endoplasmic reticulum lumen [GO:0048237]; vesicle [GO:0031982]RFUNCTION: Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.Q9UNW1MINP1-Multiple inositol polyphosphate phosphatase 1bone mineralization [GO:0030282]; dephosphorylation [GO:0016311]; inositol phosphate metabolic process [GO:0043647]; ossification [GO:0001503]; polyphosphate metabolic process [GO:0006797]; small molecule metabolic process [GO:0044281]acid phosphatase activity [GO:0003993]; bisphosphoglycerate 3-phosphatase activity [GO:0034417]; inositol hexakisphosphate 2-phosphatase activity [GO:0052826]; phosphohistidine phosphatase activity [GO:0008969]pendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]FUNCTION: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). {ECO:0000269|PubMed:18413611}.P62487RPB7+DNA-directed RNA polymerase II subunit RPB77-methylguanosine mRNA capping [GO:0006370]; apoptotic process [GO:0006915]; DNA repair [GO:0006281]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, exonucleolytic [GO:0000291]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; positive regulation of translational initiation [GO:0045948]; positive regulation of viral transcription [GO:0050434]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]DNA-directed RNA polymerase activity [GO:0003899]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; translation initiation factor binding [GO:0031369]< cytoplasmic mRNA processing body [GO:0000932]; DNA-directed RNA polymerase II, core complex [GO:0005665]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634](FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). Binds RNA. {ECO:0000250, ECO:0000269|PubMed:9852112}.Q93034CUL5Cullin-5`calcium ion transmembrane transport [GO:0070588]; cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; cerebral cortex radially oriented cell migration [GO:0021799]; cytosolic calcium ion homeostasis [GO:0051480]; G1/S transition of mitotic cell cycle [GO:0000082]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of cell proliferation [GO:0008285]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; radial glia guided migration of Purkinje cell [GO:0021942]; response to osmotic stress [GO:0006970]; viral process [GO:0016032]tcalcium channel activity [GO:0005262]; receptor activity [GO:0004872]; ubiquitin protein ligase binding [GO:0031625]yCul5-RING ubiquitin ligase complex [GO:0031466]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. Seems to be involved in proteosomal degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a cell surface vasopressin receptor.Q14185DOCK1"Dedicator of cytokinesis protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}. Note=Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000305}.apoptotic process [GO:0006915]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; hematopoietic progenitor cell differentiation [GO:0002244]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; phagocytosis, engulfment [GO:0006911]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]_GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]scytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]?FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1. {ECO:0000269|PubMed:8657152}.Q96HY6DDRGK!DDRGK domain-containing protein 1JSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:20018847}.positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of proteasomal protein catabolic process [GO:1901800]; protein K69-linked ufmylation [GO:1990592]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; response to endoplasmic reticulum stress [GO:0034976]2ubiquitin-like protein ligase binding [GO:0044389]Oendoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]TFUNCTION: Protein which interacts with the E3 UFM1-protein ligase UFL1 and one of its substrates TRIP4 and is required for TRIP4 ufmylation. Through TRIP4 ufmylation may regulate nuclear receptors-mediated transcription (PubMed:25219498). May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIB, the inhibitor of NF-kappa-B (PubMed:23675531). May also play a role in the cellular response to endoplasmic reticulum stress (By similarity). {ECO:0000250|UniProtKB:Q80WW9, ECO:0000269|PubMed:23675531, ECO:0000269|PubMed:25219498}.Q00765REEP5'Receptor expression-enhancing protein 5PFUNCTION: May promote functional cell surface expression of olfactory receptors.P62072TIM10=Mitochondrial import inner membrane translocase subunit Tim10chaperone binding [GO:0051087]; protein homodimerization activity [GO:0042803]; protein transporter activity [GO:0008565]; transporter activity [GO:0005215]; zinc ion binding [GO:0008270] mitochondrial inner membrane [GO:0005743]; mitochondrial inner membrane presequence translocase complex [GO:0005744]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]Q6FI81CPIN1 AnamorsinSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Mitochondrion intermembrane space {ECO:0000305}. Note=Imported into mitochondria (in vitro).apoptotic process [GO:0006915]; hemopoiesis [GO:0030097]; iron-sulfur cluster assembly [GO:0016226]; negative regulation of apoptotic process [GO:0043066]; small molecule metabolic process [GO:0044281]u2 iron, 2 sulfur cluster binding [GO:0051537]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]xcytoplasm [GO:0005737]; mitochondrial intermembrane space [GO:0005758]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]6FUNCTION: Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity). Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Electrons are transferred to the Fe-S cluster from NADPH via the FAD- and FMN-containing protein NDOR1. {ECO:0000250, ECO:0000269|PubMed:23596212}.P51153RAB13Ras-related protein Rab-13 SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell junction, tight junction. Golgi apparatus, trans-Golgi network membrane. Recycling endosome membrane. Cell projection, lamellipodium {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}. Note=Tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. Relocalizes to the leading edge of lamellipodia in migrating endothelial cells.bicellular tight junction assembly [GO:0070830]; cellular response to insulin stimulus [GO:0032869]; cortical actin cytoskeleton organization [GO:0030866]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; endothelial cell chemotaxis [GO:0035767]; establishment of protein localization to plasma membrane [GO:0090002]; establishment of Sertoli cell barrier [GO:0097368]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; neuron projection development [GO:0031175]; protein kinas< e A signaling [GO:0010737]; protein localization to cell leading edge [GO:1902463]; Rab protein signal transduction [GO:0032482]; trans-Golgi network to recycling endosome transport [GO:0044795]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; insulin-responsive compartment [GO:0032593]; lamellipodium [GO:0030027]; lateral plasma membrane [GO:0016328]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; transport vesicle membrane [GO:0030658]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis. {ECO:0000269|PubMed:12058051, ECO:0000269|PubMed:15096524, ECO:0000269|PubMed:15528189, ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:18779367, ECO:0000269|PubMed:20008558}.P41567EIF1*Eukaryotic translation initiation factor 1dosage compensation by inactivation of X chromosome [GO:0009048]; regulation of translational initiation [GO:0006446]; response to stress [GO:0006950]FUNCTION: Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA.Q9BVK8TM147Transmembrane protein 147SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20538592}; Multi-pass membrane protein {ECO:0000269|PubMed:20538592}.$protein destabilization [GO:0031648]Q99720SGMR1)Sigma non-opioid intracellular receptor 1SUBCELLULAR LOCATION: Nucleus inner membrane. Nucleus outer membrane. Endoplasmic reticulum membrane. Lipid droplet. Cell junction. Cell membrane. Cell projection, growth cone. Note=Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum. Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding.zlipid transport [GO:0006869]; nervous system development [GO:0007399]; regulation of neuron apoptotic process [GO:0043523]@drug binding [GO:0008144]; opioid receptor activity [GO:0004985]Hcell junction [GO:0030054]; endoplasmic reticulum membrane [GO:0005789]; growth cone [GO:0030426]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lipid particle [GO:0005811]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]NFUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. {ECO:0000269|PubMed:16472803, ECO:0000269|PubMed:9341151}.O75935DCTN3Dynactin subunit 3\SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9722614}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:9722614}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:9722614}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9722614}. Cleavage furrow {ECO:0000269|PubMed:9722614}. Midbody {ECO:0000269|PubMed:9722614}. Note=Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells.Aantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cytokinesis [GO:0000910]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; organelle organization [GO:0006996]centrosome [GO:0005813]; cleavage furrow [GO:0032154]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]qFUNCTION: Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000269|PubMed:9722614}.Q9UMX3BOK$Bcl-2-related ovarian killer proteinhSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23429263}; Single-pass membrane protein {ECO:0000269|PubMed:23429263}. Golgi apparatus membrane {ECO:0000269|PubMed:23429263}; Single-pass membrane protein {ECO:0000255}. Note=The transmembrane domain is necessary and sufficient for Golgi and ER targeting. {ECO:0000269|PubMed:23429263}.[activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; brain development [GO:0007420]; cell proliferation [GO:0008283]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; male gonad development [GO:0008584]; neuron apoptotic process [GO:0051402]; oligodendrocyte differentiation [GO:0048709]; positive regulation of execution phase of apoptosis [GO:1900119]`protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]`FUNCTION: Induces apoptosis in a manner dependent on BAX and BAK. {ECO:0000269|PubMed:23429263}.P05141ADT2ADP/ATP translocase 2ANTadenine transport [GO:0015853]; chromosome segregation [GO:0007059]; energy reserve metabolic process [GO:0006112]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; positive regulation of cell proliferation [GO:0008284]; regulation of insulin secretion [GO:0050796]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]; viral process [GO:0016032]adenine transmembrane transporter activity [GO:0015207]; poly(A) RNA binding [GO:0044822]; ubiquitin protein ligase binding [GO:0031625]< &extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; MMXD complex [GO:0071817]; myelin sheath [GO:0043209]; nucleus [GO:0005634]FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. {ECO:0000269|PubMed:20797633}.P61026RAB10Ras-related protein Rab-10_SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Endosome membrane. Recycling endosome membrane. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}. Cell projection, cilium. Endoplasmic reticulum membrane. Note=Associates with SLC2A4/GLUT4 storage vesicles. Localizes to the base of the cilium. Transiently associates with phagosomes (By similarity). According to PubMed:23263280 localizes to the endoplasmic reticulum at domains of new tubule growth. {ECO:0000250}.antigen processing and presentation [GO:0019882]; axonogenesis [GO:0007409]; basolateral protein localization [GO:0061467]; cellular response to antibiotic [GO:0071236]; cellular response to insulin stimulus [GO:0032869]; endoplasmic reticulum tubular network organization [GO:0071786]; endosomal transport [GO:0016197]; establishment of neuroblast polarity [GO:0045200]; establishment of protein localization to endoplasmic reticulum membrane [GO:0097051]; establishment of protein localization to membrane [GO:0090150]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi to plasma membrane transport [GO:0006893]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; polarized epithelial cell differentiation [GO:0030859]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0017157]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192]/cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum tubular network [GO:0071782]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; insulin-responsive compartment [GO:0032593]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle membrane [GO:0030670]; primary cilium [GO:0072372]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. According to PubMed:23263280, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. {ECO:0000250, ECO:0000269|PubMed:16641372, ECO:0000269|PubMed:21248164, ECO:0000269|PubMed:23263280}.Q9Y305ACOT9-Acyl-coenzyme A thioesterase 9, mitochondrial'acyl-CoA metabolic process [GO:0006637]\acetyl-CoA hydrolase activity [GO:0003986]; carboxylic ester hydrolase activity [GO:0052689]FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.Q9H4A3WNK1$Serine/threonine-protein kinase WNK1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660600}.)intracellular signal transduction [GO:0035556]; ion transport [GO:0006811]; negative regulation of phosphatase activity [GO:0010923]; neuron development [GO:0048666]; peptidyl-threonine phosphorylation [GO:0018107]; protein phosphorylation [GO:0006468]; regulation of cellular process [GO:0050794]ATP binding [GO:0005524]; chloride channel inhibitor activity [GO:0019869]; phosphatase binding [GO:0019902]; protein kinase inhibitor activity [GO:0004860]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival, and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D and SGK1. Controls sodium and chloride ion transport by inhibiting the activity of WNK4, by either phosphorylating the kinase or via an interaction between WNK4 and the autoinhibitory domain of WNK1. WNK4 regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1 may also play a role in actin cytoskeletal reorganization. Phosphorylates NEDD4L. Acts as a scaffold to inhibit SLC4A4, SLC26A6 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition (By similarity). {ECO:0000250|UniProtKB:P83741, ECO:0000250|UniProtKB:Q9JIH7, ECO:0000269|PubMed:10660600, ECO:0000269|PubMed:15060842}.Q8TDH9BL1S5=Biogenesis of lysosome-related organelles complex 1 subunit 5lanterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; endosome to melanosome transport [GO:0035646]; melanosome organization [GO:0032438]; melanosome transport [GO:0032402]; neuron projection development [GO:0031175]; otolith morphogenesis [GO:0032474]; positive regulation of pigment cell differentiation [GO:0050942];BLOC-1 complex [GO:0031083]; transport vesicle [GO:0030133],FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:17182842}.Q8IY17PLPL6Neuropathy target esteraseQSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15044461}; Single-pass type I membrane protein {ECO:0000269|PubMed:15044461}; Cytoplasmic side {ECO:0000269|PubMed:15044461}. Note=Anchored to the cytoplasmic face of the endoplasmic reticulum by its N-terminal transmembrane segment. {ECO:0000269|PubMed:15044461}.angiogenesis [GO:0001525]; developmental process [GO:0032502]; lipid catabolic process [GO:0016042]; organ morphogenesis [GO:0009887]; phosphatidylcholine metabolic process [GO:0046470]kFUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 position< s of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. {ECO:0000269|PubMed:15044461, ECO:0000269|PubMed:1666291}.O00499BIN1'Myc box-dependent-interacting protein 1[SUBCELLULAR LOCATION: Isoform BIN1: Nucleus.; SUBCELLULAR LOCATION: Isoform IIA: Cytoplasm.cell proliferation [GO:0008283]; endocytosis [GO:0006897]; lipid tube assembly [GO:0060988]; muscle cell differentiation [GO:0042692]; positive regulation of apoptotic process [GO:0043065]; positive regulation of astrocyte differentiation [GO:0048711]; regulation of cell cycle arrest [GO:0071156]; regulation of endocytosis [GO:0030100]; regulation of neuron differentiation [GO:0045664]; viral process [GO:0016032]midentical protein binding [GO:0042802]; RNA polymerase binding [GO:0070063]; tau protein binding [GO:0048156]actin cytoskeleton [GO:0015629]; axon [GO:0030424]; axon initial segment [GO:0043194]; cytoplasm [GO:0005737]; I band [GO:0031674]; lipid tube [GO:0060987]; membrane [GO:0016020]; node of Ranvier [GO:0033268]; nucleus [GO:0005634]; T-tubule [GO:0030315]; Z disc [GO:0030018]FUNCTION: May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation.P84103SRSF3&Serine/arginine-rich splicing factor 3)gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Lcytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]FUNCTION: May be involved in RNA processing in relation with cellular proliferation and/or maturation. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific. {ECO:0000269|PubMed:11336712, ECO:0000269|PubMed:18364396}.P47813IF1AX:Eukaryotic translation initiation factor 1A, X-chromosomalcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; translation [GO:0006412]; translational initiation [GO:0006413]FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.Q9GZS3WDR61WD repeat-containing protein 61eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16024656}. Cytoplasm {ECO:0000305|PubMed:16024656}.:histone H3-K4 trimethylation [GO:0080182]; negative regulation of myeloid cell differentiation [GO:0045638]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of histone H3-K79 methylation [GO:2001162]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]Cdc73/Paf1 complex [GO:0016593]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Ski complex [GO:0055087]; transcriptionally active chromatin [GO:0035327]eFUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C. {ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}.Q9H1I8ASCC22Activating signal cointegrator 1 complex subunit 2DNA dealkylation involved in DNA repair [GO:0006307]; DNA repair [GO:0006281]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351];FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation.P31146COR1A Coronin-1ASUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}. Note=In non-infected macrophages, associated with the cortical microtubule network. In mycobacteria-infected macrophages, becomes progressively relocalized and retained around the mycobacterial phagosomes. Retention on the phagosomal membrane is strictly dependent on mycobacterial viability and not due to impaired acidification (By similarity). {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; calcium ion transport [GO:0006816]; cell-substrate adhesion [GO:0031589]; cellular response to interleukin-4 [GO:0071353]; early endosome to recycling endosome transport [GO:0061502]; homeostasis of number of cells within a tissue [GO:0048873]; innate immune response [GO:0045087]; leukocyte chemotaxis [GO:0030595]; movement of cell or subcellular component [GO:0006928]; natural killer cell degranulation [GO:0043320]; negative regulation of actin nucleation [GO:0051126]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of vesicle fusion [GO:0031339]; nerve growth factor signaling pathway [GO:0038180]; phagocytosis [GO:0006909]; phagolysosome assembly [GO:0001845]; positive chemotaxis [GO:0050918]; positive regulation of cell migration [GO:0030335]; positive regulation of T cell proliferation [GO:0042102]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of actin filament polymerization [GO:0030833]; regulation of cell shape [GO:0008360]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; T cell homeostasis [GO:0043029]; uropod organization [GO:0032796]factin binding [GO:0003779]; actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; cytoskeletal protein binding [GO:0008092]; myosin heavy chain binding [GO:0032036]; phosphatidylinositol 3-kinase binding [GO:0043548]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; lamellipodium [GO:0030027]; membrane [GO:0016020]; phagocytic cup [GO:0001891]; phagocy< tic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. {ECO:0000269|PubMed:10338208}.P07858CATB Cathepsin BSUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted, extracellular space {ECO:0000250}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.autophagy [GO:0006914]; cellular response to mechanical stimulus [GO:0071260]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; epithelial cell differentiation [GO:0030855]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; negative regulation of cell death [GO:0060548]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of apoptotic process [GO:0042981]; regulation of catalytic activity [GO:0050790]; response to amine [GO:0014075]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to interleukin-4 [GO:0070670]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to wounding [GO:0009611]; skeletal muscle tissue development [GO:0007519]; spermatogenesis [GO:0007283]; toll-like receptor signaling pathway [GO:0002224]collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; proteoglycan binding [GO:0043394]apical plasma membrane [GO:0016324]; caveola [GO:0005901]; endolysosome lumen [GO:0036021]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.O43847NRDC Nardilysin(cell migration [GO:0016477]; cell proliferation [GO:0008283]; neuromuscular junction development [GO:0007528]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; protein processing [GO:0016485]; proteolysis [GO:0006508]; regulation of endopeptidase activity [GO:0052548]wepidermal growth factor binding [GO:0048408]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]/cell surface [GO:0009986]; cytosol [GO:0005829]]FUNCTION: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.Q96SN7ORAI2Protein orai-2ORAI[calcium ion transmembrane transport [GO:0070588]; store-operated calcium entry [GO:0002115]4store-operated calcium channel activity [GO:0015279]\growth cone [GO:0030426]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1. {ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:17452328}.Q6P2E9EDC4$Enhancer of mRNA-decapping protein 41SUBCELLULAR LOCATION: Cytoplasm, P-body. Nucleus.cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]BFUNCTION: In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro). {ECO:0000269|PubMed:16364915}.Q6V0I7FAT4Protocadherin Fat 4SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In the kidney, localizes to primary cilia. {ECO:0000250}.branching involved in ureteric bud morphogenesis [GO:0001658]; cerebral cortex development [GO:0021987]; digestive tract development [GO:0048565]; heart morphogenesis [GO:0003007]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; hippo signaling [GO:0035329]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; inner ear receptor stereocilium organization [GO:0060122]; neurogenesis [GO:0022008]; ossification involved in bone maturation [GO:0043931]; plasma membrane organization [GO:0007009]; regulation of metanephric nephron tubule epithelial cell differentiation [GO:0072307]apical part of cell [GO:0045177]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. FAT4 plays a role in the maintenance of planar cell polarity as well as in inhibition of YAP1-mediated neuroprogenitor cell proliferation and differentiation (By similarity). {ECO:0000250}.Q13443ADAM9=Disintegrin and metalloproteinase domain-containing protein 9activation of MAPKK activity [GO:0000186]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:0007160]; cellular response to lipopolysaccharide [GO:0071222]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; keratinocyte differentiation [GO:0030216]; membrane protein ectodomain proteolysis [GO:0006509]; monocyte activation [GO:0042117]; PMA-inducible membrane protein ectodomain proteolysis [GO:0051088]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of keratinocyte migration [GO:0051549]; positive regulation of macrophage fusion [GO:0034241]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of protein secretion [GO:0050714]; response to calcium ion [GO:0051592]; response to glucocorticoid [GO:0051384]; response to hydrogen peroxide [GO:0042542]; response to manganese ion [GO:0010042]; response to tumor necrosis factor [GO:0034612]; transforming growth factor beta receptor signaling pathway [GO:0007179]collagen binding [GO:0005518]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; protein kinase C binding [GO:0005080]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intrinsic component of external side of plasma membrane [GO:0031233]FUNCTION: Probable zinc protease. May mediate cell-cell or cell-matrix interactions. Isoform 2 displays alpha-secretase activity for APP. {ECO:0000269|PubMed:12054541}.P28838AMPLCytosol aminopeptidasesaminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloexopeptidase activity [GO:0008235]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802]FUNCTION: Presumably involved in the processing and regular turnover of intracellular pro< teins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.Q9BPZ3PAIP23Polyadenylate-binding protein-interacting protein 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11172725}.memory [GO:0007613]; negative regulation of translational initiation [GO:0045947]; regulation of long-term synaptic potentiation [GO:1900271]; spermatogenesis [GO:0007283]FmRNA binding [GO:0003729]; translation repressor activity [GO:0030371]FUNCTION: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization. {ECO:0000269|PubMed:11172725}.Q02252MMSADMethylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialbeta-alanine catabolic process [GO:0019484]; branched-chain amino acid catabolic process [GO:0009083]; brown fat cell differentiation [GO:0050873]; cellular nitrogen compound metabolic process [GO:0034641]; small molecule metabolic process [GO:0044281]; thymine catabolic process [GO:0006210]; thymine metabolic process [GO:0019859]; valine catabolic process [GO:0006574]; valine metabolic process [GO:0006573];aldehyde dehydrogenase (NAD) activity [GO:0004029]; fatty-acyl-CoA binding [GO:0000062]; malonate-semialdehyde dehydrogenase (acetylating) activity [GO:0018478]; methylmalonate-semialdehyde dehydrogenase (acylating) activity [GO:0004491]; poly(A) RNA binding [GO:0044822]; thiolester hydrolase activity [GO:0016790]{extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]QFUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.P63208SKP1#S-phase kinase-associated protein 1Aanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; circadian rhythm [GO:0007623]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; histone H2A monoubiquitination [GO:0035518]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; Notch signaling pathway [GO:0007219]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein ubiquitination [GO:0016567]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]Cul7-RING ubiquitin ligase complex [GO:0031467]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; SCF ubiquitin ligase complex [GO:0019005]FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. SCF(FBXO10) direct ubiquitination of BCL2. {ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23431138}.O00391QSOX1Sulfhydryl oxidase 1SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted, extracellular space. Note=Found in the extracellular medium of quiescent cells but is not found in proliferating cells.ucell redox homeostasis [GO:0045454]; negative regulation of macroautophagy [GO:0016242]; protein folding [GO:0006457]iflavin-linked sulfhydryl oxidase activity [GO:0016971]; protein disulfide isomerase activity [GO:0003756]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of Golgi membrane [GO:0030173]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. In fibroblasts, it may have tumor-suppressing capabilities being involved in growth regulation. {ECO:0000269|PubMed:10542195, ECO:0000269|PubMed:10708601, ECO:0000269|PubMed:12176051, ECO:0000269|PubMed:16806532, ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:18393449}.Q8N6T3ARFG13ADP-ribosylation factor GTPase-activating protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}.cellular protein metabolic process [GO:0044267]; COPI coating of Golgi vesicle [GO:0048205]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; membrane organization [GO:0061024]; positive regulation of GTPase activity [GO:0043547]; protein transport [GO:0015031]; regulation of endocytosis [GO:0030100]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]pcytosol [GO:0005829]; Golgi-associated vesicle membrane [GO:0030660]; neuronal postsynaptic density [GO:0097481]FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity). {ECO:0000250}.P20585MSH3 DNA mismatch repair protein Msh3mDNA repair [GO:0006281]; maintenance of DNA repeat elements [GO:0043570]; meiotic mismatch repair [GO:0000710]; mismatch repair [GO:0006298]; negative regulation of DNA recombination [GO:0045910]; positive regulation of helicase activity [GO:0051096]; reciprocal meiotic recombination [GO:0007131]; somatic recombination of immunoglobulin gene segments [GO:0016447]5ATP binding [GO:0005524]; centromeric DNA binding [GO:0019237]; damaged DNA binding [GO:0003684]; DNA-dependent ATPase activity [GO:0008094]; double-strand/single-strand DNA junction binding [GO:0000406]; enzyme binding [GO:0019899]; heteroduplex DNA loop binding [GO:0000404]; Y-form< DNA binding [GO:0000403]membrane [GO:0016020]; MutSbeta complex [GO:0032302]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]GFUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis.Q9Y519T184BTransmembrane protein 184BWFUNCTION: May activate the MAP kinase signaling pathway. {ECO:0000269|PubMed:12761501}.Q9BVG3TRI62"E3 ubiquitin-protein ligase TRIM62>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23402750}.ycytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of viral transcription [GO:0032897]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; regulation of viral entry into host cell [GO:0046596]; regulation of viral release from host cell [GO:1902186]FUNCTION: E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2. {ECO:0000269|PubMed:23402750}.Q96CT7CC124)Coiled-coil domain-containing protein 124'SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23894443}. Midbody {ECO:0000269|PubMed:23894443}. Note=Colocalizes with gamma-tubulin at interphase, prophase, metaphase, and anaphase. Relocates from centrosome to midbody at telophase.3cell cycle [GO:0007049]; cell division [GO:0051301]vcytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; plasma membrane [GO:0005886]dFUNCTION: Required for proper progression of late cytokinetic stages. {ECO:0000269|PubMed:23894443}.P36915GNL1)Guanine nucleotide-binding protein-like 1cellular response to DNA damage stimulus [GO:0006974]; ribosome biogenesis [GO:0042254]; signal transduction [GO:0007165]; T cell mediated immunity [GO:0002456]aGTPase activity [GO:0003924]; GTP binding [GO:0005525]; structural molecule activity [GO:0005198]6extracellular space [GO:0005615]; nucleus [GO:0005634]UFUNCTION: Possible regulatory or functional link with the histocompatibility cluster.P83916CBX1Chromobox protein homolog 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410, ECO:0000269|PubMed:9169582}. Note=Unassociated with chromosomes during mitosis.@negative regulation of transcription, DNA-templated [GO:0045892]kchromatin binding [GO:0003682]; enzyme binding [GO:0019899]; histone methyltransferase binding [GO:1990226]chromatin [GO:0000785]; chromocenter [GO:0010369]; chromosome, centromeric region [GO:0000775]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nuclear heterochromatin [GO:0005720]; nucleoplasm [GO:0005654]; pericentric heterochromatin [GO:0005721]; spindle [GO:0005819]FUNCTION: Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.P15151PVRPoliovirus receptorSUBCELLULAR LOCATION: Isoform Alpha: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Delta: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform Beta: Secreted.; SUBCELLULAR LOCATION: Isoform Gamma: Secreted.adherens junction organization [GO:0034332]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell recognition [GO:0008037]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002860]; regulation of immune response [GO:0050776]; susceptibility to natural killer cell mediated cytotoxicity [GO:0042271]; susceptibility to T cell mediated cytotoxicity [GO:0060370]; viral process [GO:0016032]cell adhesion molecule binding [GO:0050839]; protein homodimerization activity [GO:0042803]; receptor activity [GO:0004872]; receptor binding [GO:0005102]=cell-cell adherens junction [GO:0005913]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]YFUNCTION: Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. Serves as a receptor for poliovirus attachment to target cells. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport. {ECO:0000269|PubMed:15471548, ECO:0000269|PubMed:15607800}.Q9NUQ6SPS2LSPATS2-like protein(SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005571}. Nucleus, nucleolus {ECO:0000269|PubMed:19005571}. Note=During oxidative stress as well as UV irradiation, energy deprivation or heat shock, relocalizes to cytoplasmic stress granules. In the nucleus, found in structures lacking NPM1.bcytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein complex [GO:0043234]Q9BSF4CS052 Uncharacterized protein C19orf52P49590SYHM.Probable histidine--tRNA ligase, mitochondrialgene expression [GO:0010467]; histidyl-tRNA aminoacylation [GO:0006427]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]A2RUS2DEND3 DENN domain-containing protein 3cellular protein catabolic process [GO:0044257]; endosome to lysosome transport [GO:0008333]; positive regulation of GTPase activity [GO:0043547]gFUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB12 into its active GTP-bound form. Thereby, may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. {ECO:0000269|PubMed:20937701}.P54619AAKG1/5'-AMP-activated protein kinase subunit gamma-1Longevity regulationAMPK[cell cycle arrest [GO:0007050]; fatty acid biosynthetic process [GO:0006633]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; membrane organization [GO:0061024]; mitochondrion organization [GO:0007005]; organelle organization [GO:00< 06996]; positive regulation of gene expression [GO:0010628]; positive regulation of protein kinase activity [GO:0045860]; protein phosphorylation [GO:0006468]; regulation of glycolytic process [GO:0006110]; signal transduction [GO:0007165]; spermatogenesis [GO:0007283]; transcription initiation from RNA polymerase II promoter [GO:0006367] ADP binding [GO:0043531]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]AMP-activated protein kinase complex [GO:0031588]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. {ECO:0000269|PubMed:21680840}.P55072TERA)Transitional endoplasmic reticulum ATPaseSUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus. Note=Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parkinson disease patients. Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; aggresome assembly [GO:0070842]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to heat [GO:0034605]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated misfolded protein catabolic process [GO:0071712]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; error-free translesion synthesis [GO:0070987]; ER to Golgi vesicle-mediated transport [GO:0006888]; establishment of protein localization [GO:0045184]; flavin adenine dinucleotide catabolic process [GO:0072389]; NADH metabolic process [GO:0006734]; positive regulation of ATP biosynthetic process [GO:2001171]; positive regulation of Lys63-specific deubiquitinase activity [GO:1903007]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of oxidative phosphorylation [GO:1903862]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein complex assembly [GO:0031334]; positive regulation of protein K63-linked deubiquitination [GO:1903006]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein hexamerization [GO:0034214]; protein homooligomerization [GO:0051260]; protein N-linked glycosylation via asparagine [GO:0018279]; protein ubiquitination [GO:0016567]; regulation of aerobic respiration [GO:1903715]; regulation of apoptotic process [GO:0042981]; retrograde protein transport, ER to cytosol [GO:0030970]; translesion synthesis [GO:0019985]; viral genome replication [GO:0019079]ADP binding [GO:0043531]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; BAT3 complex binding [GO:1904288]; deubiquitinase activator activity [GO:0035800]; lipid binding [GO:0008289]; poly(A) RNA binding [GO:0044822]; polyubiquitin binding [GO:0031593]; protein domain specific binding [GO:0019904]; protein phosphatase binding [GO:0019903]; ubiquitin-like protein ligase binding [GO:0044389]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease binding [GO:1990381]7cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Hrd1p ubiquitin ligase complex [GO:0000836]; intracellular membrane-bounded organelle [GO:0043231]; lipid particle [GO:0005811]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; proteasome complex [GO:0000502]; site of double-strand break [GO:0035861]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]; VCP-NSFL1C complex [GO:1990730]SFUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. {ECO:0000250|UniProtKB:P46462, ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:21118995, ECO:0000269|PubMed:22020440, ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607}.O14656TOR1A Torsin-1AxSUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane; Peripheral membrane protein. Cell projection, growth cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cytoplasm, cytoskeleton. Note=Upon oxidative stress, redistributes to protusions from the cell surface (By similarity). Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. {ECO:0000250}.cell adhesion [GO:0007155]; chaperone-mediated protein folding [GO:0061077]; chaperone mediated protein folding requiring cofactor [GO:0051085]; chaperone-mediated protein transport [GO:0072321]; ER-associated misfolded protein catabolic process [GO:0071712]; intermediate filament cytoskelet< on organization [GO:0045104]; neuron projection development [GO:0031175]; nuclear envelope organization [GO:0006998]; nuclear membrane organization [GO:0071763]; organelle organization [GO:0006996]; positive regulation of synaptic vesicle endocytosis [GO:1900244]; protein deneddylation [GO:0000338]; protein homooligomerization [GO:0051260]; protein localization to nucleus [GO:0034504]; regulation of dopamine uptake involved in synaptic transmission [GO:0051584]; regulation of protein localization to cell surface [GO:2000008]; response to oxidative stress [GO:0006979]; synaptic vesicle transport [GO:0048489]; wound healing, spreading of cells [GO:0044319]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; cytoskeletal protein binding [GO:0008092]; kinesin binding [GO:0019894]; unfolded protein binding [GO:0051082]cell junction [GO:0030054]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extrinsic component of endoplasmic reticulum membrane [GO:0042406]; growth cone [GO:0030426]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; secretory granule [GO:0030141]; synaptic vesicle [GO:0008021]; transport vesicle [GO:0030133]FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues. {ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:23569223}.Q01850CDR2)Cerebellar degeneration-related protein 2O14737PDCD5Programmed cell death protein 5PDCDs/PD-L1/2(11)Ccellular response to transforming growth factor beta stimulus [GO:0071560]; negative regulation of cell proliferation [GO:0008285]; negative regulation of chaperone-mediated protein folding [GO:1903645]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of gene expression [GO:0010628]; positive regulation of protein import into mitochondrial outer membrane [GO:1903638]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]acetyltransferase activator activity [GO:0010698]; beta-tubulin binding [GO:0048487]; DNA binding [GO:0003677]; heparin binding [GO:0008201]3FUNCTION: May function in the process of apoptosis.O14684PTGESProstaglandin E synthasexSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18682561}; Multi-pass membrane protein {ECO:0000269|PubMed:18682561}.bacute inflammatory response [GO:0002526]; arachidonic acid metabolic process [GO:0019369]; chronic inflammatory response [GO:0002544]; cyclooxygenase pathway [GO:0019371]; negative regulation of cell proliferation [GO:0008285]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]; response to calcium ion [GO:0051592]; response to cytokine [GO:0034097]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to retinoic acid [GO:0032526]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]Pglutathione binding [GO:0043295]; prostaglandin-E synthase activity [GO:0050220]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). {ECO:0000269|PubMed:18682561}.O75787RENRRenin receptor{angiotensin maturation [GO:0002003]; cellular protein metabolic process [GO:0044267]; eye pigmentation [GO:0048069]; head morphogenesis [GO:0060323]; positive regulation of transforming growth factor beta1 production [GO:0032914]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of MAPK cascade [GO:0043408]; rostrocaudal neural tube patterning [GO:0021903]Qaspartic-type endopeptidase activity [GO:0004190]; receptor activity [GO:0004872]cell body [GO:0044297]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]LFUNCTION: Functions as a renin and prorenin cellular receptor. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS). {ECO:0000269|PubMed:12045255}.Q9Y5U9IR3IP0Immediate early response 3-interacting protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15276200}; Multi-pass membrane protein {ECO:0000269|PubMed:15276200}.7regulation of fibroblast apoptotic process [GO:2000269]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: May be implicated in the regulation of apoptosis. May be involved in protein transport between endoplasmic reticulum and Golgi apparatus (By similarity). {ECO:0000250}.Q9BZD3GCOM2(Putative GRINL1B complex locus protein 27DNA-directed RNA polymerase II, holoenzyme [GO:0016591]Q15818NPTX1Neuronal pentraxin-1KSUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000305}.qaxonogenesis involved in innervation [GO:0060385]; cellular response to glucose stimulus [GO:0071333]; cellular response to potassium ion [GO:0035865]; central nervous system development [GO:0007417]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial transport [GO:0006839]; synaptic transmission [GO:0007268]; transport [GO:0006810]xmitochondrion [GO:0005739]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]FUNCTION: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses. {ECO:0000250}.O75439MPPB/Mitochondrial-processing peptidase subunit betaaerobic respiration [GO:0009060]; cellular protein metabolic process [GO:0044267]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; protein processing [GO:0016485]; protein targeting to mitochondrion [GO:0006626][mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex III [GO:0005750]gFUNCTION: Cleaves presequences (transit peptides) from mitochondrial protein precursors. {ECO:0000250}.Q9NYL4FKB11*Peptidyl-prolyl cis-trans isomerase FKBP11UFK506 binding [GO:0005528]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]Q8IUI8CRLF3Cytokine receptor-li< ke factor 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19427400}. Note=The EGFP- and MYC-tagged protein has been shown to be cytoplasmic. {ECO:0000269|PubMed:19427400}.eG1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of cell growth [GO:0030308]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]nFUNCTION: May play a role in the negative regulation of cell cycle progression. {ECO:0000269|PubMed:19427400}.Q14624ITIH4,Inter-alpha-trypsin inhibitor heavy chain H4acute-phase response [GO:0006953]; hyaluronan metabolic process [GO:0030212]; negative regulation of endopeptidase activity [GO:0010951]; response to cytokine [GO:0034097]blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]FUNCTION: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration. {ECO:0000269|PubMed:19263524}.Q9P0V9 Septin-10SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12711328}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Using a GFP-fusion protein, detected in the nucleus. {ECO:0000269|PubMed:12711328}.jFUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). {ECO:0000305}.Q92900RENT1#Regulator of nonsense transcripts 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Nucleus. Note=Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm.DNA repair [GO:0006281]; DNA replication [GO:0006260]; dosage compensation by inactivation of X chromosome [GO:0009048]; gene expression [GO:0010467]; histone mRNA catabolic process [GO:0071044]; mRNA export from nucleus [GO:0006406]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translational termination [GO:0006449]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supraspliceosomal complex [GO:0044530]FUNCTION: RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD. Essential for embryonic viability. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21145460, ECO:0000269|PubMed:21419344}.Q96AQ6PBIP1>Pre-B-cell leukemia transcription factor-interacting protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus.cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; negative regulation of transcription, DNA-templated [GO:0045892]Dcytosol [GO:0005829]; microtubule [GO:0005874]; nucleus [GO:0005634]FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling. {ECO:0000269|PubMed:10825160, ECO:0000269|PubMed:12360403, ECO:0000269|PubMed:17043237}.Q16186ADRM1$Proteasomal ubiquitin receptor ADRM1positive regulation of endopeptidase activity [GO:0010950]; proteasome assembly [GO:0043248]; transcription elongation from RNA polymerase II promoter [GO:0006368]mendopeptidase activator activity [GO:0061133]; protease binding [GO:0002020]; proteasome binding [GO:0070628]cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]'FUNCTION: Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity. {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817}.Q9BZF1OSBL8+Oxysterol-binding protein-related protein 8activation of protein kinase B activity [GO:0032148]; fat cell differentiation [GO:0045444]; lipid transport [GO:0006869]; negative regulation of cell migration [GO:0030336]; negative regulation of sequestering of triglyceride [GO:0010891]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of protein kinase B signaling [GO:0051897]; protein localization to nuclear pore [GO:0090204]4membrane [GO:0016020]; nuclear membrane [GO:0031965]UFUNCTION: Binds 25-hydroxycholesterol and cholesterol. {ECO:0000269|PubMed:17428193}.Q9UBP0SPASTSpastin;SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Endoplasmic reticulum. Endosome. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Isoform 3 is the main endosomal form.axonogenesis [GO:0007409]; cytokinetic process [GO:0032506]; cytoplasmic microtubule organization [GO:0031122]; ER to Golgi vesicle-mediated transport [GO:0006888]; microtubule bundle formation [GO:0001578]; microtubule severing [GO:0051013]; positive regulation of cytokinesis [GO:0032467]; positive regulation of microtubule depolymerization [GO:0031117]; protein hexamerization [GO:0034214]; protein homooligomerization [GO:0051260]alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; microtubule-severing ATPase activity [GO:0008568]gcentrosome [GO:0005813]; cyto< plasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]RFUNCTION: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. May also play a role in axon growth and the formation of axonal branches. {ECO:0000269|PubMed:11809724, ECO:0000269|PubMed:15716377, ECO:0000269|PubMed:16219033, ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:19000169, ECO:0000269|PubMed:22637577}.Q03167TGBR3/Transforming growth factor beta receptor type 3SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Exists both as a membrane-bound form and as soluble form in serum and in the extracellular matrix.yBMP signaling pathway [GO:0030509]; cardiac epithelial to mesenchymal transition [GO:0060317]; cardiac muscle cell proliferation [GO:0060038]; cell growth [GO:0016049]; cell migration [GO:0016477]; definitive erythrocyte differentiation [GO:0060318]; definitive hemopoiesis [GO:0060216]; epithelial to mesenchymal transition [GO:0001837]; heart morphogenesis [GO:0003007]; heart trabecula formation [GO:0060347]; immune response [GO:0006955]; intracellular signal transduction [GO:0035556]; liver development [GO:0001889]; negative regulation of cellular component movement [GO:0051271]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; organ regeneration [GO:0031100]; palate development [GO:0060021]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of protein binding [GO:0043393]; response to follicle-stimulating hormone [GO:0032354]; response to hypoxia [GO:0001666]; response to luteinizing hormone [GO:0034699]; response to prostaglandin E [GO:0034695]; transforming growth factor beta receptor complex assembly [GO:0007181]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]coreceptor activity [GO:0015026]; glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; PDZ domain binding [GO:0030165]; SMAD binding [GO:0046332]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type III [GO:0070123]; transforming growth factor beta receptor binding [GO:0005160]; type II transforming growth factor beta receptor binding [GO:0005114]Zcell surface [GO:0009986]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; inhibin-betaglycan-ActRII complex [GO:0034673]; integral component of plasma membrane [GO:0005887]; proteinaceous extracellular matrix [GO:0005578]; receptor complex [GO:0043235]FUNCTION: Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors.Q9HAV7GRPE1%GrpE protein homolog 1, mitochondrial~cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]; protein targeting to mitochondrion [GO:0006626]^adenyl-nucleotide exchange factor activity [GO:0000774]; unfolded protein binding [GO:0051082]3FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.O00115DNS2ADeoxyribonuclease-2-alpha nucleases(2)vapoptotic DNA fragmentation [GO:0006309]; DNA metabolic process [GO:0006259]; erythrocyte differentiation [GO:0030218]Ddeoxyribonuclease II activity [GO:0004531]; DNA binding [GO:0003677]9extracellular exosome [GO:0070062]; lysosome [GO:0005764]ZFUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the degradation of nuclear DNA in cellular apoptosis during development. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver, where it degrades nuclear DNA expelled from erythroid precursor cells.P46020KPB1HPhosphorylase b kinase regulatory subunit alpha, skeletal muscle isoformFUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.Q8WVE0N6MT2-N(6)-adenine-specific DNA methyltransferase 2BSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03187}.Jmethyltransferase activity [GO:0008168]; nucleic acid binding [GO:0003676]FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha. {ECO:0000255|HAMAP-Rule:MF_03187}.Q96EU6RRP36+Ribosomal RNA processing protein 36 homologSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20038530}. Note=Concentrated in the fibrillar region of the nucleolus.maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]J90S preribosome [GO:0030686]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA. {ECO:0000269|PubMed:20038530}.Q96GI7FA89AProtein FAM89AQ13308PTK7"Inactive tyrosine-protein kinase 7 RegulatorSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20837484}; Single-pass type I membrane protein {ECO:0000269|PubMed:20837484}. Cell junction {ECO:0000269|PubMed:20837484}. Note=Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.actin cytoskeleton reorganization [GO:0031532]; axis elongation [GO:0003401]; canonical Wnt signaling pathway [GO:0060070]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cellular response to retinoic acid [GO:0071300]; cochlea morphogenesis [GO:0090103]; convergent extension [GO:0060026]; establishment of epithelial cell apical/basal polarity [GO:0045198]; establishment of planar polarity [GO:0001736]; lung-associated mesenchyme development [GO:0060484]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of neuron projection development [GO:0010976]; signal transduction [GO:0007165]; wound healing [GO:0042060]GATP binding [GO:0005524]; protein tyrosine kinase activity [GO:0004713]pcell-cell junction [GO:0005911]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]%FUNCTION: Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis. {ECO:0000269|PubMed:18471990, ECO:0000269|PubMed:20558616, ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:21103379, ECO:0000269|PubMed:21132015}.Q96IW7SC22A"Vesicle-trafficking protein SEC22aER to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]; vesicle fusion with Golgi apparatus [GO:0048280]tendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; SNARE complex [GO:0031201]tFUNCTION: May< be involved in vesicle transport between the ER and the Golgi complex. {ECO:0000250|UniProtKB:Q642F4}.Q8IWE4DCNL3DCN1-like protein 3BSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25349211}.negative regulation of cell growth [GO:0030308]; positive regulation of apoptotic process [GO:0043065]; response to gamma radiation [GO:0010332]; response to UV-C [GO:0010225]Jperinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886],FUNCTION: Antagonizes DCUN1D1-mediated CUL1 neddylation by sequestering CUL1 at the cell membrane (PubMed:25349211). When overexpressed in transformed cells, may promote mesenchymal to epithelial-like changes and inhibit colony formation in soft agar (PubMed:25349211). {ECO:0000269|PubMed:25349211}.O14967CLGNCalmeginbinding of sperm to zona pellucida [GO:0007339]; protein complex assembly [GO:0006461]; protein folding [GO:0006457]; single fertilization [GO:0007338]Gcalcium ion binding [GO:0005509]; unfolded protein binding [GO:0051082]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; nuclear envelope [GO:0005635]mFUNCTION: Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions (By similarity). {ECO:0000250}.Q9BPX6MICU1'Calcium uptake protein 1, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. Mitochondrion intermembrane space. Note=Localizes at the outer surface of the mitochondrion inner membrane.]calcium ion import [GO:0070509]; calcium ion transmembrane import into mitochondrion [GO:0036444]; defense response [GO:0006952]; mitochondrial calcium ion homeostasis [GO:0051560]; mitochondrial calcium ion transport [GO:0006851]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; protein homooligomerization [GO:0051260]zcalcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]calcium channel complex [GO:0034704]; integral component of mitochondrial membrane [GO:0032592]; intracellular [GO:0005622]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; uniplex complex [GO:1990246]FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required to increase calcium uptake by MCU when cytoplasmic calcium is high. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, respectively. MICU1 acts as a stimulator of MCU that senses calcium level via its EF-hand domains: enhances MCU opening at high Ca(2+) concentration, allowing a rapid response of mitochondria to Ca(2+) signals generated in the cytoplasm. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG. {ECO:0000269|PubMed:16002733, ECO:0000269|PubMed:20693986, ECO:0000269|PubMed:22904319, ECO:0000269|PubMed:23101630, ECO:0000269|PubMed:23747253, ECO:0000269|PubMed:24313810, ECO:0000269|PubMed:24332854, ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927}.Q8N7H5PAF1-RNA polymerase II-associated factor 1 homologSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491129}. Note=Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin.tcellular response to lipopolysaccharide [GO:0071222]; endodermal cell fate commitment [GO:0001711]; histone H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; mRNA polyadenylation [GO:0006378]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome positioning [GO:0016584]; positive regulation of histone methylation [GO:0031062]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein localization to nucleus [GO:0034504]; stem cell maintenance [GO:0019827]; transcription elongation from RNA polymerase II promoter [GO:0006368]; Wnt signaling pathway [GO:0016055]Kchromatin binding [GO:0003682]; RNA polymerase II core binding [GO:0000993]NCdc73/Paf1 complex [GO:0016593]; cytoplasm [GO:0005737]; membrane [GO:0016020]FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro. {ECO:0000269|PubMed:16491129, ECO:0000269|PubMed:19410543, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879, ECO:0000269|PubMed:22419161}.Q8IZ81ELMD2 ELMO domain-containing protein 2\defense response to virus [GO:0051607]; regulation of defense response to virus [GO:0050688]FUNCTION: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family. Regulates IFN-related antiviral responses. {ECO:0000269|PubMed:17452337, ECO:0000269|PubMed:19966137}.O43390HNRPR)Heterogeneous nuclear ribonucleoprotein RSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]; spliceosomal complex [GO:0005681]FUNCTION: Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.P29317EPHA2Ephrin type-A receptor 2\SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane; Single-pass type I membrane protein. Cell projection, lamellipodium membrane; Single-pass type I membrane protein. Cell junction, focal adhesion. Note=Present at regions of cell-cell contacts but also at the leading edge of migrating cells.activation of GTPase activity [GO:0090630];< angiogenesis [GO:0001525]; axial mesoderm formation [GO:0048320]; axon guidance [GO:0007411]; bone remodeling [GO:0046849]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; keratinocyte differentiation [GO:0030216]; lens fiber cell morphogenesis [GO:0070309]; mammary gland epithelial cell proliferation [GO:0033598]; multicellular organismal development [GO:0007275]; negative regulation of protein kinase B signaling [GO:0051898]; neural tube development [GO:0021915]; notochord cell development [GO:0060035]; notochord formation [GO:0014028]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; post-anal tail morphogenesis [GO:0036342]; protein kinase B signaling [GO:0043491]; regulation of angiogenesis [GO:0045765]; regulation of blood vessel endothelial cell migration [GO:0043535]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of lamellipodium assembly [GO:0010591]; response to growth factor [GO:0070848]; skeletal system development [GO:0001501]; vasculogenesis [GO:0001570]; viral process [GO:0016032]ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] cell surface [GO:0009986]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; lamellipodium membrane [GO:0031258]; leading edge membrane [GO:0031256]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]0FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. {ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:16236711, ECO:0000269|PubMed:18339848, ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:20861311, ECO:0000269|PubMed:23358419}.Q13907IDI1)Isopentenyl-diphosphate Delta-isomerase 1cholesterol biosynthetic process [GO:0006695]; dimethylallyl diphosphate biosynthetic process [GO:0050992]; isoprenoid biosynthetic process [GO:0008299]; small molecule metabolic process [GO:0044281]hydrolase activity [GO:0016787]; isopentenyl-diphosphate delta-isomerase activity [GO:0004452]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]-cytosol [GO:0005829]; peroxisome [GO:0005777]FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000269|PubMed:8806705}.Q6ZWL3CP4V2Cytochrome P450 4V2! Lipid metabolism. {ECO:0000305}.SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22772592}; Single-pass membrane protein {ECO:0000305}.jfatty acid omega-oxidation [GO:0010430]; response to stimulus [GO:0050896]; visual perception [GO:0007601]DFUNCTION: Omega-hydroxylase that oxidizes medium-chain saturated fatty acids and polyunsaturated omega-3 fatty acids, and which plays a role in fatty acid and steroid metabolism in the eye (PubMed:19661213, PubMed:22772592). Catalyzes the omega-hydroxylation of medium-chain saturated fatty acids such as laurate, myristate and palmitate in an NADPH-dependent pathway. The substrate specificity is higher for myristate > laurate > palmitate (C14>C16>C12) (PubMed:19661213). Acts as a polyunsaturated omega-3 fatty acids hydroxylase by mediating oxidation of docosahexaenoate (DHA) to 22-hydroxydocosahexaenoate (PubMed:22772592). Also produces some 21-hydroxydocosahexaenoate. Also converts eicosapentaenoate (EPA) to 20-hydroxyeicosapentaenoate (20-OH-EPA) (PubMed:22772592). {ECO:0000269|PubMed:19661213, ECO:0000269|PubMed:22772592}.Q8WVV9HNRLL.Heterogeneous nuclear ribonucleoprotein L-likeNmRNA processing [GO:0006397]; positive regulation of RNA splicing [GO:0033120]Smembrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: RNA-binding protein that functions as regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. {ECO:0000269|PubMed:18669861}.Q5VTB9RN220"E3 ubiquitin-protein ligase RNF220?SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6PDX6}.positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]ZFUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling (PubMed:25266658). {ECO:0000250|UniProtKB:Q6PDX6, ECO:0000269|PubMed:25266658}.O75676KS6A4#Ribosomal protein S6 kinase alpha-4XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:9792677}.axon guidance [GO:0007411]; histone H3-S10 phosphorylation [GO:0043987]; histone H3-S28 phosphorylation [GO:0043988]; histone phosphorylation [GO:0016572]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; negative regulation of cytokine production [GO:0001818]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of histone acetylation [GO:0035066]; positive regulation of histone phosphorylation [GO:0033129]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of transcription, DNA-templated [GO:0006355]ATP binding [GO:0005524]; histone kinase activity (H3-S10 specific) [GO:0035175]; magnesium ion binding [GO:0000287]; mitogen-activated protein kinase p38 binding [GO:0048273]; protein serine/threonine kinase activity [GO:0004674]; ribosomal protein S6 kinase activity [GO:0004711]WFUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress < stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:9792677}.Q7RTP6MICA3+Protein-methionine sulfoxide oxidase MICAL3SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Note=Mainly localizes in the nucleus. {ECO:0000269|PubMed:24440334}.actin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; exocytosis [GO:0006887]; oxidation-reduction process [GO:0055114]actin binding [GO:0003779]; FAD binding [GO:0071949]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process. {ECO:0000269|PubMed:21596566, ECO:0000269|PubMed:24440334}.Q07666KHDR1KKH domain-containing, RNA-binding, signal transduction-associated protein 1bSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1374686}. Membrane {ECO:0000269|PubMed:1374686}.>cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; G2/M transition of mitotic cell cycle [GO:0000086]; mRNA processing [GO:0006397]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of RNA export from nucleus [GO:0046833]; positive regulation of signal transduction [GO:0009967]; positive regulation of translational initiation [GO:0045948]; regulation of RNA export from nucleus [GO:0046831]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; identical protein binding [GO:0042802]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; SH3/SH2 adaptor activity [GO:0005070]|cytoplasm [GO:0005737]; Grb2-Sos complex [GO:0070618]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). {ECO:0000269|PubMed:22253824}.; FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. {ECO:0000269|PubMed:9013542}.O95721SNP29"Synaptosomal-associated protein 29}SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23217709}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:25686604}; Peripheral membrane protein {ECO:0000305}. Cell projection, cilium membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250}.autophagosome fusion [GO:0000046]; exocytosis [GO:0006887]; membrane fusion [GO:0061025]; protein transport [GO:0015031]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle targeting [GO:0006903]BSNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]autophagosome membrane [GO:0000421]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]KFUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Plays also a role in ciliogenesis by regulating membrane fusions. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}.P84101SERF2Small EDRK-rich factor 2Q14393GAS6 Growth arrest-specific protein 6<SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9326369}.Zactivation of protein kinase B activity [GO:0032148]; apoptotic cell clearance [GO:0043277]; B cell chemotaxis [GO:0035754]; blood coagulation [GO:0007596]; calcium ion transmembrane transport [GO:0070588]; cell adhesion [GO:0007155]; cell cycle arrest [GO:0007050]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cell-substrate adhesion [GO:0031589]; cellular protein metabolic process [GO:0044267]; cellular response to drug [GO:0035690]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; cellular response to interferon-alpha [GO:0035457]; cellular response to starvation [GO:0009267]; cellular response to vitamin K [GO:0071307]; dendritic cell differentiation [GO:0097028]; enzyme linked receptor protein signaling pathway [GO:0007167]; extracellular matrix assembly [GO:0085029]; fusion of virus membrane with host plasma membrane [GO:0019064]; hematopoietic stem cell migration to bone marrow [GO:0097241]; leukocyte migration [GO:0050900]; macrophage cytokine production [GO:0010934]; negative regulation of apoptotic process [GO:0043066]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of dendritic cell apoptotic process [GO:2000669]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of fibroblast apoptotic process [GO:2000270]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of interleukin-1 secretion [GO:0050711]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of interleukin-6 secretion [GO:1900165]; negative regulation of oligodendrocyte apoptotic process [GO:1900142]; negative regulation of protein import into nucleus, translocation [GO:0033159]; negative regulation of renal < albumin absorption [GO:2000533]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of tumor necrosis factor production [GO:0032720]; neuron migration [GO:0001764]; organ regeneration [GO:0031100]; peptidyl-glutamic acid carboxylation [GO:0017187]; peptidyl-serine phosphorylation [GO:0018105]; phagocytosis [GO:0006909]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of glomerular filtration [GO:0003104]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of TOR signaling [GO:0032008]; post-translational protein modification [GO:0043687]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; protein targeting to plasma membrane [GO:0072661]; proteolysis [GO:0006508]; receptor-mediated virion attachment to host cell [GO:0046813]; regulation of growth [GO:0040008]; signal transduction [GO:0007165]; viral entry into host cell [GO:0046718]; viral genome replication [GO:0019079]binding, bridging [GO:0060090]; calcium ion binding [GO:0005509]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; phosphatidylserine binding [GO:0001786]; protein tyrosine kinase activator activity [GO:0030296]; receptor agonist activity [GO:0048018]; receptor binding [GO:0005102]; receptor tyrosine kinase binding [GO:0030971]; voltage-gated calcium channel activity [GO:0005245]cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; platelet alpha granule lumen [GO:0031093]@FUNCTION: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. {ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:18840707}.O43663PRC1"Protein regulator of cytokinesis 1 SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Note=Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles and localizes with the cell midbody during cytokinesis.ycytokinesis [GO:0000910]; mitotic spindle elongation [GO:0000022]; small GTPase mediated signal transduction [GO:0007264]iidentical protein binding [GO:0042802]; kinesin binding [GO:0019894]; protein kinase binding [GO:0019901]cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]nFUNCTION: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. {ECO:0000269|PubMed:12082078, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902, ECO:0000269|PubMed:9885575}.Q9BUM1G6PC3Glucose-6-phosphatase 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:13129915}; Multi-pass membrane protein {ECO:0000269|PubMed:13129915}.]carbohydrate metabolic process [GO:0005975]; dephosphorylation [GO:0016311]; gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glucose-6-phosphate transport [GO:0015760]; glucose transport [GO:0015758]; hexose transport [GO:0008645]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]+glucose-6-phosphatase activity [GO:0004346]endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function. {ECO:0000269|PubMed:12370122, ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:13129915}.Q9H6U6BCAS3%Breast carcinoma-amplified sequence 3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058}. Cytoplasm {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:18030336}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8CCN5}. Note=Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells (By similarity). Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner. {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.activation of GTPase activity [GO:0090630]; angiogenesis [GO:0001525]; cellular response to estrogen stimulus [GO:0071391]; Golgi organization [GO:0007030]; microtubule organizing center organization [GO:0031023]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of GTPase activity [GO:0034260]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of catalytic activity [GO:0043085]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of establishment of cell polarity [GO:2000114]; response to starvation [GO:0042594]; transcription, DNA-templated [GO:0006351]; tube formation [GO:0035148]acetyltransferase activator activity [GO:0010698]; beta-tubulin binding [GO:0048487]; chromatin binding [GO:0003682]; histone acetyltransferase binding [GO:0035035]; histone binding [GO:0042393]; nuclear hormone receptor binding [GO:0035257]; transcription factor binding [GO:0008134]cell leading edge [GO:0031252]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; intermediate filament cytoskeleton [GO:0045111]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]"FUNCTION: Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at th< e cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.Q9BQA1MEP50Methylosome protein 50SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear in Leydig cells and cytoplasmic in germ cells during fetal testicular development. In adult testis, predominantly nuclear. Subcellular location varies from nuclear to cytoplasmic in various tumors.chromatin organization [GO:0006325]; gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; negative regulation of epithelial cell proliferation involved in prostate gland development [GO:0060770]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development [GO:0060528]; spliceosomal snRNP assembly [GO:0000387]Qligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Non-catalytic component of the 20S PRMT5-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The 20S PRMT5-containing methyltransferase complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. {ECO:0000269|PubMed:11756452, ECO:0000269|PubMed:23071334}.Q7RTV0PHF5A,PHD finger-like domain-containing protein 5AKSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}.gene expression [GO:0010467]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of transcription, DNA-templated [GO:0045893]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]catalytic step 2 spliceosome [GO:0071013]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; precatalytic spliceosome [GO:0071011]; U12-type spliceosomal complex [GO:0005689]; U2 snRNP [GO:0005686]FUNCTION: Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha. Also involved in pre-mRNA splicing. {ECO:0000269|PubMed:12234937}.P36404ARL2&ADP-ribosylation factor-like protein 2SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. {ECO:0000250}.{bicellular tight junction assembly [GO:0070830]; cell cycle [GO:0007049]; centrosome organization [GO:0051297]; energy reserve metabolic process [GO:0006112]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of GTPase activity [GO:0034260]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of microtubule polymerization [GO:0031116]; regulation of insulin secretion [GO:0050796]; regulation of microtubule polymerization [GO:0031113]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; tubulin complex assembly [GO:0007021]xGDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTPase inhibitor activity [GO:0005095]; GTP binding [GO:0005525]centrosome [GO:0005813]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lateral plasma membrane [GO:0016328]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]#FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. {ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:16525022, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18588884, ECO:0000269|PubMed:20740604}.P35606COPB2Coatomer subunit beta'+SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}. FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250}.; FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner (By similarity). Interacts with JAGN1. {ECO:0000250, ECO:0000269|PubMed:25129144}.A8MYA2CX049Uncharacterized protein CXorf49P55036PSMD4.26S proteasome non-ATPase regulatory subunit 4Hidentical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]FUNCTION: Binds and presumably selects ubiquitin-conjugates for destruction. Displays selectivity for longer polyubiquitin chains. Modulates intestinal fluid secretion.Q02127PYRD5Dihydroorotate dehydrogenase (quinone), mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10727948}; Single-pass membrane protein {ECO:0000269|PubMed:10727948}.[de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; female pregnancy [GO:0007565]; lactation [< GO:0007595]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of apoptotic process [GO:0043065]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; regulation of mitochondrial fission [GO:0090140]; response to caffeine [GO:0031000]; response to drug [GO:0042493]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]dihydroorotate dehydrogenase activity [GO:0004152]; drug binding [GO:0008144]; FMN binding [GO:0010181]; ubiquinone binding [GO:0048039]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]bFUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.Q9HBM6TAF9B0Transcription initiation factor TFIID subunit 9B\gene expression [GO:0010467]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell growth [GO:0030307]; protein stabilization [GO:0050821]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]ynucleoplasm [GO:0005654]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276]FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. {ECO:0000269|PubMed:15899866}.Q9Y520PRC2CProtein PRRC2CIpoly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]Q9H490PIGU?Phosphatidylinositol glycan anchor biosynthesis class U proteinattachment of GPI anchor to protein [GO:0016255]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; GPI anchor biosynthetic process [GO:0006506]; post-translational protein modification [GO:0043687]; regulation of JAK-STAT cascade [GO:0046425]endoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI. {ECO:0000269|PubMed:12802054}.Q5GLZ8HERC4*Probable E3 ubiquitin-protein ligase HERC4wSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15676274}. Note=shows a punctate cytoplasmic distribution.cell differentiation [GO:0030154]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; spermatogenesis [GO:0007283]FUNCTION: Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates (By similarity). {ECO:0000250}.O75122CLAP2CLIP-associating protein 2ZSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Golgi apparatus {ECO:0000250|UniProtKB:Q8BRT1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17543864}. Cell membrane {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane {ECO:0000269|PubMed:20937854}. Note=Localizes to microtubule plus ends (PubMed:15631994). Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase (PubMed:16866869, PubMed:16914514). In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2 (PubMed:16824950). The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane. {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:20937854}._axon guidance [GO:0007411]; cell division [GO:0051301]; establishment of protein localization to plasma membrane [GO:0090002]; establishment or maintenance of cell polarity [GO:0007163]; fucosylation [GO:0036065]; Golgi organization [GO:0007030]; microtubule anchoring [GO:0034453]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleation [GO:0007020]; microtubule organizing center organization [GO:0031023]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of stress fiber assembly [GO:0051497]; negative regulation of wound healing, spreading of epidermal cells [GO:1903690]; positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of exocytosis [GO:0045921]; positive regulation of extracellular matrix disassembly [GO:0090091]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gastrulation [GO:0010470]; regulation of microtubule-based process [GO:0032886]; regulation of microtubule polymerization or depolymerization [GO:0031110]; small GTPase mediated signal transduction [GO:0007264]; vesicle targeting [GO:0006903]dystroglycan binding [GO:0002162]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107]; microtubule plus-end binding [GO:0051010]basal cortex [GO:0045180]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; kinetochore microtubule [GO:0005828]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; trans-Golgi network [GO:0005802]FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of < microtubules at the cell cortex. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.Q8NFD5ARI1B0AT-rich interactive domain-containing protein 1BbSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:11988099}.chromatin-mediated maintenance of transcription [GO:0048096]; nervous system development [GO:0007399]; transcription, DNA-templated [GO:0006351]icytoplasm [GO:0005737]; nBAF complex [GO:0071565]; nucleoplasm [GO:0005654]; SWI/SNF complex [GO:0016514]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically. {ECO:0000250}.Q53GQ0DHB12"Estradiol 17-beta-dehydrogenase 12SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12482854}; Multi-pass membrane protein {ECO:0000269|PubMed:12482854}.cellular lipid metabolic process [GO:0044255]; estrogen biosynthetic process [GO:0006703]; extracellular matrix organization [GO:0030198]; fatty acid biosynthetic process [GO:0006633]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of cell-substrate adhesion [GO:0010811]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]Sestradiol 17-beta-dehydrogenase activity [GO:0004303]; heparin binding [GO:0008201]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16166196}.O75506HSBP1#Heat shock factor-binding protein 1HSFscellular response to heat [GO:0034605]; endodermal cell differentiation [GO:0035987]; muscle contraction [GO:0006936]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of cellular response to heat [GO:1900034]Icytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.Q53S33BOLA3BolA-like protein 3xSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18548201}. Note=Could be secreted via a non-classical export pathway.P49354FNTAJProtein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaapoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; neurotransmitter receptor metabolic process [GO:0045213]; phototransduction, visible light [GO:0007603]; positive regulation of deacetylase activity [GO:0090045]; positive regulation of tubulin deacetylation [GO:0090044]; programmed cell death [GO:0012501]; protein farnesylation [GO:0018343]; protein geranylgeranylation [GO:0018344]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; rhodopsin mediated signaling pathway [GO:0016056]; transforming growth factor beta receptor signaling pathway [GO:0007179][acetylcholine receptor regulator activity [GO:0030548]; alpha-tubulin binding [GO:0043014]; CAAX-protein geranylgeranyltransferase activity [GO:0004662]; microtubule binding [GO:0008017]; protein farnesyltransferase activity [GO:0004660]; protein geranylgeranyltransferase activity [GO:0004661]; Rab geranylgeranyltransferase activity [GO:0004663]CAAX-protein geranylgeranyltransferase complex [GO:0005953]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule associated complex [GO:0005875]; protein farnesyltransferase complex [GO:0005965]FUNCTION: Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8419339, ECO:0000269|PubMed:8494894}.Q27J81INF2Inverted formin-2RSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20023659}.actin cytoskeleton organization [GO:0030036]; regulation of cellular component size [GO:0032535]; regulation of mitochondrial fission [GO:0090140]~cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]jFUNCTION: Severs actin filaments and accelerates their polymerization and depolymerization. {ECO:0000250}.Q9BXJ9NAA154N-alpha-acetyltransferase 15, NatA auxiliary subunitSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes.<angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; negative regulation of apoptotic process [GO:0043066]; N-terminal protein amino acid acetylation [GO:0006474]; positive regulation of transcription, DNA-templated [GO:0045893]; protein stabilization [GO:0050821]; transcription, DNA-templated [GO:0006351]jN-acetyltransferase activity [GO:0008080]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]cytoplasm [GO:0005737]; membrane [GO:0016020]; NatA complex [GO:0031415]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. {ECO:0000269|PubMed:11687548, ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:15496142}.P50416CPT1A1Carnitine O-palmitoyltransferase 1, liver isoformSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:145< 17221}; Multi-pass membrane protein {ECO:0000269|PubMed:11350182, ECO:0000269|PubMed:14517221}.carnitine metabolic process [GO:0009437]; carnitine shuttle [GO:0006853]; cellular lipid metabolic process [GO:0044255]; cellular response to fatty acid [GO:0071398]; circadian rhythm [GO:0007623]; eating behavior [GO:0042755]; epithelial cell differentiation [GO:0030855]; fatty acid beta-oxidation [GO:0006635]; glucose metabolic process [GO:0006006]; long-chain fatty acid metabolic process [GO:0001676]; positive regulation of fatty acid beta-oxidation [GO:0032000]; protein homooligomerization [GO:0051260]; regulation of insulin secretion [GO:0050796]; response to drug [GO:0042493]; response to organic cyclic compound [GO:0014070]; small molecule metabolic process [GO:0044281]; triglyceride metabolic process [GO:0006641]6carnitine O-palmitoyltransferase activity [GO:0004095]integral component of mitochondrial outer membrane [GO:0031307]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]!FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism.Q8N3D4EH1L1*EH domain-binding protein 1-like protein 1Q15070OXA1L*Mitochondrial inner membrane protein OXA1LSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17936786}; Multi-pass membrane protein {ECO:0000269|PubMed:17936786}. aerobic respiration [GO:0009060]; mitochondrial proton-transporting ATP synthase complex assembly [GO:0033615]; mitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrial respiratory chain complex I biogenesis [GO:0097031]; negative regulation of ATPase activity [GO:0032780]; negative regulation of oxidoreductase activity [GO:0051354]; oxidation-reduction process [GO:0055114]; protein complex assembly [GO:0006461]; protein insertion into membrane [GO:0051205]; protein tetramerization [GO:0051262][mitochondrial ribosome binding [GO:0097177]; protein homodimerization activity [GO:0042803]integral component of mitochondrial membrane [GO:0032592]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain [GO:0005746]; mitochondrion [GO:0005739]; protein complex [GO:0043234]6FUNCTION: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome oxidase. Required for the correct biogenesis of ATP synthase and complex I in mitochondria. {ECO:0000269|PubMed:17936786, ECO:0000269|PubMed:7991568}.P53384NUBP1,Cytosolic Fe-S cluster assembly factor NUBP1_SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:18573874}.2cell growth [GO:0016049]; cellular iron ion homeostasis [GO:0006879]; centrosome localization [GO:0051642]; iron-sulfur cluster assembly [GO:0016226]; negative regulation of centrosome duplication [GO:0010826]; protein localization to cell cortex [GO:0072697]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]FUNCTION: Implicated in the regulation of centrosome duplication (By similarity). Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. {ECO:0000250, ECO:0000269|PubMed:18573874}.Q96F85CNRP1.CB1 cannabinoid receptor-interacting protein 1myelin sheath [GO:0043209]FUNCTION: Isoform 1 suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels. Isoform 2 does not have this effect. {ECO:0000269|PubMed:17895407}.Q6ZSR9YJ005 Uncharacterized protein FLJ45252Q5TCZ1SPD2A'SH3 and PX domain-containing protein 2ASUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.Iosteoclast fusion [GO:0072675]; superoxide metabolic process [GO:0006801]NFUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide. {ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15710328, ECO:0000269|PubMed:15710903, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.Q08431MFGM LactadherinSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19204935}; Peripheral membrane protein {ECO:0000269|PubMed:19204935}. Secreted {ECO:0000269|PubMed:19204935}.\angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; phagocytosis, engulfment [GO:0006911]; phagocytosis, recognition [GO:0006910]; positive regulation of apoptotic cell clearance [GO:2000427]; positive regulation of cell proliferation [GO:0008284]; response to estrogen [GO:0043627]; single fertilization [GO:0007338]; viral process [GO:0016032]Vphosphatidylethanolamine binding [GO:0008429]; phosphatidylserine binding [GO:0001786]external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; extrinsic component of plasma membrane [GO:0019897]; membrane [GO:0016020]FUNCTION: Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Binds specifically to rotavirus and inhibits its replication. {ECO:0000250, ECO:0000269|PubMed:19204935}.; FUNCTION: Medin is the main constituent of aortic medial amyloid. {ECO:0000269|PubMed:19204935}.P08621RU17)U1 small nuclear ribonucleoprotein 70 kDaSUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Colocalizes with SCNM1 and LUC7L2 in nuclear speckles. {ECO:0000250}.gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA.Q9NVT9ARMC1%Armadillo repeat-containing protein 1 metal ion transport [GO:0030001]Q7Z2Z2ETUD1<Elongation factor Tu GTP-binding domain-containing protein 1%mature ribosome assembly [GO:0042256]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; ribosome binding [GO:0043022]; translation elongation factor activity [GO:0003746]%FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling t< o the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits. {ECO:0000269|PubMed:21536732}.O94906PRP6Pre-mRNA-processing factor 6aSUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus speckle. Note=Localized in splicing speckles.vgene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; RNA localization [GO:0006403]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]; spliceosomal tri-snRNP complex assembly [GO:0000244]androgen receptor binding [GO:0050681]; poly(A) RNA binding [GO:0044822]; ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723]; transcription coactivator activity [GO:0003713] catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]dFUNCTION: Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. {ECO:0000269|PubMed:12039962}.Q9H300PARL;Presenilins-associated rhomboid-like protein, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17116872}; Multi-pass membrane protein {ECO:0000269|PubMed:17116872}.; SUBCELLULAR LOCATION: P-beta: Nucleus. Note=Translocated into the nucleus by an unknown mechanism.membrane protein proteolysis [GO:0033619]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; protein processing [GO:0016485]; proteolysis [GO:0006508]; regulation of mitochondrion degradation [GO:1903146]; regulation of protein targeting to mitochondrion [GO:1903214]; regulation of proteolysis [GO:0030162]; regulation of reactive oxygen species metabolic process [GO:2000377]Tendopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals (By similarity). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain. {ECO:0000250, ECO:0000269|PubMed:14732705, ECO:0000269|PubMed:17116872}.Q96CW5GCP3!Gamma-tubulin complex component 3YSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.G2/M transition of mitotic cell cycle [GO:0000086]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; single fertilization [GO:0007338]gamma-tubulin binding [GO:0043015]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; polar microtubule [GO:0005827]; spindle [GO:0005819]ZFUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.Q9UKU7ACAD8+Isobutyryl-CoA dehydrogenase, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11013134}.branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; regulation of transcription, DNA-templated [GO:0006355]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; valine catabolic process [GO:0006574]acyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]FUNCTION: Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex. {ECO:0000269|PubMed:12359132}.O15391TYY2Transcription factor YY2FUNCTION: Functions as a multifunctional transcription factor that may exhibit positive and negative control on a large number of genes. May antagonize YY1 and function in development and differentiation. {ECO:0000269|PubMed:16260628}.Q12824SNF5]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1nATP-dependent chromatin remodeling [GO:0043044]; blastocyst hatching [GO:0001835]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA integration [GO:0015074]; DNA repair [GO:0006281]; mitotic cell cycle phase transition [GO:0044772]; negative regulation of cell proliferation [GO:0008285]; nervous system development [GO:0007399]; nucleosome disassembly [GO:0006337]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; single stranded viral RNA replication via double stranded DNA intermediate [GO:0039692]; transcription, DNA-templated [GO:0006351]kp53 binding [GO:0002039]; Tat protein binding [GO:0030957]; transcription coactivator activity [GO:0003713]nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]; XY body [GO:0001741]FUNCTION: Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. {ECO:0000250, ECO:0000269|Pub< Med:10078207, ECO:0000269|PubMed:12226744, ECO:0000269|PubMed:14604992, ECO:0000269|PubMed:16267391, ECO:0000269|PubMed:16314535, ECO:0000269|PubMed:9448295}.Q92930RAB8BRas-related protein Rab-8BSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:21255211}; Lipid-anchor {ECO:0000269|PubMed:21255211}; Cytoplasmic side {ECO:0000269|PubMed:21255211}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.adherens junction organization [GO:0034332]; antigen processing and presentation [GO:0019882]; cellular response to insulin stimulus [GO:0032869]; Golgi vesicle fusion to target membrane [GO:0048210]; positive regulation of cell projection organization [GO:0031346]; positive regulation of corticotropin secretion [GO:0051461]; protein import into peroxisome membrane [GO:0045046]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0017157]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking involved in exocytosis [GO:0006904]oGDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; receptor binding [GO:0005102]cell tip [GO:0051286]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; synaptic vesicle [GO:0008021]; trans-Golgi network transport vesicle [GO:0030140]:FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity). {ECO:0000250}.Q9Y295DRG1/Developmentally-regulated GTP-binding protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15676025, ECO:0000269|PubMed:19819225}. Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes.\multicellular organismal development [GO:0007275]; transcription, DNA-templated [GO:0006351]kGTP binding [GO:0005525]; identical protein binding [GO:0042802]; transcription factor binding [GO:0008134]Dcytoplasm [GO:0005737]; membrane [GO:0016020]; polysome [GO:0005844]{FUNCTION: Critical regulator of cell growth under specific conditions. Implicated in differentiation and cell cycle arrest.Q969E2SCAM4/Secretory carrier-associated membrane protein 4Kintegral component of membrane [GO:0016021]; transport vesicle [GO:0030133]KFUNCTION: Probably involved in membrane protein trafficking. {ECO:0000250}.P49768PSN1 Presenilin-1XSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell surface. Cell membrane {ECO:0000269|PubMed:21143716}. Note=Bound to NOTCH1 also at the cell surface. Colocalizes with CDH1/2 at sites of cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum and the proximity of the plasma membrane. Also present in azurophil granules of neutrophils. Colocalizes with UBQLN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes (PubMed:21143716). {ECO:0000269|PubMed:21143716}.J activation of MAPKK activity [GO:0000186]; amyloid precursor protein catabolic process [GO:0042987]; autophagosome assembly [GO:0000045]; beta-amyloid formation [GO:0034205]; beta-amyloid metabolic process [GO:0050435]; blood vessel development [GO:0001568]; brain morphogenesis [GO:0048854]; Cajal-Retzius cell differentiation [GO:0021870]; calcium ion transmembrane transport [GO:0070588]; canonical Wnt signaling pathway [GO:0060070]; cell fate specification [GO:0001708]; cellular response to DNA damage stimulus [GO:0006974]; cerebral cortex cell migration [GO:0021795]; choline transport [GO:0015871]; dorsal/ventral neural tube patterning [GO:0021904]; embryonic limb morphogenesis [GO:0030326]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; epithelial cell proliferation [GO:0050673]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; heart looping [GO:0001947]; hematopoietic progenitor cell differentiation [GO:0002244]; intracellular signal transduction [GO:0035556]; L-glutamate transport [GO:0015813]; membrane protein ectodomain proteolysis [GO:0006509]; memory [GO:0007613]; mitochondrial transport [GO:0006839]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of apoptotic process [GO:0043066]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of axonogenesis [GO:0050771]; negative regulation of epidermal growth factor-activated receptor activity [GO:0007175]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000059]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; neural retina development [GO:0003407]; neuron apoptotic process [GO:0051402]; neuron development [GO:0048666]; neuron migration [GO:0001764]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; positive regulation of coagulation [GO:0050820]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor recycling [GO:0001921]; positive regulation of transcription, DNA-templated [GO:0045893]; post-embryonic development [GO:0009791]; protein glycosylation [GO:0006486]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation of phosphorylation [GO:0042325]; regulation of protein binding [GO:0043393]; regulation of resting membrane potential [GO:0060075]; regulation of synaptic plasticity [GO:0048167]; regulation of synaptic transmission, glutamatergic [GO:0051966]; response to oxidative stress [GO:0006979]; single organismal cell-cell adhesion [GO:0016337]; skeletal system morphogenesis [GO:0048705]; skin morphogenesis [GO:0043589]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563]; somitogenesis [GO:0001756]; synaptic vesicle targeting [GO:0016080]; T cell activation involved in immune response [GO:0002286]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]aspartic-type endopeptidase activity [GO:0004190]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium channel activity [GO:0005262]; endopeptidase activity [GO:0004175]; PDZ domain binding [GO:0030165]2aggresome [GO:0016235]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; cell cortex [GO:0005938]; cell surface [GO:0009986]; centrosome [GO:0005813]; ciliary rootlet [GO:0035253]; cytoplasmic vesicle [GO:0031410]; dendritic shaft [GO:0043198]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; kinetochore [GO:0000776]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; neurom< uscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]; smooth endoplasmic reticulum [GO:0005790]; Z disc [GO:0030018]FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx, cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin, thus negatively regulating Wnt signaling. May also play a role in hematopoiesis. {ECO:0000269|PubMed:10206644, ECO:0000269|PubMed:10545183, ECO:0000269|PubMed:10593990, ECO:0000269|PubMed:10811883, ECO:0000269|PubMed:10899933, ECO:0000269|PubMed:11226248, ECO:0000269|PubMed:15341515, ECO:0000269|PubMed:16305624}.P61587RND3$Rho-related GTP-binding protein RhoELSUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein.actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; small GTPase mediated signal transduction [GO:0007264]\extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]tFUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.Q9NQH7XPP3!Probable Xaa-Pro aminopeptidase 3BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20179356}.Cglomerular filtration [GO:0003094]; protein processing [GO:0016485]paminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metallopeptidase activity [GO:0008237]P63092GNAS2DGuanine nucleotide-binding protein G(s) subunit alpha isoforms shortGqalphaNSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; blood coagulation [GO:0007596]; bone development [GO:0060348]; cAMP biosynthetic process [GO:0006171]; cellular response to catecholamine stimulus [GO:0071870]; cellular response to glucagon stimulus [GO:0071377]; cellular response to prostaglandin E stimulus [GO:0071380]; cognition [GO:0050890]; developmental growth [GO:0048589]; energy reserve metabolic process [GO:0006112]; hair follicle placode formation [GO:0060789]; intracellular transport [GO:0046907]; platelet aggregation [GO:0070527]; positive regulation of cAMP biosynthetic process [GO:0030819]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of GTPase activity [GO:0043547]; regulation of insulin secretion [GO:0050796]; renal water homeostasis [GO:0003091]; sensory perception of chemical stimulus [GO:0007606]; sensory perception of smell [GO:0007608]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; water transport [GO:0006833]adenylate cyclase activity [GO:0004016]; beta-2 adrenergic receptor binding [GO:0031698]; corticotropin-releasing hormone receptor 1 binding [GO:0051430]; D1 dopamine receptor binding [GO:0031748]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; insulin-like growth factor receptor binding [GO:0005159]; ionotropic glutamate receptor binding [GO:0035255]; metal ion binding [GO:0046872]; mu-type opioid receptor binding [GO:0031852]; signal transducer activity [GO:0004871] cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; intrinsic component of membrane [GO:0031224]; membrane [GO:0016020]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]lFUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. Stimulates the Ras signaling pathway via RAPGEF2. {ECO:0000269|PubMed:12391161}.Q14C86GAPD1>GTPase-activating protein and VPS9 domain-containing protein 1SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16410077}; Peripheral membrane protein {ECO:0000269|PubMed:16410077}. Endosome {ECO:0000269|PubMed:16410077}. Note=Recruited to the plasma membrane by TRIP10/CIP4 in response to insulin.endocytosis [GO:0006897]; positive regulation of GTPase activity [GO:0043547]; regulation of protein transport [GO:0051223]; signal transduction [GO:0007165]GTPase activating protein binding [GO:0032794]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]Bcytosol [GO:0005829]; endosome [GO:0005768]; membrane [GO:0016020]FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras. {ECO:0000269|PubMed:16410077}.Q9HAB3S52A2:Solute carrier family 52, riboflavin transporter, member 2}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20463145}; Multi-pass membrane protein {ECO:0000269|PubMed:20463145}.!riboflavin transport [GO:0032218]Rriboflavin transporter activity [GO:0032217]; virus receptor activity [GO:0001618]2integral component of plasma membrane [GO:0005887]FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)-independent but moderately pH-sensitive. Activity is strongly inhibited by riboflavin analogs, such as lumiflavin. Weakly inhibited by flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). In case of infection by retroviruses, acts as a cell receptor to retroviral envelopes similar to the porcine endogenous retrovirus (PERV-A). {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:19307586, ECO:0000269|PubMed:20463145}.Q6P3W7SCYL2SCY1-like protein 2SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network membrane. Endosome membrane. Note=According to PubMed:15809293, plasma membrane-associated in clathrin-coated vesicles. According to PubMed:16914521, colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes.Dendosome to lysosome transport [GO:0008333]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of clathrin-mediated endocytosis [GO:2000370]; positive regulation of receptor internalization [GO:0002092]; receptor internalization involved in canonical Wnt signaling pathway [GO:2000286]]ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; receptor binding [GO:0005102]clathrin-coated vesicle [GO:0030136]; endosome membrane [GO:0010008]; Gol< gi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]+FUNCTION: Component of AP2-containing clathrin coated structures at the plasma membrane or of endocytic coated vesicles. According to PubMed:15809293, probable serine/threonine-protein kinase that phosphorylates, in vitro, the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine. According to PubMed:16914521, has no detectable kinase activity in vitro. May regulate clathrin-dependent trafficking between the TGN and/or the endosomal system. {ECO:0000269|PubMed:15809293, ECO:0000269|PubMed:16914521}.Q12981SEC20Vesicle transport protein SEC20jSUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.&apoptotic process [GO:0006915]; autophagy [GO:0006914]; endoplasmic reticulum membrane fusion [GO:0016320]; endoplasmic reticulum organization [GO:0007029]; execution phase of apoptosis [GO:0097194]; negative regulation of apoptotic process [GO:0043066]; vesicle-mediated transport [GO:0016192]#SNAP receptor activity [GO:0005484] cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; integral component of endoplasmic reticulum membrane [GO:0030176]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; SNARE complex [GO:0031201]5FUNCTION: SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. Required for maintenance of ER network. Implicated in the suppression of cell death. May be involved in mitochondrial autophagy. {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:21931693}.Q9H0W5CCDC8'Coiled-coil domain-containing protein 8SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24793695}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24793695}.microtubule cytoskeleton organization [GO:0000226]; negative regulation of phosphatase activity [GO:0010923]; regulation of mitotic nuclear division [GO:0007088]f3M complex [GO:1990393]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Required for localization of CUL7 to the centrosome (PubMed:24793695). {ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.Q96C24SYTL4Synaptotagmin-like protein 4SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles (By similarity). {ECO:0000250}.calcium ion-dependent exocytosis of neurotransmitter [GO:0048791]; intracellular protein transport [GO:0006886]; multivesicular body sorting pathway [GO:0071985]; negative regulation of insulin secretion [GO:0046676]; positive regulation of exocytosis [GO:0045921]; positive regulation of protein secretion [GO:0050714]; regulation of calcium ion-dependent exocytosis [GO:0017158]; synaptic vesicle exocytosis [GO:0016079]calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; clathrin binding [GO:0030276]; neurexin family protein binding [GO:0042043]; phospholipid binding [GO:0005543]; syntaxin binding [GO:0019905]; zinc ion binding [GO:0008270]Bapical plasma membrane [GO:0016324]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; endosome [GO:0005768]; exocytic vesicle [GO:0070382]; extrinsic component of membrane [GO:0019898]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; transport vesicle membrane [GO:0030658]FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). {ECO:0000250}.P12277KCRBCreatine kinase B-typecellular chloride ion homeostasis [GO:0030644]; cellular nitrogen compound metabolic process [GO:0034641]; creatine metabolic process [GO:0006600]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]nATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; ubiquitin protein ligase binding [GO:0031625]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]'FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.Q9NY61AATF Protein AATFapoptotic signaling pathway [GO:0097190]; cell adhesion [GO:0007155]; cellular response to DNA damage stimulus [GO:0006974]; embryonic cleavage [GO:0040016]; negative regulation of amyloid precursor protein biosynthetic process [GO:0042985]; negative regulation of apoptotic process [GO:0043066]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of superoxide anion generation [GO:0032929]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of mitotic cell cycle [GO:0007346]; ribosome biogenesis [GO:0042254]leucine zipper domain binding [GO:0043522]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]centrosome [GO:0005813]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date. {ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:12847090, ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15207272}.Q9NPL8TIDC10Complex I assembly factor TIMMDC1, mitochondrialSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:24191001}; Multi-pass membrane protein {ECO:0000269|PubMed:24191001}.integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Chaperone protein involved in the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Participates in constructing the membrane arm of complex I. {ECO:0000269|PubMed:24191001}.Q9H0E3SP130*Histone deacetylase complex subunit SAP130<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15561718}.]chromatin organization [GO:0006325]; gene expression [GO:0010467]; histone H3 acetylation [GO:0043966]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]4nucleoplasm [GO:0005654]; STAGA complex [GO:0030914]FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions< between the complex and other regulatory complexes. {ECO:0000269|PubMed:12724404}.Q9UIJ7KAD3-GTP:AMP phosphotransferase AK3, mitochondrialjSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:11485571}.ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; blood coagulation [GO:0007596]; GTP metabolic process [GO:0046039]; ITP metabolic process [GO:0046041]; UTP metabolic process [GO:0046051]rATP binding [GO:0005524]; GTP binding [GO:0005525]; nucleoside triphosphate adenylate kinase activity [GO:0046899]FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:11485571}.P29218IMPA1Inositol monophosphatase 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17068342}.inositol biosynthetic process [GO:0006021]; inositol phosphate dephosphorylation [GO:0046855]; inositol phosphate metabolic process [GO:0043647]; phosphate-containing compound metabolic process [GO:0006796]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]identical protein binding [GO:0042802]; inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; inositol monophosphate phosphatase activity [GO:0052834]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]PFUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. {ECO:0000269|PubMed:17068342, ECO:0000269|PubMed:8718889, ECO:0000269|PubMed:9462881}.Q96DG6CMBL$Carboxymethylenebutenolidase homologGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20177059}.hydrolase activity [GO:0016787]-FUNCTION: Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. {ECO:0000269|PubMed:20177059}.P26374RAE24Rab proteins geranylgeranyltransferase component A 2GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12356470}.Vintracellular protein transport [GO:0006886]; protein geranylgeranylation [GO:0018344]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; Rab-protein geranylgeranyltransferase complex [GO:0005968]FUNCTION: Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Less effective than CHM in supporting prenylation of Rab3 family. {ECO:0000269|PubMed:12356470, ECO:0000269|PubMed:15186776, ECO:0000269|PubMed:8294464}.Q86VP6CAND1-Cullin-associated NEDD8-dissociated protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21249194}. Nucleus {ECO:0000269|PubMed:21249194}. Note=Predominantly cytoplasmic.cell differentiation [GO:0030154]; negative regulation of catalytic activity [GO:0043086]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; protein ubiquitination [GO:0016567]; SCF complex assembly [GO:0010265]cullin-RING ubiquitin ligase complex [GO:0031461]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes. {ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}.Q9UL40ZN346Zinc finger protein 346SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15254228}. Cytoplasm {ECO:0000269|PubMed:15254228}. Note=Nuclear at steady state, primarily in the nucleolus. Shuttles between the nucleus and cytoplasm when associated with XPO5.5positive regulation of apoptotic process [GO:0043065]double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high affinity to dsRNA, with no detectable sequence specificity. {ECO:0000269|PubMed:24521053}.Q99543DNJC2!DnaJ homolog subfamily C member 22SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol.de novo' cotranslational protein folding [GO:0051083]; cellular response to heat [GO:0034605]; chromatin modification [GO:0016568]; DNA replication [GO:0006260]; negative regulation of DNA biosynthetic process [GO:2000279]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of cellular response to heat [GO:1900034]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone binding [GO:0042393]; Hsp70 protein binding [GO:0030544]; poly(A) RNA binding [GO:0044822]; ubiquitin binding [GO:0043130]{cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]gFUNCTION: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'. {ECO:0000269|PubMed:15802566, ECO:0000269|PubMed:16002468, ECO:0000269|PubMed:21179169}.P23458JAK1Tyrosine-protein kinase JAK1SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Wholly intracellular, possibly membrane associated.cell differentiation [GO:0030154]; cell migration [GO:0016477]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; interleukin-2-mediated signaling pathway [GO:0038110]; intracellular signal transduction [GO:0035556]; peptidyl-tyrosine autophosphorylation [GO:0038083]; protein phosphorylation [GO:0006468]; regulation of cell proliferation [GO:0042127]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of type < I interferon-mediated signaling pathway [GO:0060338]; response to antibiotic [GO:0046677]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; type I interferon signaling pathway [GO:0060337]ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; nucleus [GO:0005634]FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. {ECO:0000269|PubMed:11909529}.O95810SDPR"Serum deprivation-response proteindSUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane, caveola. Note=Colocalizes with CAV1 to caveolae.qphosphatidylserine binding [GO:0001786]; phospholipid binding [GO:0005543]; protein kinase C binding [GO:0005080]^caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]YFUNCTION: May play a role in targeting PRKCA to caveolae. {ECO:0000250|UniProtKB:Q66H98}.Q15050RRS1.Ribosome biogenesis regulatory protein homologZSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|Ref.3}.yendonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; hematopoietic progenitor cell differentiation [GO:0002244]; mitotic metaphase plate congression [GO:0007080]; ribosomal large subunit biogenesis [GO:0042273]; ribosomal large subunit export from nucleus [GO:0000055]condensed nuclear chromosome [GO:0000794]; endoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]; nucleus [GO:0005634]; preribosome, large subunit precursor [GO:0030687]9FUNCTION: Involved in ribosome biogenesis. {ECO:0000250}.P51805PLXA3 Plexin-A3Esignaling molecule(PC00207);tyrosine protein kinase receptor(PC00233)eSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.faxon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; facial nerve structural organization [GO:0021612]; hippocampus development [GO:0021766]; multicellular organismal development [GO:0007275]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; positive regulation of cytoskeleton organization [GO:0051495]; pyramidal neuron development [GO:0021860]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; trigeminal nerve structural organization [GO:0021637]asemaphorin receptor activity [GO:0017154]; transmembrane signaling receptor activity [GO:0004888]integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine morphology in pyramidal neurons. May play a role in regulating semaphorin-mediated programmed cell death in the developing nervous system. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.Q96T88UHRF1!E3 ubiquitin-protein ligase UHRF1JSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21777816}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.?cell cycle [GO:0007049]; cell proliferation [GO:0008283]; DNA methylation on cytosine [GO:0032776]; DNA repair [GO:0006281]; gene expression [GO:0010467]; histone monoubiquitination [GO:0010390]; histone ubiquitination [GO:0016574]; maintenance of DNA methylation [GO:0010216]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity [GO:2000373]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein autoubiquitination [GO:0051865]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]core promoter proximal region sequence-specific DNA binding [GO:0000987]; hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; ligase activity [GO:0016874]; methylated histone binding [GO:0035064]; methyl-CpG binding [GO:0008327]; nucleosomal histone binding [GO:0031493]; sequence-specific DNA binding transcription factor activity [GO:0003700]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nuclear chromatin [GO:0000790]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; replication fork [GO:0005657]FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. {ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:15009091, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:22945642}.P20594ANPRB%Atrial natriuretic peptide receptor 2Lbone development [GO:0060348]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cGMP biosynthetic process [GO:0006182]; intracellular signal transduction [GO:0035556]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of oocyte maturation [GO:1900194]; ossification [GO:0001503]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; signal transduction [GO:0007165]; single organism reproductive process [GO:0044702]QATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; hormone binding [GO:0042562]; natriuretic peptide receptor activity [GO:0016941]; peptide hormone binding [GO:0017046]; protein kinase activity [GO:0004672]; receptor activity [GO:000< 4872]; transmembrane signaling receptor activity [GO:0004888]eintegral component of membrane [GO:0016021]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. {ECO:0000269|PubMed:15146390, ECO:0000269|PubMed:1672777}.P98082DAB2Disabled homolog 26SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm.2apoptotic process [GO:0006915]; cell proliferation [GO:0008283]; leading edge cell differentiation [GO:0035026]; membrane organization [GO:0061024]; multicellular organismal development [GO:0007275]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of protein binding [GO:0032091]; negative regulation of protein localization to plasma membrane [GO:1903077]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cell migration [GO:0030335]; positive regulation of clathrin-mediated endocytosis [GO:2000370]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of endocytosis [GO:0045807]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of SMAD protein import into nucleus [GO:0060391]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; Wnt signaling pathway [GO:0016055]cargo receptor activity [GO:0038024]; clathrin adaptor activity [GO:0035615]; protein C-terminus binding [GO:0008022]; SMAD binding [GO:0046332];clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; coated pit [GO:0005905]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]} FUNCTION: Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containg non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. {ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:16267015, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19306879, ECO:0000269|PubMed:21995445, ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22491013}.Q5J8M3EMC4%ER membrane protein complex subunit 4.FUNCTION: May mediate anti-apoptotic activity.Q4V328GRAP1GRIP1-associated protein 1CSUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:15897011}.=blood microparticle [GO:0072562]; early endosome [GO:0005769]Q5SSJ5HP1B3+Heterochromatin protein 1-binding protein 3iSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24830416}. Chromosome {ECO:0000269|PubMed:20042602, ECO:0000269|PubMed:24830416}. Note=localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S). {ECO:0000269|PubMed:24830416}.cellular response to hypoxia [GO:0071456]; heterochromatin organization [GO:0070828]; nucleosome assembly [GO:0006334]; regulation of cell proliferation [GO:0042127]; regulation of nucleus size [GO:0097298]; regulation of transcription, DNA-templated [GO:0006355]9DNA binding [GO:0003677]; nucleosome binding [GO:0031491]Fchromosome [GO:0005694]; nucleosome [GO:0000786]; nucleus [GO:0005634]FUNCTION: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity (PubMed:24830416). Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self-renewal(PubMed:25100860). {ECO:0000269|PubMed:24830416, ECO:0000269|PubMed:25100860}.Q14678KANK17KN motif and ankyrin repeat domain-containing protein 1SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000269|PubMed:12133830, ECO:0000269|PubMed:16968744}. Note=Colocalizes with KIF21A in membrane ruffles.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Cell projection, ruffle membrane. Note=Shuttles between the cytoplasm and nucleus.Znegative regulation of actin filament polymerization [GO:0030837]; negative regulation of cell migration [GO:0030336]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of lamellipodium morphogenesis [GO:2000393]; negative regulation of neuron projection development [GO:0010977]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of ruffle assembly [GO:1900028]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; positive regulation of catenin import into nucleus [GO:0035413]; positive regulation of Wnt signaling pathway [GO:0030177]; positive regulation of wound healing < [GO:0090303]; regulation of establishment of cell polarity [GO:2000114]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]!beta-catenin binding [GO:0008013]Jcytoplasm [GO:0005737]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]FUNCTION: Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma. {ECO:0000269|PubMed:16968744, ECO:0000269|PubMed:18458160, ECO:0000269|PubMed:19171758, ECO:0000269|PubMed:22084092}.Q96RF0SNX18Sorting nexin-186SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Partially colocalized with clathrin and dynamin at the cell membrane. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation.1cleavage furrow formation [GO:0036089]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; intracellular protein transport [GO:0006886]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0007067]; positive regulation of GTPase activity [GO:0043547]; vesicle organization [GO:0016050]:phosphatidylinositol-4,5-bisphosphate binding [GO:0005546];cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle membrane [GO:0030659]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]FUNCTION: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Stimulates the GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane. {ECO:0000269|PubMed:18411244, ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350}.P63244GBLP8Guanine nucleotide-binding protein subunit beta-2-like 1SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Nucleus. Perikaryon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, phagocytic cup. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery. In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei. Localized to phagocytic cups following infection by Y.pestis.uactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; cell cycle [GO:0007049]; cellular response to glucose stimulus [GO:0071333]; gastrulation [GO:0007369]; negative regulation of cell growth [GO:0030308]; negative regulation of endoplasmic reticulum unfolded protein response [GO:1900102]; negative regulation of gene expression [GO:0010629]; negative regulation of hydrogen peroxide-induced neuron death [GO:1903208]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of phagocytosis [GO:0050765]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of protein tyrosine kinase activity [GO:0061099]; negative regulation of translation [GO:0017148]; negative regulation of Wnt signaling pathway [GO:0030178]; osteoblast differentiation [GO:0001649]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cAMP catabolic process [GO:0030822]; positive regulation of cell migration [GO:0030335]; positive regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051343]; positive regulation of gastrulation [GO:2000543]; positive regulation of GTPase activity [GO:0043547]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein homooligomerization [GO:0032464]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell cycle [GO:0051726]; regulation of cell division [GO:0051302]; regulation of establishment of cell polarity [GO:2000114]; regulation of establishment of protein localization to plasma membrane [GO:0090003]; regulation of protein localization [GO:0032880]; rhythmic process [GO:0048511]; viral process [GO:0016032]>cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; poly(A) RNA binding [GO:0044822]; protein complex scaffold [GO:0032947]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase inhibitor activity [GO:0030292]; receptor binding [GO:0005102]; receptor tyrosine kinase binding [GO:0030971]; SH2 domain binding [GO:0042169]; signaling adaptor activity [GO:0035591]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; IRE1-RACK1-PP2A complex [GO:1990630]; midbody [GO:0030496]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; small ribosomal subunit [GO:0015935] FUNCTION: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellula< r polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA. {ECO:0000269|PubMed:11312657, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:9584165}.P56715RP1Oxygen-regulated protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:11773008}. Note=Specifically localized in the connecting cilia of rod and cone photoreceptors.axoneme assembly [GO:0035082]; cellular response to light stimulus [GO:0071482]; intracellular signal transduction [GO:0035556]; photoreceptor cell development [GO:0042461]; photoreceptor cell maintenance [GO:0045494]; photoreceptor cell outer segment organization [GO:0035845]; phototransduction, visible light [GO:0007603]; retina development in camera-type eye [GO:0060041]; retinal cone cell development [GO:0046549]; retinal rod cell development [GO:0046548]; visual perception [GO:0007601] microtubule binding [GO:0008017]axoneme [GO:0005930]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; photoreceptor connecting cilium [GO:0032391]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]FUNCTION: Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme (By similarity). {ECO:0000250}.Q8NFC6BD1L1>Biorientation of chromosomes in cell division protein 1-like 1P41250SYGGlycine--tRNA ligaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9524218}. Mitochondrion {ECO:0000269|PubMed:9524218}. Cell projection, axon {ECO:0000269|PubMed:17035524, ECO:0000269|PubMed:25168514}. Note=Associated with granules in cultured neuron cells. {ECO:0000269|PubMed:17035524}.diadenosine tetraphosphate biosynthetic process [GO:0015966]; gene expression [GO:0010467]; glycyl-tRNA aminoacylation [GO:0006426]; tRNA aminoacylation for protein translation [GO:0006418]oATP binding [GO:0005524]; glycine-tRNA ligase activity [GO:0004820]; protein dimerization activity [GO:0046983]axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; secretory granule [GO:0030141]!FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. {ECO:0000269|PubMed:17544401, ECO:0000269|PubMed:19710017}.Q14978NOLC1*Nucleolar and coiled-body phosphoprotein 1SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase.cell cycle [GO:0007049]; mitotic nuclear division [GO:0007067]; nucleolus organization [GO:0007000]; rRNA processing [GO:0006364]TATP binding [GO:0005524]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]aCajal body [GO:0015030]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]'FUNCTION: Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I.O43823AKAP8A-kinase anchor protein 8SUBCELLULAR LOCATION: Nucleus matrix. Note=Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis.Gmitotic nuclear division [GO:0007067]; signal transduction [GO:0007165]double-stranded DNA binding [GO:0003690]; poly(A) RNA binding [GO:0044822]; protein kinase A regulatory subunit binding [GO:0034237]; zinc ion binding [GO:0008270]female pronucleus [GO:0001939]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]zFUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II).Q9BQ51PD1L2 Programmed cell death 1 ligand 2SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Endomembrane system; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.=immune response [GO:0006955]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of interleukin-10 production [GO:0032693]; positive regulation of T cell proliferation [GO:0042102]; T cell costimulation [GO:0031295]endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity). {ECO:0000250}.P52907CAZA1'F-actin-capping protein subunit alpha-1actin binding [GO:0003779]<actin cytoskeleton [GO:0015629]; cell-cell junction [GO:0005911]; cortical cytoskeleton [GO:0030863]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; F-actin capping protein complex [GO:0008290]; membrane [GO:0016020]; WASH complex [GO:0071203]Q53H82LACB2Beta-lactamase-like protein 2?hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]P0DI81TPC2A.Trafficking protein particle complex subunit 2SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic reticulum. Golgi apparatus. Nucleus. Note=Localized in perinuclear granular structures.ER to Golgi vesicle-mediated transport [GO:0006888]; regulation of transcription, DNA-templated [GO:0006355]; skeletal system development [GO:0001501]; transcription, DNA-templated [GO:0006351]Kion channel binding [GO:0044325]; transcription factor binding [GO:0008134]endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Prevents transcriptional repression and induction of cell death by ENO1 (By similarity). May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.Q58G82SY14L&Putative synaptotagmin-14-like proteinpositive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of dendrite extension [GO:1903861]; positive regulation of E< RK1 and ERK2 cascade [GO:0070374]Q53FP2TMM35Transmembrane protein 35SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Shedding may lead to a soluble peptide. {ECO:0000250}.cytoplasmic membrane-bounded vesicle [GO:0016023]; integral component of membrane [GO:0016021]; peroxisomal membrane [GO:0005778]vFUNCTION: A soluble peptide released by shedding may interact with NGFR and modulate neurite outgrowth. {ECO:0000250}.Q08722CD47Leukocyte surface antigen CD47{SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7691831}; Multi-pass membrane protein {ECO:0000269|PubMed:7691831}.blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; opsonization [GO:0008228]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of cell proliferation [GO:0008284]; positive regulation of inflammatory response [GO:0050729]; positive regulation of phagocytosis [GO:0050766]; positive regulation of T cell activation [GO:0050870]; response to bacterium [GO:0009617][FUNCTION: Has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells. May be involved in membrane permeability changes induced following virus infection. {ECO:0000250, ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453, ECO:0000269|PubMed:7691831}.Q5VZ66JKIP32Janus kinase and microtubule-interacting protein 34SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.O75665OFD1&Oral-facial-digital syndrome 1 proteinHSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Note=Localizes to centriole distal ends and to centriolar satellites. {ECO:0000250}.axoneme assembly [GO:0035082]; cilium morphogenesis [GO:0060271]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]Falpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]FUNCTION: Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164. Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis. Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250}.Q969U7PSMG2Proteasome assembly chaperone 2=SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9EST4}.mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of apoptotic process [GO:0043066]; proteasome assembly [GO:0043248]vFUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.Q9HBA0TRPV4@Transient receptor potential cation channel subfamily V member 4SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:18826956}; Multi-pass membrane protein. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9EPK8}. Cell projection, cilium {ECO:0000269|PubMed:18695040}. Note=Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum. {ECO:0000269|PubMed:16293632, ECO:0000269|PubMed:20037587, ECO:0000269|PubMed:20037588}.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane.+actin cytoskeleton reorganization [GO:0031532]; actin filament organization [GO:0007015]; calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cell-cell junction assembly [GO:0007043]; cellular calcium ion homeostasis [GO:0006874]; cellular hypotonic response [GO:0071476]; cellular response to heat [GO:0034605]; cellular response to osmotic stress [GO:0071470]; cell volume homeostasis [GO:0006884]; cortical microtubule organization [GO:0043622]; hyperosmotic salinity response [GO:0042538]; ion transmembrane transport [GO:0034220]; microtubule polymerization [GO:0046785]; negative regulation of neuron projection development [GO:0010977]; osmosensory signaling pathway [GO:0007231]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of microtubule depolymerization [GO:0031117]; regulation of response to osmotic stress [GO:0047484]; response to mechanical stimulus [GO:0009612]; transmembrane transport [GO:0055085]; vasopressin secretion [GO:0030103]actin binding [GO:0003779]; actin filament binding [GO:0051015]; alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; calcium channel activity [GO:0005262]; calmodulin binding [GO:0005516]; cation channel activity [GO:0005261]; microtubule binding [GO:0008017]; osmosensor activity [GO:0005034]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; SH2 domain binding [GO:0042169]adherens junction [GO:0005912]; cell surface [GO:0009986]; cilium [GO:0005929]; cortical actin cytoskeleton [GO:0030864]; cytoplasmic microtubule [GO:0005881]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; integral component of membrane [GO:0016021]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]rFUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:18826956, PubMed:18695040). Also activated by heat, low pH, citrate and phorbol esters (PubMed:18826956, PubMed:18695040). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (PubMed:12724311, PubMed:18826956). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (PubMed:19759329). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (PubMed:19759329). Together with PKD2, forms mechano- and thermosensitive channels in cilium (Pub< Med:18695040). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9EPK8, ECO:0000269|PubMed:11025659, ECO:0000269|PubMed:12724311, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:19759329}.Q96LL9DJC30"DnaJ homolog subfamily C member 30P42226STAT62Signal transducer and activator of transcription 6lSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the nucleus in response to phosphorylation. innate immune response [GO:0045087]; interleukin-4-mediated signaling pathway [GO:0035771]; mammary gland epithelial cell proliferation [GO:0033598]; mammary gland morphogenesis [GO:0060443]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of type 2 immune response [GO:0002829]; positive regulation of isotype switching to IgE isotypes [GO:0048295]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of cell proliferation [GO:0042127]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; T-helper 1 cell lineage commitment [GO:0002296]; transcription, DNA-templated [GO:0006351]identical protein binding [GO:0042802]; protein phosphatase binding [GO:0019903]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]fcytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling. {ECO:0000269|PubMed:17210636}.P62834RAP1ARas-related protein Rap-1ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11359771}; Lipid-anchor {ECO:0000269|PubMed:11359771}. Cytoplasm {ECO:0000269|PubMed:11359771}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359771}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions (By similarity). Colocalized with RAPGEF2 in the perinuclear region. {ECO:0000250}.activation of MAPKK activity [GO:0000186]; blood coagulation [GO:0007596]; cellular response to cAMP [GO:0071320]; cellular response to nerve growth factor stimulus [GO:1990090]; energy reserve metabolic process [GO:0006112]; establishment of endothelial barrier [GO:0061028]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; nerve growth factor signaling pathway [GO:0038180]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of vasculogenesis [GO:2001214]; protein transport [GO:0015031]; Rap protein signal transduction [GO:0032486]; regulation of cell junction assembly [GO:1901888]; regulation of insulin secretion [GO:0050796]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; protein complex binding [GO:0032403]; protein transporter activity [GO:0008565]; Rap guanyl-nucleotide exchange factor activity [GO:0017034]ecell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; guanyl-nucleotide exchange factor complex [GO:0032045]; late endosome [GO:0005770]; myelin sheath [GO:0043209]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions. {ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:21840392}.Q96Q45TM237Transmembrane protein 2377SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:22152675}. Note=Localizes at the proximal region of primary cilia were observed, consistent with localization to the transition zone. Anchored to the transition zone by RPGRIP1L.Ncilium assembly [GO:0042384]; regulation of Wnt signaling pathway [GO:0030111]hciliary transition zone [GO:0035869]; integral component of membrane [GO:0016021]; membrane [GO:0016020]vFUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis. {ECO:0000269|PubMed:22152675}.Q86VP3PACS2-Phosphofurin acidic cluster sorting protein 2}SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15692567}. Mitochondrion {ECO:0000269|PubMed:15692567}.apoptotic process [GO:0006915]; autophagosome assembly [GO:0000045]; protein localization to pre-autophagosomal structure [GO:0034497]; protein targeting to plasma membrane [GO:0072661]; viral process [GO:0016032]hendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; mitochondrion [GO:0005739]FUNCTION: Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. {ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:15692567}.Q9P000COMD9 COMM domain-containing protein 9oSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21778237}. Cytoplasmic vesicle {ECO:0000269|PubMed:21778237}.Gcytoplasmic membrane-bounded vesicle [GO:0016023]; nucleus [GO:0005634]P35241RADIRadixinSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.Oactin filament capping [GO:0051693]; apical protein localization [GO:0045176]; cellular response to thyroid hormone stimulus [GO:0097067]; establishment of endothelial barrier [GO:0061028]; establishment of protein localization [GO:0045184]; establishment of protein localization to plasma membrane [GO:0090002]; microvillus assembly [GO:0030033]; negative regulation of adherens junction organization [GO:1903392]; negative regulation of cell size [GO:0045792]; negative regulation of GTPase activity [GO:0034260]; negative regulation of homotypic cell-cell adhesion [GO:0034111]; positive regulation of cell migration [GO:0030335]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of G1/S transition of mitotic cell cyc< le [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of protein localization to early endosome [GO:1902966]; protein kinase A signaling [GO:0010737]; regulation of actin filament bundle assembly [GO:0032231]; regulation of cell shape [GO:0008360]; regulation of cell size [GO:0008361]; regulation of GTPase activity [GO:0043087]; regulation of organelle assembly [GO:1902115]; regulation of Rap protein signal transduction [GO:0032487]; regulation of ruffle assembly [GO:1900027]actin binding [GO:0003779]; ATPase binding [GO:0051117]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; protein kinase A binding [GO:0051018]apical plasma membrane [GO:0016324]; cell periphery [GO:0071944]; cleavage furrow [GO:0032154]; cortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of membrane [GO:0019898]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; stereocilium [GO:0032420]sFUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.Q92574TSC1HamartinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9809973}. Membrane {ECO:0000269|PubMed:9809973}; Peripheral membrane protein {ECO:0000269|PubMed:9809973}. Note=At steady state found in association with membranes.activation of GTPase activity [GO:0090630]; cardiac muscle cell differentiation [GO:0055007]; cell cycle arrest [GO:0007050]; cell-matrix adhesion [GO:0007160]; cell projection organization [GO:0030030]; cerebral cortex development [GO:0021987]; gene expression [GO:0010467]; glucose import [GO:0046323]; hippocampus development [GO:0021766]; insulin receptor signaling pathway [GO:0008286]; kidney development [GO:0001822]; myelination [GO:0042552]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cell size [GO:0045792]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of TOR signaling [GO:0032007]; negative regulation of translation [GO:0017148]; neural tube closure [GO:0001843]; positive regulation of focal adhesion assembly [GO:0051894]; potassium ion transport [GO:0006813]; protein heterooligomerization [GO:0051291]; protein stabilization [GO:0050821]; regulation of cell cycle [GO:0051726]; regulation of cell-matrix adhesion [GO:0001952]; regulation of phosphoprotein phosphatase activity [GO:0043666]; regulation of protein kinase activity [GO:0045859]; regulation of stress fiber assembly [GO:0051492]; regulation of translation [GO:0006417]; response to insulin [GO:0032868]; rRNA export from nucleus [GO:0006407]; synapse organization [GO:0050808]; transcription initiation from RNA polymerase II promoter [GO:0006367]ochaperone binding [GO:0051087]; GTPase regulator activity [GO:0030695]; protein N-terminus binding [GO:0047485]Acell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; growth cone [GO:0030426]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; TSC1-TSC2 complex [GO:0033596]FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. {ECO:0000269|PubMed:12271141, ECO:0000269|PubMed:15340059}.P16333NCK1Cytoplasmic protein NCK1NCK=SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments.actin filament organization [GO:0007015]; axon guidance [GO:0007411]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; lamellipodium assembly [GO:0030032]; negative regulation of cell death [GO:0060548]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress [GO:1990441]; peptidyl-serine dephosphorylation [GO:0070262]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cap-dependent translational initiation [GO:1903676]; positive regulation of cap-independent translational initiation [GO:1903679]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; response to other organism [GO:0051707]; signal complex assembly [GO:0007172]; small GTPase mediated signal transduction [GO:0007264]; substrate-dependent cell migration, cell extension [GO:0006930]; T cell activation [GO:0042110]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]jcytoskeletal adaptor activity [GO:0008093]; eukaryotic initiation factor eIF2 binding [GO:0071074]; protein binding, bridging [GO:0030674]; protein kinase inhibitor activity [GO:0004860]; receptor binding [GO:0005102]; receptor signaling complex scaffold activity [GO:0030159]; receptor tyrosine kinase binding [GO:0030971]; SH3/SH2 adaptor activity [GO:0005070] cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase type 1 complex [GO:0000164]; ribosome [GO:0005840]; vesicle membrane [GO:0012506]2FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:23358419, ECO:0000269|PubMed:9430661}.Q9H0D6XRN25'-3' exoribonuclease 2cell growth [GO:0016049]; DNA catabolic process, exonucleolytic [GO:0000738]; DNA-templated transcription, termination [GO:0006353]; mRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]; RNA catabolic process [GO:0006401]; RNA metabolic process [GO:0016070]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; RNA processing [GO:0006396]; spermatogenesis [GO:0007283]5'-3' exonuclease activity [GO:0008409]; 5'-3' exoribonuclease activity [GO:0004534]; nuclease activity [GO:0004518]; poly(A) RNA binding [GO:0044822]; transcription termination site sequence-specific DNA binding [GO:0001147]; zinc ion binding [GO:0008270][aggresome [GO:0016235]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Possesses 5'->3' exoribonuclease activity (By similarity). May pro< mote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (PubMed:21700224). {ECO:0000250, ECO:0000269|PubMed:15565158, ECO:0000269|PubMed:16648491, ECO:0000269|PubMed:21700224}.Q01968OCRL+Inositol polyphosphate 5-phosphatase OCRL-1LSUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250}. Early endosome membrane. Membrane, clathrin-coated pit. Cell projection, cilium, photoreceptor outer segment. Cytoplasmic vesicle {ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Also found on macropinosomes.Jcilium assembly [GO:0042384]; inositol phosphate metabolic process [GO:0043647]; in utero embryonic development [GO:0001701]; lipid metabolic process [GO:0006629]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; positive regulation of GTPase activity [GO:0043547]; regulation of GTPase activity [GO:0043087]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]GTPase activator activity [GO:0005096]; inositol phosphate phosphatase activity [GO:0052745]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; Rac GTPase binding [GO:0048365]clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; Golgi-associated vesicle [GO:0005798]; Golgi stack [GO:0005795]; nucleus [GO:0005634]; phagocytic vesicle membrane [GO:0030670]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes. Involved in primary cilia assembly. {ECO:0000269|PubMed:22228094, ECO:0000269|PubMed:22543976}.O15083ERC2 ERC protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923177}. Cell junction, synapse {ECO:0000269|PubMed:12923177}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:12923177}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12923177}. Note=In neurons, localized to synapses, and colocalizes with PCLO. Localized to the active zone of presynaptic density (By similarity). {ECO:0000250}.cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; growth cone [GO:0030426]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]FUNCTION: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.P49411EFTU#Elongation factor Tu, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; organelle organization [GO:0006996]; translational elongation [GO:0006414]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; translation elongation factor activity [GO:0003746]zextracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.Q8IYS2K2013 Uncharacterized protein KIAA2013Q8N4C8MINK1Misshapen-like kinase 14SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15469942, ECO:0000269|PubMed:18930710}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 4: Golgi apparatus.actin cytoskeleton reorganization [GO:0031532]; activation of protein kinase activity [GO:0032147]; dendrite morphogenesis [GO:0048813]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; multicellular organismal development [GO:0007275]; negative thymic T cell selection [GO:0045060]; neuron projection morphogenesis [GO:0048812]; positive regulation of JNK cascade [GO:0046330]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity [GO:2000311]; regulation of apoptotic process [GO:0042981]; regulation of cell-cell adhesion [GO:0022407]; regulation of cell-matrix adhesion [GO:0001952]; regulation of cell migration [GO:0030334]; regulation of mitotic cell cycle [GO:0007346]; response to stress [GO:0006950]; synaptic transmission [GO:0007268]axon [GO:0030424]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]1FUNCTION: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking. Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons. Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1.; FUNCTION: Isoform 4 can activate the JNK pathway. Involved in the regulation of actin cytoskeleton reorganization, cell-matrix adhesion, cell-cell adhesion and cell migration.Q8NAB2KBTB30Kelch repeat and BTB domain-containing protein 3P35813PPM1AProtein phosphatase 1ASUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Membrane {ECO:0000250}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250}.cell cycle arrest [GO:0007050]; dephosphorylation [GO:0016311]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of NF-kappaB import into nucleus [GO:0042347]; negative regulation of SMAD protein complex assembly [GO:0010991]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; N-terminal protein myristoylation [GO:0006499]; peptidyl-threonine dephosphorylation [GO:0035970]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of Wnt signaling pathway [GO:0030177]; protein dephosphorylation [GO:0006470]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055]calmodulin-dependent protein phosphatase activity [GO:0033192]; magnesium ion binding [GO:0000287]; manganese ion binding [< GO:0030145]; protein serine/threonine phosphatase activity [GO:0004722]; R-SMAD binding [GO:0070412]; signal transducer activity [GO:0004871]cytosol [GO:0005829]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; voltage-gated calcium channel complex [GO:0005891]FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:18930133}.Q96C90PP14B,Protein phosphatase 1 regulatory subunit 14B*regulation of phosphorylation [GO:0042325]3protein phosphatase inhibitor activity [GO:0004864]~FUNCTION: Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity). {ECO:0000250}.O60493SNX3Sorting nexin-3SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:11433298, ECO:0000269|PubMed:21725319}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:23237080}. Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures (PubMed:21725319) Colocalizes with EEA1 on nascent phagosomes in dendritic cells but competes with EEA1 for binding to phagosomal membrane (PubMed:23237080). In the case of Salmonella enterica infection localizes to Salmonella-containing vacuoles (SCVs) from which SNX3-containing tubules form 30-60 min after infection (PubMed:20482551). {ECO:0000269|PubMed:20482551, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:23237080}.0endocytosis [GO:0006897]; hemoglobin biosynthetic process [GO:0042541]; intralumenal vesicle formation [GO:0070676]; membrane invagination [GO:0010324]; negative regulation of early endosome to late endosome transport [GO:2000642]; negative regulation of phagocytosis [GO:0050765]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein transport [GO:0051224]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of neuron projection development [GO:0010976]; protein to membrane docking [GO:0022615]; regulation of cellular protein metabolic process [GO:0032268]; regulation of intracellular protein transport [GO:0033157]; regulation of Wnt signaling pathway [GO:0030111]; response to bacterium [GO:0009617]; transferrin transport [GO:0033572] phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; protein phosphatase binding [GO:0019903]\clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Also can bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:21725319, PubMed:24344282). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (PubMed:23237080). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor TFRC presumably by delivering the tranferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (By similarity). In the case of Salmonella enterica infection plays arole in maturation of the Salmonella-containing vacuole (SCV) and promotes recruitment of LAMP1 to SCVs (PubMed:20482551). {ECO:0000250|UniProtKB:O70492, ECO:0000269|PubMed:11433298, ECO:0000269|PubMed:18767904, ECO:0000269|PubMed:21725319, ECO:0000269|PubMed:23237080, ECO:0000269|PubMed:24344282, ECO:0000305|PubMed:21725319}.P20042IF2B4Eukaryotic translation initiation factor 2 subunit 21cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; male germ cell proliferation [GO:0002176]; male gonad development [GO:0008584]; translation [GO:0006412]; translational initiation [GO:0006413]; transmembrane transport [GO:0055085]metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]mcytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 2 complex [GO:0005850]1FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.P86791CCZ1$Vacuolar fusion protein CCZ1 homologFSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319}.}intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane-bounded vesicle [GO:0031988]Q10472GALT1/Polypeptide N-acetylgalactosaminyltransferase 1SUBCELLULAR LOCATION: Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted.'cellular protein metabolic process [GO:0044267]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]extracellular region [GO:0005576]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]:FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. {ECO:0000269|PubMed:9295285}.Q969Q5RAB24Ras-related protein Rab-24SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10660536}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Only about 20-25% is recovered in the particulate fraction.rautophagy [GO:0006914]; intracellular protein transport [GO:0006886]; Rab protein signal transduction [GO:0032482]autophagosome [GO:0005776]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; membrane [GO:0016020]; mitochondrion [GO:0005739]HFUNCTION: May be involved in autophagy-related processes. {ECO:0000250}.< Q13045FLIIProtein flightless-1 homologSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes (By similarity). {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; actin filament severing [GO:0051014]; multicellular organismal development [GO:0007275]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]brush border [GO:0005903]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]FUNCTION: May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development (By similarity). May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation. {ECO:0000250, ECO:0000269|PubMed:14966289}.Q66K14TBC9BTBC1 domain family member 9BHcalcium ion binding [GO:0005509]; GTPase activator activity [GO:0005096]P53667LIMK1LIM domain kinase 1TSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly found in the cytoplasm.actin cytoskeleton organization [GO:0030036]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; nervous system development [GO:0007399]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of axon extension [GO:0045773]; positive regulation of stress fiber assembly [GO:0051496]; protein phosphorylation [GO:0006468]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]ATP binding [GO:0005524]; heat shock protein binding [GO:0031072]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]FUNCTION: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1). {ECO:0000269|PubMed:10196227, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:16230460, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:23633677}.Q13217DNJC3!DnaJ homolog subfamily C member 3cellular protein metabolic process [GO:0044267]; defense response to virus [GO:0051607]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; proteolysis involved in cellular protein catabolic process [GO:0051603].protein kinase inhibitor activity [GO:0004860]cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum Sec complex [GO:0031205]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; membrane [GO:0016020]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity. {ECO:0000269|PubMed:12601012, ECO:0000269|PubMed:8576172, ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.Q9NRY4RHG35 Rho GTPase-activating protein 35axon guidance [GO:0007411]; camera-type eye development [GO:0043010]; forebrain development [GO:0030900]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of vascular permeability [GO:0043116]; neural tube closure [GO:0001843]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron projection development [GO:0010976]; regulation of cell shape [GO:0008360]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; GTPase activator activity [GO:0005096]; GTP binding [GO:0005525]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; transcription corepressor activity [GO:0003714]Kactin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor. {ECO:0000269|PubMed:1894621}.Q9NYP7ELOV53Elongation of very long chain fatty acids protein 5<SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:25065913}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000269|PubMed:25065913}.[alpha-linolenic acid metabolic process [GO:0036109]; cellular lipid metabolic process [GO:0044255]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; linoleic acid metabolic process [GO:0043651]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; unsaturated fatty acid biosynthetic process [GO:0006636]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid biosynthetic process [GO:0042761])fatty acid elongase activity [GO:0009922]dendrite [GO:0030425]; dendritic tree [GO:0097447]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; neuronal cell body [GO:0043025]FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. T< his endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:10970790, ECO:0000269|PubMed:20937905}.P49006MRPMARCKS-related proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+)/calmodulin (By similarity). In prostate cancers, detected in the cytoplasm and associated with apical or basal membranes (By similarity). {ECO:0000250}.FUNCTION: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration. When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration. May also affect cancer cell migration. May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity). {ECO:0000250}.Q9NPD3EXOS4Exosome complex component RRP41SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}. Nucleus, nucleolus {ECO:0000269|PubMed:17545563}. Nucleus {ECO:0000269|PubMed:17545563}.tdefense response to virus [GO:0051607]; DNA deamination [GO:0045006]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; histone mRNA catabolic process [GO:0071044]; maturation of 5.8S rRNA [GO:0000460]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; positive regulation of cell growth [GO:0030307]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA 3'-end processing [GO:0031125]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; U4 snRNA 3'-end processing [GO:0034475]Q3'-5'-exoribonuclease activity [GO:0000175]; AU-rich element binding [GO:0017091]cytoplasm [GO:0005737]; cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC4 binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:21255825}.O43665RGS10#Regulator of G-protein signaling 10RGS}positive regulation of GTPase activity [GO:0043547]; termination of G-protein coupled receptor signaling pathway [GO:0038032]FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Associates specifically with the activated forms of the G protein subunits G(i)-alpha and G(z)-alpha but fails to interact with the structurally and functionally distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited by palmitoylation of the G-protein.Q8IVD9NUDC3 NudC domain-containing protein 3Q7KZ85SPT6H$Transcription elongation factor SPT6\chromatin remodeling [GO:0006338]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; negative regulation of histone H3-K27 methylation [GO:0061086]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; regulation of isotype switching [GO:0045191]; regulation of mRNA export from nucleus [GO:0010793]; regulation of mRNA processing [GO:0050684]; regulation of muscle cell differentiation [GO:0051147]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]DNA binding [GO:0003677]; histone binding [GO:0042393]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]cFUNCTION: Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A. {ECO:0000269|PubMed:15060154, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:22316138, ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9514752}.Q5HYK3COQ5?2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191, ECO:0000269|PubMed:25152161}.umethylation [GO:0032259]; small molecule metabolic process [GO:0044281]; ubiquinone biosynthetic process [GO:0006744]FS-adenosylmethionine-dependent methyltransferase activity [GO:0008757]FUNCTION: Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}.< Q9Y3C6PPIL1*Peptidyl-prolyl cis-trans isomerase-like 1}mRNA splicing, via spliceosome [GO:0000398]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]9peptidyl-prolyl cis-trans isomerase activity [GO:0003755]Mcatalytic step 2 spliceosome [GO:0071013]; extracellular exosome [GO:0070062]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing. {ECO:0000269|PubMed:16595688}.Q93096TP4A1'Protein tyrosine phosphatase type IVA 1SUBCELLULAR LOCATION: Cell membrane. Early endosome. Endoplasmic reticulum. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=And mitotic spindle.cell cycle [GO:0007049]; multicellular organismal development [GO:0007275]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of cell migration [GO:0030335]cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; spindle [GO:0005819]}FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. {ECO:0000269|PubMed:12235145, ECO:0000269|PubMed:12782572, ECO:0000269|PubMed:14643450}.Q8TAB3PCD19Protocadherin-19lbrain development [GO:0007420]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]<FUNCTION: Potential calcium-dependent cell-adhesion protein.O15119TBX3T-box transcription factor TBX3ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.anterior/posterior axis specification, embryo [GO:0008595]; atrioventricular bundle cell differentiation [GO:0003167]; blood vessel development [GO:0001568]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cardiac muscle cell fate commitment [GO:0060923]; cell aging [GO:0007569]; cellular senescence [GO:0090398]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; female genitalia development [GO:0030540]; follicle-stimulating hormone secretion [GO:0046884]; forelimb morphogenesis [GO:0035136]; heart looping [GO:0001947]; in utero embryonic development [GO:0001701]; limbic system development [GO:0021761]; luteinizing hormone secretion [GO:0032275]; male genitalia development [GO:0030539]; mammary gland development [GO:0030879]; mammary placode formation [GO:0060596]; mesoderm morphogenesis [GO:0048332]; negative regulation of apoptotic process [GO:0043066]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; organ morphogenesis [GO:0009887]; outflow tract morphogenesis [GO:0003151]; palate development [GO:0060021]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; sinoatrial node cell development [GO:0060931]; skeletal system development [GO:0001501]; specification of organ position [GO:0010159]; stem cell maintenance [GO:0019827]; transcription, DNA-templated [GO:0006351]; ventricular septum morphogenesis [GO:0060412]RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II transcription factor binding [GO:0001085]; sequence-specific DNA binding [GO:0043565]FUNCTION: Transcriptional repressor involved in developmental processes. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. {ECO:0000269|PubMed:10468588, ECO:0000269|PubMed:22002537}.P49750YLPM1YLP motif-containing protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17890166}. Nucleus speckle {ECO:0000250}. Note=Migrates to nucleolar caps upon blockage of transcription.Zregulation of telomere maintenance [GO:0032204]; transcription, DNA-templated [GO:0006351]poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]bcytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation. {ECO:0000250}.P00390GSHR$Glutathione reductase, mitochondrialcell redox homeostasis [GO:0045454]; gene expression [GO:0010467]; glutathione metabolic process [GO:0006749]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; response to reactive oxygen species [GO:0000302]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]electron carrier activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase activity [GO:0004362]; NADP binding [GO:0050661]cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]FFUNCTION: Maintains high levels of reduced glutathione in the cytosol.Q13496MTM1 MyotubularinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:11001925}. Cell projection, filopodium {ECO:0000269|PubMed:12118066}. Cell projection, ruffle {ECO:0000269|PubMed:12118066}. Late endosome {ECO:0000269|PubMed:14722070}. Note=Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation. {ECO:0000269|PubMed:11001925, ECO:0000269|PubMed:12118066}. endosome to lysosome transport [GO:0008333]; intermediate filament organization [GO:0045109]; mitochondrion distribution [GO:0048311]; mitochondrion morphogenesis [GO:0070584]; muscle cell cellular homeostasis [GO:0046716]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; protein dephosphorylation [GO:0006470]; protein transport [GO:0015031]; regulation of vacuole organization [GO:0044088]; small molecule metabolic process [GO:0044281]@intermediate filament binding [GO:0019215]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; phosphatidylinositol binding [GO:0035091]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; I band [GO:0031674]; late endosome [GO:0005770]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR de< gradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. {ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925, ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:14722070, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:9537414}.O94923GLCED-glucuronyl C5-epimerase,carbohydrate metabolic process [GO:0005975]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210]; small molecule metabolic process [GO:0044281]heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]; UDP-glucuronate 5'-epimerase activity [GO:0050379]fGolgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]RFUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269|PubMed:20118238}.Q8TAE8G45IPEGrowth arrest and DNA damage-inducible proteins-interacting protein 1SUBCELLULAR LOCATION: Mitochondrion. Nucleus. Note=Using N-terminally tagged constructs, has been found in the nucleus (PubMed:12482659). C-terminally tagged constructs are targeted exclusively to mitochondria (PubMed:22453275). This discrepancy may be explained by masking of a potential N-terminal mitochondrial targeting signal by the tag (PubMed:22453275). {ECO:0000269|PubMed:12482659, ECO:0000269|PubMed:22453275}./mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; mitotic cell cycle arrest [GO:0071850]; organelle organization [GO:0006996]; viral process [GO:0016032]FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occurs also in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis.Q92625ANS1A3Ankyrin repeat and SAM domain-containing protein 1AzSUBCELLULAR LOCATION: Cytoplasm. Cell projection {ECO:0000250}. Note=Cytoplasmic before and after growth factor treatment.ephrin receptor signaling pathway [GO:0048013]; neuron remodeling [GO:0016322]; substrate-dependent cell migration [GO:0006929]Pcytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]FUNCTION: Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity). {ECO:0000250}.P04279SEMG1 Semenogelin-1@antibacterial humoral response [GO:0019731]; coagulation [GO:0050817]; insemination [GO:0007320]; negative regulation of calcium ion import [GO:0090281]; negative regulation of sperm motility [GO:1901318]; positive regulation of serine-type endopeptidase activity [GO:1900005]; protein heterooligomerization [GO:0051291]Imetal ion binding [GO:0046872]; structural molecule activity [GO:0005198]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; protein complex [GO:0043234]; secretory granule [GO:0030141]BFUNCTION: Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA. {ECO:0000269|PubMed:19889947}.; FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the proteolytic degradation of semenogelin, inhibit the secretion of pituitary follicle-stimulating hormone. {ECO:0000269|PubMed:19889947}.Q969M7UBE2FNEDD8-conjugating enzyme UBE2F protein neddylation [GO:0045116]_ATP binding [GO:0005524]; ligase activity [GO:0016874]; NEDD8 transferase activity [GO:0019788]JFUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. {ECO:0000269|PubMed:19250909}.P28161GSTM2Glutathione S-transferase Mu 2cellular detoxification of nitrogen compound [GO:0070458]; cellular response to caffeine [GO:0071313]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; nitrobenzene metabolic process [GO:0018916]; positive regulation of ryanodine-sensitive calcium-release channel activity [GO:0060316]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014809]; relaxation of cardiac muscle [GO:0055119]; small molecule metabolic process [GO:0044281]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]enzyme binding [GO:0019899]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]ucytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:16549767}.P53794SC5A3!Sodium/myo-inositol cotransporterinositol metabolic process [GO:0006020]; peripheral nervous system development [GO:0007422]; regulation of respiratory gaseous exchange [GO:0043576]; transmembrane transport [GO:0055085]; transport [GO:0006810]3myo-inositol:sodium symporter activity [GO:0005367]}integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Prevents intracellular accumulation of high concentrations of myo-inositol (an osmolyte) that result in impairment of cellular function.Q9BUT1BDH2&3-hydroxybutyrate dehydrogenase type 2 Siderophore biosynthesis.>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16380372}.epithelial cell differentiation [GO:0030855]; fatty acid beta-oxidation [GO:0006635]; heme metabolic process [GO:0042168]; iron ion homeostasis [GO:0055072]; siderophore biosynthetic process [GO:0019290]3-hydroxybutyrate dehydrogenase activity [GO:0003858]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]QFUNCTION: Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity). {ECO:0000250}.P25116PAR1Proteinase-activated receptor 1 activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of MAPKK activity [GO:0000186]; ana< tomical structure morphogenesis [GO:0009653]; blood coagulation [GO:0007596]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; establishment of synaptic specificity at neuromuscular junction [GO:0007529]; G-protein coupled receptor signaling pathway [GO:0007186]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; negative regulation of cell proliferation [GO:0008285]; negative regulation of glomerular filtration [GO:0003105]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of renin secretion into blood stream [GO:1900134]; phospholipase C-activating G-protein coupled receptor signaling pathway [GO:0007200]; platelet activation [GO:0030168]; platelet dense granule organization [GO:0060155]; positive regulation of blood coagulation [GO:0030194]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway [GO:0051482]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-6 secretion [GO:2000778]; positive regulation of interleukin-8 secretion [GO:2000484]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of vasoconstriction [GO:0045907]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]; regulation of blood coagulation [GO:0030193]; regulation of interleukin-1 beta production [GO:0032651]; regulation of sensory perception of pain [GO:0051930]; release of sequestered calcium ion into cytosol [GO:0051209]; response to lipopolysaccharide [GO:0032496]; response to wounding [GO:0009611]; STAT protein import into nucleus [GO:0007262]; tyrosine phosphorylation of STAT protein [GO:0007260]G-protein alpha-subunit binding [GO:0001965]; G-protein beta-subunit binding [GO:0031681]; G-protein coupled receptor activity [GO:0004930]; receptor binding [GO:0005102]; thrombin receptor activity [GO:0015057]caveola [GO:0005901]; cell surface [GO:0009986]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; platelet dense tubular network [GO:0031094]; postsynaptic membrane [GO:0045211]FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development. {ECO:0000269|PubMed:10079109}.P11387TOP1DNA topoisomerase 12SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12149243}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12149243}. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumolyated forms found in both nucleoplasm and nucleoli.|chromatin remodeling [GO:0006338]; chromosome segregation [GO:0007059]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA replication [GO:0006260]; DNA topological change [GO:0006265]; embryonic cleavage [GO:0040016]; phosphorylation [GO:0016310]; programmed cell death [GO:0012501]; response to drug [GO:0042493]; viral process [GO:0016032]chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA topoisomerase type I activity [GO:0003917]; DNA topoisomerase type II (ATP-hydrolyzing) activity [GO:0003918]; poly(A) RNA binding [GO:0044822]cytoplasmic mRNA processing body [GO:0000932]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; replication fork protection complex [GO:0031298]FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter. {ECO:0000250|UniProtKB:Q13472, ECO:0000269|PubMed:14594810, ECO:0000269|PubMed:16033260, ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:22904072, ECO:0000269|PubMed:2833744}.Q14146URB2/Unhealthy ribosome biogenesis protein 2 homologGSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15635413}.Daggresome [GO:0016235]; nucleolus [GO:0005730]; nucleus [GO:0005634]Q9BXS9S26A6!Solute carrier family 26 member 6SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Microsome {ECO:0000250}. Note=Localized in sperm membranes. Colocalizes with CFTR at the midpiece of sperm tail. Localizes to the apical membrane brush border of epithelial cells in the proximal tubules of kidney, of enterocytes of the small intestine and of gastric parietal cells in the stomach. May be translocated from the cytosolic surface of the cell membrane to the intracellular space by PKC in phorbol myristate acetate (PMA)-induced cells (By similarity). Colocalized with CA2 at the surface of the cell membrane in order to form a bicarbonate transport metabolon; colocalization is reduced in phorbol myristate acetate (PMA)-induced cells. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Note=Localizes to the apical and basolateral surfaces of tubular wall cells in kidney and in the brush border of pancreatic duct cells.; SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Multi-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 6: Cell membrane; Multi-pass membrane protein.angiotensin-activated signaling pathway [GO:0038166]; anion transmembrane transport [GO:0098656]; bicarbonate transport [GO:0015701]; cellular response to cAMP [GO:0071320]; cellular response to fructose stimulus [GO:0071332]; cellular response to interferon-gamma [GO:0071346]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; epithelial fluid transport [GO:0042045]; formate transport [GO:0015724]; intestinal absorption [GO:0050892]; intracellular pH elevation [GO:0051454]; ion transport [GO:0006811]; mannitol transport [GO:0015797]; oxalate transport [GO:0019532]; oxali< c acid secretion [GO:0046724]; positive regulation of dipeptide transmembrane transport [GO:2001150]; protein kinase C signaling [GO:0070528]; regulation of intracellular pH [GO:0051453]; sperm capacitation [GO:0048240]; sulfate transmembrane transport [GO:1902358]; sulfate transport [GO:0008272]; transepithelial chloride transport [GO:0030321]; transepithelial transport [GO:0070633]; transmembrane transport [GO:0055085]anion:anion antiporter activity [GO:0015301]; bicarbonate transmembrane transporter activity [GO:0015106]; chloride channel activity [GO:0005254]; chloride transmembrane transporter activity [GO:0015108]; efflux transmembrane transporter activity [GO:0015562]; formate efflux transmembrane transporter activity [GO:0015660]; formate transmembrane transporter activity [GO:0015499]; formate uptake transmembrane transporter activity [GO:0015659]; oxalate transmembrane transporter activity [GO:0019531]; PDZ domain binding [GO:0030165]; secondary active sulfate transmembrane transporter activity [GO:0008271]; sulfate transmembrane transporter activity [GO:0015116]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; membrane [GO:0016020]; membrane-bounded vesicle [GO:0031988]; plasma membrane [GO:0005886]; sperm midpiece [GO:0097225]; vesicle membrane [GO:0012506]FUNCTION: Apical membrane anion-exchanger with wide epithelial distribution that plays a role as a component of the pH buffering system for maintaining acid-base homeostasis. Acts as a versatile DIDS-sensitive inorganic and organic anion transporter that mediates the uptake of monovalent anions like chloride, bicarbonate, formate and hydroxyl ion and divalent anions like sulfate and oxalate. Function in multiple exchange modes involving pairs of these anions, which include chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate-sulfate and chloride-formate exchange. Apical membrane chloride-bicarbonate exchanger that mediates luminal chloride absorption and bicarbonate secretion by the small intestinal brush border membrane and contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption, possibly by providing a bicarbonate import pathway. Mediates also intestinal chloride absorption and oxalate secretion, thereby preventing hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate secretion, chloride-formate, chloride-oxalate and chloride-bicarbonate transport activities in the duodenum are inhibited by PKC activation in a calcium-independent manner. The apical membrane chloride-bicarbonate exchanger provides also a major route for fluid and bicarbonate secretion into the proximal tubules of the kidney as well as into the proximal part of the interlobular pancreatic ductal tree, where it mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize protein-rich acinar secretion. Mediates also the transcellular sulfate absorption and oxalate secretion across the apical membrane in the duodenum and the formate ion efflux at the apical brush border of cells in the proximal tubules of kidney. Plays a role in sperm capacitation by increasing intracellular pH.; FUNCTION: Isoform 4: Apical membrane chloride-bicarbonate exchanger. Its association with carbonic anhydrase CA2 forms a bicarbonate transport metabolon; hence maximizes the local concentration of bicarbonate at the transporter site.P62995TRA2B"Transformer-2 protein homolog betaCommon components(26)WSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9212162, ECO:0000269|PubMed:9546399}."cerebral cortex regionalization [GO:0021796]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing, via transesterification reactions [GO:0000375]<FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:9546399}.Q9HA64KT3KKetosamine-3-kinasephosphorylation [GO:0016310]kinase activity [GO:0016301]_FUNCTION: Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein-bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation. {ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908}.Q14697GANABNeutral alpha-glucosidase ABSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Melanosome {ECO:0000269|PubMed:10929008, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.wcarbohydrate binding [GO:0030246]; glucan 1,3-alpha-glucosidase activity [GO:0033919]; poly(A) RNA binding [GO:0044822]endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; glucosidase II complex [GO:0017177]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane [GO:0016020]FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. {ECO:0000269|PubMed:10929008}.Q9HBR0S38AA9Putative sodium-coupled neutral amino acid transporter 10qamino acid transmembrane transport [GO:0003333]; bone development [GO:0060348]; sodium ion transport [GO:0006814]:amino acid transmembrane transporter activity [GO:0015171]PFUNCTION: Putative sodium-dependent amino acid/proton antiporter. {ECO:0000250}.Q96AQ8MCUR1+Mitochondrial calcium uniporter regulator 1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23178883}; Multi-pass membrane protein {ECO:0000269|PubMed:23178883}.calcium ion import [GO:0070509]; mitochondrial calcium ion transport [GO:0006851]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]?integral component of mitochondrial inner membrane [GO:0031305]FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. Plays a direct role in uniporter-mediated calcium uptake, possibly via a direct interaction with MCU. {ECO:0000269|PubMed:23178883}.Q9UL18AGO1Protein argonaute-1cSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:20616046}.epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; innate immune response [GO:0045087]; miRNA loading onto RISC involved in gene silencing by miRNA [GO:0035280]; miRNA metabolic process [GO:0010586]; negative regulation of translation involved in gene silencing by miRNA [GO:0035278]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; nuclear-transcribed mRNA catabolic process [GO:0000956]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; posttranscriptional gene silencing [GO:0016441]; pre-miRNA processing [GO:0031054]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; RNA secondary structure unwinding [GO:0010501]; transcription, DNA-templated [G< O:0006351]wcore promoter binding [GO:0001047]; double-stranded RNA binding [GO:0003725]; miRNA binding [GO:0035198]; poly(A) RNA binding [GO:0044822]; pre-miRNA binding [GO:0070883]; RNA binding [GO:0003723]; RNA polymerase II core binding [GO:0000993]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; single-stranded RNA binding [GO:0003727]6cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; micro-ribonucleoprotein complex [GO:0035068]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs). {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:18771919}.Q9NNW5WDR6WD repeat-containing protein 6qSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17216128}. Note=Colocalizes in the cytoplasm with STK11/LKB1.cell cycle arrest [GO:0007050]; negative regulation of autophagy [GO:0010507]; negative regulation of cell proliferation [GO:0008285]FUNCTION: Enhances the STK11/LKB1-induced cell growth suppression activity. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:17216128, ECO:0000269|PubMed:22354037}.P61956SUMO2"Small ubiquitin-related modifier 21SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body.9cellular protein metabolic process [GO:0044267]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]wpoly(A) RNA binding [GO:0044822]; SUMO transferase activity [GO:0019789]; ubiquitin protein ligase binding [GO:0031625]Enucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:9556629}.Q9BX70BTBD2#BTB/POZ domain-containing protein 2_SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:12878161}. Note=Cytoplasmic bodies.-cytoplasmic mRNA processing body [GO:0000932]Q13464ROCK1Rho-associated protein kinase 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Cell projection, bleb. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Note=Associated with the mother centriole and an intercentriolar linker. Colocalizes with ITGB1BP1 and ITGB1 at the cell membrane predominantly in lamellipodia and membrane ruffles, but also in retraction fibers. Localizes at the cell membrane in an ITGB1BP1-dependent manner (By similarity). A small proportion is associated with Golgi membranes. {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; apical constriction [GO:0003383]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; bleb assembly [GO:0032060]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; ephrin receptor signaling pathway [GO:0048013]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; leukocyte tethering or rolling [GO:0050901]; membrane to membrane docking [GO:0022614]; myoblast migration [GO:0051451]; negative regulation of angiogenesis [GO:0016525]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein binding [GO:0032091]; positive regulation of focal adhesion assembly [GO:0051894]; programmed cell death [GO:0012501]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell adhesion [GO:0030155]; regulation of cell motility [GO:2000145]; regulation of establishment of cell polarity [GO:2000114]; regulation of focal adhesion assembly [GO:0051893]; regulation of keratinocyte differentiation [GO:0045616]; regulation of stress fiber assembly [GO:0051492]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle contraction [GO:0006939]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]bleb [GO:0032059]; centriole [GO:0005814]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle [GO:0001726]4FUNCTION: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. {ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}.Q13637RAB32Ras-related protein Rab-32SUBCELLULAR LOCATION: Mitochondrion. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.antigen processing and presentation [GO:0019882]; endosome to melanosome transport [GO:0035646]; intracellular protein transport [GO:0006886]; melanosome assembly [GO:1903232]; phagosome maturation [GO:0090382]; Rab protein signal transduction [GO:0032482]AP-1 adaptor complex binding [GO:0035650]; AP-3 adaptor complex binding [GO:0035651]; BLOC-2 complex binding [GO:0036461]; GTPase activity [GO:0003924]; G< TP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]early endosome [GO:0005769]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; trans-Golgi network [GO:0005802]wFUNCTION: Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000269|PubMed:12186851, ECO:0000269|PubMed:21255211}.P49593PPM1FProtein phosphatase 1Fcellular response to drug [GO:0035690]; histone dephosphorylation [GO:0016576]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein kinase activity by regulation of protein phosphorylation [GO:0044387]; negative regulation of transcription, DNA-templated [GO:0045892]; peptidyl-threonine dephosphorylation [GO:0035970]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of chemotaxis [GO:0050921]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of stress fiber assembly [GO:0051496]calmodulin-dependent protein phosphatase activity [GO:0033192]; metal ion binding [GO:0046872]; phosphatase activity [GO:0016791]; protein serine/threonine phosphatase activity [GO:0004722]`cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]FUNCTION: Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.Q14847LASP1LIM and SH3 domain protein 1SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich cortical cytoskeleton. {ECO:0000250}.Sion transport [GO:0006811]; positive regulation of signal transduction [GO:0009967]yion transmembrane transporter activity [GO:0015075]; SH3/SH2 adaptor activity [GO:0005070]; zinc ion binding [GO:0008270]icortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]bFUNCTION: Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity). {ECO:0000250}.Q8N5C1FA26EProtein FAM26Etcation transmembrane transport [GO:0098655]; cation transport [GO:0006812]; ion transmembrane transport [GO:0034220]$cation channel activity [GO:0005261]MFUNCTION: Pore-forming subunit of a voltage-gated ion channel. {ECO:0000250}.Q969P0IGSF8#Immunoglobulin superfamily member 8PSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein.cell proliferation [GO:0008283]; movement of cell or subcellular component [GO:0006928]; nervous system development [GO:0007399]; single fertilization [GO:0007338]; skeletal muscle tissue development [GO:0007519]!FUNCTION: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:12752121, ECO:0000269|PubMed:14662754, ECO:0000269|PubMed:15070678}.Q8NBM4UBAC20Ubiquitin-associated domain-containing protein 2negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; protein localization to endoplasmic reticulum [GO:0070972]Oendoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]Q8IVH4MMAA4Methylmalonic aciduria type A protein, mitochondrialpcellular lipid metabolic process [GO:0044255]; cobalamin biosynthetic process [GO:0009236]; cobalamin metabolic process [GO:0009235]; fatty acid beta-oxidation [GO:0006635]; short-chain fatty acid catabolic process [GO:0019626]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]9GTP binding [GO:0005525]; hydrolase activity [GO:0016787]FUNCTION: Probable GTPase. May function as chaperone. May be involved in the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis.Q9UGP4LIMD1LIM domain-containing protein 1 YAP activatorHSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body. Cell junction, adherens junction. Cell junction, focal adhesion. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions. Down-regulation and/or elimination of its expression from the nucleus of neoplastic cells correlates strongly with poor patient prognosis and aggressive forms of breast carcinoma. Conversely, strong nuclear localization correlates with low-tumor grade and better patient prognosis.cell migration [GO:0016477]; cytoplasmic mRNA processing body assembly [GO:0033962]; cytoskeleton organization [GO:0007010]; gene silencing by miRNA [GO:0035195]; multicellular organismal development [GO:0007275]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of hippo signaling [GO:0035331]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription, DNA-templated [GO:0045892]; osteoblast development [GO:0002076]; phosphorylation [GO:0016310]; positive regulation of gene silencing by miRNA [GO:2000637]; regulation of cell shape [GO:0008360]; regulation of transcription, DNA-templated [GO:0006355]; response to hypoxia [GO:0001666]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]Ntranscription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; RISC complex [GO:0016442]JFUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to < activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation. {ECO:0000269|PubMed:15542589, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22286099}.Q9HBM0VEZAVezatinSUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, adherens junction. Nucleus. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}.^chordate embryonic development [GO:0043009]; single organismal cell-cell adhesion [GO:0016337]acrosomal vesicle [GO:0001669]; adherens junction [GO:0005912]; cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stereocilia ankle link complex [GO:0002142]FUNCTION: Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life. In case of Listeria infection, promotes bacterial internalization by participating in myosin VIIa recruitment to the entry site. {ECO:0000269|PubMed:15090598}.P40189IL6RB#Interleukin-6 receptor subunit betaciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; cytokine-mediated signaling pathway [GO:0019221]; glycogen metabolic process [GO:0005977]; interleukin-27-mediated signaling pathway [GO:0070106]; interleukin-6-mediated signaling pathway [GO:0070102]; leukemia inhibitory factor signaling pathway [GO:0048861]; negative regulation of apoptotic process [GO:0043066]; negative regulation of interleukin-6-mediated signaling pathway [GO:0070104]; oncostatin-M-mediated signaling pathway [GO:0038165]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell proliferation [GO:0008284]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of tyrosine phosphorylation of Stat1 protein [GO:0042511]; positive regulation of tyrosine phosphorylation of Stat3 protein [GO:0042517]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of Notch signaling pathway [GO:0008593]; response to cytokine [GO:0034097]; viral process [GO:0016032]'ciliary neurotrophic factor receptor activity [GO:0004897]; ciliary neurotrophic factor receptor binding [GO:0005127]; growth factor binding [GO:0019838]; interleukin-11 receptor activity [GO:0004921]; interleukin-27 receptor activity [GO:0045509]; protein homodimerization activity [GO:0042803]ciliary neurotrophic factor receptor complex [GO:0070110]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; interleukin-6 receptor complex [GO:0005896]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; oncostatin-M receptor complex [GO:0005900]; plasma membrane [GO:0005886]FUNCTION: Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not bind IL6. May have a role in embryonic development (By similarity). The type I OSM receptor is capable of transducing OSM-specific signaling events. {ECO:0000250}.Q9UK39NOCT NocturninrSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.<circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; cytoplasmic mRNA processing body assembly [GO:0033962]; deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoblast differentiation [GO:0045668]; positive regulation of fat cell differentiation [GO:0045600]; regulation of circadian rhythm [GO:0042752]; regulation of embryonic development [GO:0045995]; regulation of transcription, DNA-templated [GO:0006355]; response to extracellular stimulus [GO:0009991]; response to lipopolysaccharide [GO:0032496]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; transcription from RNA polymerase II promoter [GO:0006366]metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A)-specific ribonuclease activity [GO:0004535]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Circadian deadenylase which plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Degrades poly(A) tails of specific target mRNAs leading to their degradation and suppression of translation. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by activating PPARG transcriptional activity in a deadenylase-independent manner by facilitating its nuclear translocation. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos (By similarity). {ECO:0000250}.Q9P031TAP264Thyroid transcription factor 1-associated protein 26FUNCTION: Component of the transcription complexes of the pulmonary surfactant-associated protein-B (SFTPB) and -C (SFTPC). Enhances homeobox protein Nkx-2.1-activated SFTPB and SFTPC promoter activities. {ECO:0000269|PubMed:12882447, ECO:0000269|PubMed:16630564}.Q9UQ53MGT4BHAlpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase Bcellular protein metabolic process [GO:0044267]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]{alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity [GO:0008454]; metal ion binding [GO:0046872]FUNCTION: Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis.P50570DYN2 Dynamin-2SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P39052}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Midbody. Note=Colocalizes with CTTN at the basis of filopodia in hippocampus neuron growth zones (By similarity). Microtubule-associated. Also found in the postsynaptic density of neuronal cells. {ECO:0000250|UniProtKB:P39052}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cellular response to carbon monoxide [GO:0071245]; cellular response to dopamine [GO:1903351]; cellular response to nitric oxide [GO:0071732]; cellular response to X-ray [GO:0071481]; cilium morphogenesis [GO:0060271]; endocytosis [GO:0006897]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi to plasma membrane transport [GO:0006893]; G-protein cou< pled receptor internalization [GO:0002031]; macropinocytosis [GO:0044351]; membrane organization [GO:0061024]; negative regulation of membrane tubulation [GO:1903526]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neuron projection morphogenesis [GO:0048812]; nitric oxide metabolic process [GO:0046209]; positive regulation of apoptotic process [GO:0043065]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phagocytosis [GO:0050766]; positive regulation of sodium:potassium-exchanging ATPase activity [GO:1903408]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of transcription, DNA-templated [GO:0045893]; post-Golgi vesicle-mediated transport [GO:0006892]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of axon extension [GO:0030516]; regulation of Golgi organization [GO:1903358]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of Rac protein signal transduction [GO:0035020]; regulation of transcription, DNA-templated [GO:0006355]; response to cocaine [GO:0042220]; response to light stimulus [GO:0009416]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; synaptic vesicle transport [GO:0048489]; transferrin transport [GO:0033572]enzyme binding [GO:0019899]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; microtubule binding [GO:0008017]; SH3 domain binding [GO:0017124]centrosome [GO:0005813]; clathrin-coated endocytic vesicle [GO:0045334]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; ruffle membrane [GO:0032587]; trans-Golgi network [GO:0005802]FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. {ECO:0000250|UniProtKB:P39052, ECO:0000269|PubMed:12498685}.Q15238PSG5(Pregnancy-specific beta-1-glycoprotein 5female pregnancy [GO:0007565]P30048PRDX37Thioredoxin-dependent peroxide reductase, mitochondrialapoptotic process [GO:0006915]; cellular response to oxidative stress [GO:0034599]; cellular response to reactive oxygen species [GO:0034614]; hydrogen peroxide catabolic process [GO:0042744]; maternal placenta development [GO:0001893]; mitochondrion organization [GO:0007005]; myeloid cell differentiation [GO:0030099]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of kinase activity [GO:0033673]; peptidyl-cysteine oxidation [GO:0018171]; positive regulation of cell proliferation [GO:0008284]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; regulation of mitochondrial membrane potential [GO:0051881]; response to hydrogen peroxide [GO:0042542]; response to lipopolysaccharide [GO:0032496]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]'alkyl hydroperoxide reductase activity [GO:0008785]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; kinase binding [GO:0019900]; protein C-terminus binding [GO:0008022]; protein kinase binding [GO:0019901]; thioredoxin peroxidase activity [GO:0008379]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]FUNCTION: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol. {ECO:0000269|PubMed:12492477}.Q08AD1CAMP22Calmodulin-regulated spectrin-associated protein 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23169647}. Note=Associated with the minus-end of microtubules and also detected at the centrosomes.emicrotubule cytoskeleton organization [GO:0000226]; regulation of organelle organization [GO:0033043]*microtubule minus-end binding [GO:0051011]:cytoplasm [GO:0005737]; microtubule minus-end [GO:0036449]jFUNCTION: Microtubule minus-end binding protein that may regulate the organization of non-centrosomal microtubules. May regulate the nucleation and the polymerization of microtubules. Indirectly, through the microtubule cytoskeleton, may regulate the organization of cellular organelles including the Golgi and the early endosomes. {ECO:0000269|PubMed:23169647}.Q06265EXOS9Exosome complex component RRP45SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:24105744}. Nucleus, nucleolus {ECO:0000269|PubMed:24105744}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24105744}. Note=Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744). {ECO:0000269|PubMed:24105744}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus.; SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleolus.; SUBCELLULAR LOCATION: Isoform 3: Nucleus. Note=Excluded from the nucleolus.<exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; immune response [GO:0006955]; nuclear mRNA surveillance [GO:0071028]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of cell growth [GO:0030307]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA processing [GO:0006364]3'-5'-exoribonuclease activity [GO:0000175]; AU-rich element binding [GO:0017091]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]>cytoplasm [GO:0005737]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; nuclear chromosome [GO:0000228]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA< . The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC9 binds to ARE-containing RNAs. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}.Q9NUY8TBC23TBC1 domain family member 23positive regulation of interleukin-6 production [GO:0032755]; regulation of inflammatory response [GO:0050727]; regulation of tumor necrosis factor production [GO:0032680]Q9UKK9NUDT5ADP-sugar pyrophosphataseFD-ribose catabolic process [GO:0019303]; nucleobase-containing small molecule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide metabolic process [GO:0009117]; ribonucleoside diphosphate catabolic process [GO:0009191]; small molecule metabolic process [GO:0044281]ADP-ribose diphosphatase activity [GO:0047631]; ADP-sugar diphosphatase activity [GO:0019144]; magnesium ion binding [GO:0000287]; nucleoside-diphosphatase activity [GO:0017110]; snoRNA binding [GO:0030515]jcytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; nucleus [GO:0005634]FUNCTION: Hydrolyzes with similar activities ADP-ribose ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:17052728}.Q13438OS9 Protein OS-9SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021}.ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; protein retention in ER lumen [GO:0006621]; protein targeting [GO:0006605]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; response to endoplasmic reticulum stress [GO:0034976]Dcarbohydrate binding [GO:0030246]; glycoprotein binding [GO:0001948]endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum quality control compartment [GO:0044322]; Hrd1p ubiquitin ligase complex [GO:0000836]FUNCTION: Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4. {ECO:0000269|PubMed:17932042, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:19346256, ECO:0000269|PubMed:21172656}.Q9H6R0DHX33)Putative ATP-dependent RNA helicase DHX33SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Predominantly in the nucleolus. During mitosis, localizes with the nucleolar organizing regions.mpositive regulation of transcription from RNA polymerase I promoter [GO:0045943]; RNA processing [GO:0006396]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]; rDNA binding [GO:0000182]Hcytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment. Important element of nucleolar organization. {ECO:0000269|PubMed:21930779}.Q8N5G0SMI20"Small integral membrane protein 20Q9BRX2PELOProtein pelota homologmRNA surveillance pathway(56)ESUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.(cell cycle [GO:0007049]; cell division [GO:0051301]; cell proliferation [GO:0008283]; chromosome organization [GO:0051276]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:0070966]; nuclear-transcribed mRNA catabolic process, non-stop decay [GO:0070481]; RNA surveillance [GO:0071025]Bendonuclease activity [GO:0004519]; metal ion binding [GO:0046872]fFUNCTION: Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential). {ECO:0000250, ECO:0000305}.P11274BCR!Breakpoint cluster region protein~SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}.-actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; inner ear morphogenesis [GO:0042472]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of cellular extravasation [GO:0002692]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neutrophil degranulation [GO:0043314]; neuromuscular process controlling balance [GO:0050885]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of GTPase activity [GO:0043547]; positive regulation of phagocytosis [GO:0050766]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell cycle [GO:0051726]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of vascular permeability [GO:0043114]; response to lipopolysaccharide [GO:0032496]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]ATP binding [GO:0005524]; GTPase activator activity [GO:0005096]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]cell junction [GO:0030054]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; protein complex [GO:0043234]FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity. {ECO:0000269|PubMed:1657398, ECO:0000269|PubMed:1903516}.O60831PRAF2PRA1 family protein 2SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305|PubMed:17975142}; Multi-pass membrane protein {ECO:0000305|PubMed:17975142}.BL-glutamate transport [GO:0015813]; protein transport [GO:0015031]Kendosome membrane [GO:0010008]; integral component of membrane [GO:0016021]FUNCTION: May be involved in ER/Golgi transport and vesicular traffic. Plays a proapoptic role in cerulenin-induced neuroblastoma apoptosis. {ECO:0000269|PubMed:17975142, ECO:0000269|PubMed:18395978}.Q00059TFAM%Transcription factor A, mitochondrialchromatin remodeling [GO:0006338]; DNA-dependent DNA replication [GO:0006261]; gene expression [GO:0010467]; mitochondrial respiratory chain complex assembly [GO:0033108]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase I promoter [GO:0006356]; transcription from mitochondrial promoter [GO:0006390]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from mitochondrial promoter [GO:0006391]chromatin binding [GO:0003682]; DNA binding, bending [GO:0008301]; mitochondrial light strand promoter sense binding [GO:0070363]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA < binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA. {ECO:0000269|PubMed:1737790, ECO:0000269|PubMed:19304746, ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:22037171, ECO:0000269|PubMed:22037172, ECO:0000269|PubMed:22841477}.Q9Y4P1ATG4BCysteine protease ATG4Bautophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to nitrogen starvation [GO:0006995]; C-terminal protein lipidation [GO:0006501]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; positive regulation of autophagy [GO:0010508]; positive regulation of protein catabolic process [GO:0045732]; protein delipidation [GO:0051697]; protein processing [GO:0016485]; protein targeting to membrane [GO:0006612]; proteolysis [GO:0006508]cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]FUNCTION: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:17347651, ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:22302004}.Q16854DGUOK$Deoxyguanosine kinase, mitochondrial;deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; dGTP metabolic process [GO:0046070]; guanosine metabolic process [GO:0008617]; negative regulation of neuron projection development [GO:0010977]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide biosynthetic process [GO:0009165]; protein phosphorylation [GO:0006468]; purine-containing compound salvage [GO:0043101]; purine deoxyribonucleoside metabolic process [GO:0046122]; purine nucleobase metabolic process [GO:0006144]; small molecule metabolic process [GO:0044281]nATP binding [GO:0005524]; deoxyguanosine kinase activity [GO:0004138]; nucleoside kinase activity [GO:0019206]icytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents. {ECO:0000269|PubMed:8706825}.Q53EP0FND3B1Fibronectin type III domain-containing protein 3BYSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.UFUNCTION: May be a positive regulator of adipogenesis. {ECO:0000269|PubMed:15564382}.Q14161GIT2"ARF GTPase-activating protein GIT2ybehavioral response to pain [GO:0048266]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]5focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]KFUNCTION: GTPase-activating protein for the ADP ribosylation factor family.P42704LPPRC8Leucine-rich PPR motif-containing protein, mitochondrialSUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note=Seems to be predominantly mitochondrial.6mitochondrion transport along microtubule [GO:0047497]; mRNA transport [GO:0051028]; negative regulation of mitochondrial RNA catabolic process [GO:0000961]; regulation of mitochondrial translation [GO:0070129]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; ubiquitin protein ligase binding [GO:0031625]condensed nuclear chromosome [GO:0000794]; cytoskeleton [GO:0005856]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:0030529]FUNCTION: May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). {ECO:0000250}.Q15287RNPS1-RNA-binding protein with serine-rich domain 1SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.hgene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]}mRNA 3'-UTR binding [GO:0003730]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]ASAP complex [GO:0061574]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]aFUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54< and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions. {ECO:0000269|PubMed:10449421, ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:14752011, ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17586820, ECO:0000269|PubMed:22203037}.Q9BTZ2DHRS4+Dehydrogenase/reductase SDR family member 4SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10333503}. Note=Isoform 1 is peroxisomal, while isoform 4 is not.; SUBCELLULAR LOCATION: Isoform 7: Nucleus {ECO:0000269|PubMed:22227495}.alcohol metabolic process [GO:0006066]; cellular ketone metabolic process [GO:0042180]; oxidation-reduction process [GO:0055114]; protein tetramerization [GO:0051262]; steroid metabolic process [GO:0008202]3-keto sterol reductase activity [GO:0000253]; alcohol dehydrogenase [NAD(P)+] activity [GO:0018455]; carbonyl reductase (NADPH) activity [GO:0004090]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; receptor binding [GO:0005102]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones (By similarity). {ECO:0000250}.P14735IDEInsulin-degrading enzymeSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Secreted {ECO:0000250}. Note=Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.beta-amyloid metabolic process [GO:0050435]; bradykinin catabolic process [GO:0010815]; determination of adult lifespan [GO:0008340]; hormone catabolic process [GO:0042447]; insulin catabolic process [GO:1901143]; insulin metabolic process [GO:1901142]; insulin receptor signaling pathway [GO:0008286]; negative regulation of proteolysis [GO:0045861]; positive regulation of protein oligomerization [GO:0032461]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein homotetramerization [GO:0051289]; protein processing [GO:0016485]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; ubiquitin homeostasis [GO:0010992]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; beta-amyloid binding [GO:0001540]; beta-endorphin binding [GO:0031626]; glycoprotein binding [GO:0001948]; insulin binding [GO:0043559]; metalloendopeptidase activity [GO:0004222]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270]8cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]FUNCTION: Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia. {ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166}.P62316SMD2%Small nuclear ribonucleoprotein Sm D2gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; pICln-Sm protein complex [GO:0034715]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U4 snRNP [GO:0005687]FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.Q9Y2B0CNPY2Protein canopy homolog 2negative regulation of gene expression [GO:0010629]; positive regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045716]; regulation of low-density lipoprotein particle clearance [GO:0010988]Vendoplasmic reticulum [GO:0005783]; integral component of plasma membrane [GO:0005887]FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation.Q9UNQ2DIM1&Probable dimethyladenosine transferase18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase activity [GO:0052909]; poly(A) RNA binding [GO:0044822]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179]FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. {ECO:0000250}.Q9H2H8PPIL3*Peptidyl-prolyl cis-trans isomerase-like 3)catalytic step 2 spliceosome [GO:0071013]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.Q96A65EXOC4Exocyst complex component 4cellular protein metabolic process [GO:0044267]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]Hprotein N-terminus binding [GO:0047485]; Ral GTPase binding [GO:0017160]cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocyst [GO:0000145]; growth cone membrane [GO:0032584]; membrane [GO:0016020]; myelin sheath abaxonal region [GO:0035748]; plasma membrane [GO:0005886]FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250}.Q9BWG4SSBP4%Single-stranded DNA-binding protein 4(single-stranded DNA binding [GO:0003697]Q9ULC3RAB23Ras-related protein Rab-23Hedgehog LRP2/Rab23SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane. Cytoplasm. Cytoplasmic vesicle, autophagosome. Endosome membrane {ECO:0000250}. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or< M.tuberculosis./autophagosome assembly [GO:0000045]; cellular defense response [GO:0006968]; cilium assembly [GO:0042384]; craniofacial suture morphogenesis [GO:0097094]; embryonic digit morphogenesis [GO:0042733]; intracellular protein transport [GO:0006886]; negative regulation of proteolysis [GO:0045861]; negative regulation of transcription factor import into nucleus [GO:0042992]; neural tube closure [GO:0001843]; Rab protein signal transduction [GO:0032482]; regulation of smoothened signaling pathway [GO:0008589]; spinal cord dorsal/ventral patterning [GO:0021513]autophagosome [GO:0005776]; cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]}FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes. {ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:22452336}.P19883FST Follistatin6hematopoietic progenitor cell differentiation [GO:0002244]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of hair follicle development [GO:0051798]; signal transduction [GO:0007165]Eactivin binding [GO:0048185]; signal transducer activity [GO:0004871]FUNCTION: Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).Q9P2R3ANFY1 Rabankyrin-5CSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10940552}. Endosome membrane {ECO:0000269|PubMed:10940552}; Peripheral membrane protein {ECO:0000269|PubMed:10940552}. Early endosome {ECO:0000269|PubMed:15328530}. Note=Also associated with endosomal membranes. Localizes to macropinosomes. {ECO:0000269|PubMed:15328530}.endocytosis [GO:0006897]; endosomal vesicle fusion [GO:0034058]; endosome localization [GO:0032439]; Golgi to lysosome transport [GO:0090160]; positive regulation of pinocytosis [GO:0048549]; retrograde transport, endosome to Golgi [GO:0042147]tmetal ion binding [GO:0046872]; phosphatidylinositol phosphate binding [GO:1901981]; Rab GTPase binding [GO:0017137]early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; macropinosome [GO:0044354]; membrane [GO:0016020]"FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI(3)P). Involved in homotypic early endosome fusion and to a lesser extend in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Involved in macropinocytosis; the function is dependent on Rab5-GTP. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the sucellular localization of the retromer complex in a EHD1-dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport. {ECO:0000269|PubMed:15328530, ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721}.Q9BSK0MALD1"MARVEL domain-containing protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000269|PubMed:19364627}. Note=Observed in the nucleus and at the perinuclear region during interphase, but localizes at the mitotic spindle and midbody at metaphase. A significant fraction of MARVELD1 translocates to the plasma membrane during anaphase or upon microtubule depolymerization (By similarity). {ECO:0000250}.cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Microtubule-associated protein that exhibits cell cycle-dependent localization and can inhibit cell proliferation and migration. {ECO:0000250}.P24390ERD21%ER lumen protein-retaining receptor 1wSUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:14517323}; Multi-pass membrane protein {ECO:0000269|PubMed:14517323}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14517323}; Multi-pass membrane protein {ECO:0000269|PubMed:14517323}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:14517323}.intracellular protein transport [GO:0006886]; protein retention in ER lumen [GO:0006621]; vesicle-mediated transport [GO:0016192]"KDEL sequence binding [GO:0005046]Icis-Golgi network [GO:0005801]; COPI-coated vesicle membrane [GO:0030663]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Required for the retention of luminal endoplasmic reticulum resident proteins via vesicular recycling. This receptor recognizes the C-terminal K-D-E-L motif. COPI-coated transport intermediates, either in the form of round vesicles or as tubular processes, mediate retrograde traffic of the KDEL receptor-ligand complexes. Also required for normal vesicular traffic through the Golgi. {ECO:0000269|PubMed:11703931}.Q15291RBBP5 Retinoblastoma-binding protein 5<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17355966}. cellular response to DNA damage stimulus [GO:0006974]; chromatin organization [GO:0006325]; histone H3-K4 methylation [GO:0051568]; regulation of transcription, DNA-templated [GO:0006355]; response to estrogen [GO:0043627]; transcription, DNA-templated [GO:0006351]amethylated histone binding [GO:0035064]; transcription regulatory region DNA binding [GO:0044212]histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]FUNCTION: In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. {ECO:0000250, ECO:0000269|PubMed:19556245}.Q9H5X1FA96AMIP18 family protein FAM96A>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22683786}.Nchromosome segregation [GO:0007059]; iron-sulfur cluster assembly [GO:0016226]vFUNCTION: May play a role in chromosome segregation through establishment of sister chromatid cohesion. {ECO:0000250}.O60763USO1'General vesicular transport factor p115ASUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus membrane; Peripheral membrane protein. Note=Recycles between the cytosol and the Golgi apparatus during interphase. During interphase, the phosphorylated form is found exclusively in cytosol; the unphosphorylated form is associated with Golgi apparatus membranes.ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi vesicle docking [GO:0048211]; intracellular protein transport [GO:0006886]; memb< rane fusion [GO:0061025]; mitotic cell cycle [GO:0000278]; transcytosis [GO:0045056]; vesicle fusion with Golgi apparatus [GO:0048280]Kpoly(A) RNA binding [GO:0044822]; protein transporter activity [GO:0008565]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; membrane [GO:0016020]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]vFUNCTION: General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity (By similarity). {ECO:0000250}.Q9NP61ARFG33ADP-ribosylation factor GTPase-activating protein 3intracellular protein transport [GO:0006886]; positive regulation of GTPase activity [GO:0043547]; protein secretion [GO:0009306]; vesicle-mediated transport [GO:0016192]qGTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; protein transporter activity [GO:0008565]~cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes. {ECO:0000269|PubMed:11172815}.Q9HCE0EPG5$Ectopic P granules protein 5 homolog_autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; endocytic recycling [GO:0032456]FUNCTION: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:23222957}.Q9Y376CAB39Calcium-binding protein 39cell cycle arrest [GO:0007050]; cellular hypotonic response [GO:0071476]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of rubidium ion transmembrane transporter activity [GO:2000687]; negative regulation of rubidium ion transport [GO:2000681]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; signal transduction by protein phosphorylation [GO:0023014]kinase binding [GO:0019900]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activator activity [GO:0043539]ncytosol [GO:0005829]; extracellular exosome [GO:0070062]; serine/threonine protein kinase complex [GO:1902554]FUNCTION: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1. {ECO:0000269|PubMed:19892943}.Q5T8D3ACBD5,Acyl-CoA-binding domain-containing protein 5dSUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.;peroxisome degradation [GO:0030242]; transport [GO:0006810]integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters. {ECO:0000269|PubMed:24535825}.Q9UP83COG5,Conserved oligomeric Golgi complex subunit 5SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9792665}. Golgi apparatus membrane {ECO:0000269|PubMed:9792665}; Peripheral membrane protein {ECO:0000269|PubMed:9792665}.Sintra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]; nucleoplasm [GO:0005654]<FUNCTION: Required for normal Golgi function. {ECO:0000250}.O75503CLN5(Ceroid-lipofuscinosis neuronal protein 5=SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11971870}.brain development [GO:0007420]; glycosylation [GO:0070085]; lysosomal lumen acidification [GO:0007042]; neurogenesis [GO:0022008]; neuron maturation [GO:0042551]; protein catabolic process [GO:0030163]; signal peptide processing [GO:0006465]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]Q9NRM1ENAMEnameliniSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O97939}.Eamelogenesis [GO:0097186]; biomineral tissue development [GO:0031214]/proteinaceous extracellular matrix [GO:0005578]FUNCTION: Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation. {ECO:0000250|UniProtKB:O97939}.P23381SYWC$Tryptophan--tRNA ligase, cytoplasmicAminoacyl-tRNA biosynthesis(42)angiogenesis [GO:0001525]; gene expression [GO:0010467]; negative regulation of cell proliferation [GO:0008285]; regulation of angiogenesis [GO:0045765]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]; tryptophanyl-tRNA aminoacylation [GO:0006436]FATP binding [GO:0005524]; tryptophan-tRNA ligase activity [GO:0004830] FUNCTION: Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression. {ECO:0000269|PubMed:11773625, ECO:0000269|PubMed:11773626, ECO:0000269|PubMed:1373391, ECO:0000269|PubMed:14630953}.Q99459CDC5L"Cell division cycle 5-like proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9598309}. Nucleus speckle {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:10827081, ECO:0000269|PubMed:11544257}. Cytoplasm {ECO:0000269|PubMed:9038199}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000269|PubMed:9038199}.%DNA repair [GO:0006281]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; signal transduction involved in DNA damage checkpoint [GO:0072422]; transcription, DNA-templated [GO:0006351]cDNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; WD40-repeat domain binding [GO:0071987]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Prp19 complex [GO:0000974]\FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). {ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11082045, ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:18583928, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:9038199, ECO:0000269|PubMed:9468527, ECO< :0000269|PubMed:9632794}.Q13905RPGF1(Rap guanine nucleotide exchange factor 1CSUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:17724123}.lactivation of MAPKK activity [GO:0000186]; blood vessel development [GO:0001568]; cellular response to cAMP [GO:0071320]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of endothelial barrier [GO:0061028]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of neural precursor cell proliferation [GO:2000178]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of Ras protein signal transduction [GO:0046580]; nerve growth factor signaling pathway [GO:0038180]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron projection development [GO:0010976]; Rap protein signal transduction [GO:0032486]; regulation of cell junction assembly [GO:1901888]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169];Rap guanyl-nucleotide exchange factor activity [GO:0017034]Hcytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]FUNCTION: Guanine nucleotide-releasing protein that binds to SH3 domain of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS. Plays a role in the establishment of basal endothelial barrier function. Plays a role in nerve growth factor (NGF)-induced sustained activation of Rap1 and neurite outgrowth. {ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:7806500}.Q5VW36FOCAD FocadhesinSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell junction, focal adhesion. Note=Colocalizes with VCL in astrocytes.Hfocal adhesion [GO:0005925]; integral component of membrane [GO:0016021]?FUNCTION: Potential tumor suppressor in gliomas. {ECO:0000250}.Q5T0D9TPRGL/Tumor protein p63-regulated gene 1-like proteinSUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Note=Localized to presynaptic nerve terminals. {ECO:0000250}.]cell junction [GO:0030054]; extracellular exosome [GO:0070062]; synaptic vesicle [GO:0008021]O60925PFD1Prefoldin subunit 1de novo' posttranslational protein folding [GO:0051084]; cell cycle [GO:0007049]; cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]; regulation of transcription, DNA-templated [GO:0006355]protein binding involved in protein folding [GO:0044183]; sequence-specific DNA binding transcription factor activity [GO:0003700]prefoldin complex [GO:0016272]FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.P25774CATS Cathepsin Sadaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; basement membrane disassembly [GO:0034769]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of cation channel activity [GO:2001259]; positive regulation of inflammatory response [GO:0050729]; protein processing [GO:0016485]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; response to acidic pH [GO:0010447]; toll-like receptor signaling pathway [GO:0002224]collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; fibronectin binding [GO:0001968]; laminin binding [GO:0043236]; proteoglycan binding [GO:0043394]endolysosome lumen [GO:0036021]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:0016020]FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.Q5T013HYI"Putative hydroxypyruvate isomerase/hydroxypyruvate isomerase activity [GO:0008903]FUNCTION: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). {ECO:0000250}.Q7Z5G4GOGA7Golgin subfamily A member 7SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:14522980, ECO:0000269|PubMed:16000296}; Lipid-anchor {ECO:0000269|PubMed:14522980, ECO:0000269|PubMed:16000296}.Golgi to plasma membrane protein transport [GO:0043001]; peptidyl-L-cysteine S-palmitoylation [GO:0018230]; protein stabilization [GO:0050821]extracellular exosome [GO:0070062]; Golgi stack [GO:0005795]; intrinsic component of Golgi membrane [GO:0031228]; palmitoyltransferase complex [GO:0002178]FUNCTION: May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. {ECO:0000269|PubMed:14522980, ECO:0000269|PubMed:16000296}.Q9NZ09UBAP1Ubiquitin-associated protein 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21757351}. Endosome {ECO:0000269|PubMed:21757351}. Note=Predominantly cytosolic. Recruited to endosomes as part of the ESCRT-I complex.protein transport [GO:0015031]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]ubiquitin binding [GO:0043130]cytoplasm [GO:0005737]; cytosol [GO:0005829]; ESCRT I complex [GO:0000813]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2. {ECO:0000269|PubMed:21757351, ECO:0000269|PubMed:22405001}.P13797PLST Plastin-3bone development [GO:0060348]FUNCTION: Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development.Q99442SEC62Translocation protein SEC62cellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; posttranslational protein targeting to membrane [GO:0006620]Iprotein transporter activity [GO:0008565]; receptor activity [GO:0004872]aggresome [GO:0016235]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; rough endoplasmic reticulum [GO:0005791]?FUNCTION: Required for preprotein translocation. {ECO:0000250}.P30837AL1B1'Aldehyde dehydrogenase X, mitochondrial Alcohol metabolismScarbohydrate metabolic process [GO:0005975]; ethanol catabolic process [GO:0006068]2aldehyde dehydrogenase (NAD) activity [GO:0004029]intracellular membra< ne-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation.Q9BY77PDIP3&Polymerase delta-interacting protein 3dSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Nucleocytoplasmic shuttling protein._poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of translation [GO:0045727]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]FUNCTION: Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex. {ECO:0000269|PubMed:18423201, ECO:0000269|PubMed:22928037}.P62079TSN5 Tetraspanin-5establishment of protein localization to plasma membrane [GO:0090002]; positive regulation of Notch signaling pathway [GO:0045747]; protein maturation [GO:0051604]Q9BXS4TMM59Transmembrane protein 59SUBCELLULAR LOCATION: Late endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded.autophagy [GO:0006914]; negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; negative regulation of protein glycosylation in Golgi [GO:0090285]; negative regulation of protein processing [GO:0010955]; positive regulation of autophagy [GO:0010508]#endopeptidase activity [GO:0004175]kextracellular exosome [GO:0070062]; Golgi cis cisterna [GO:0000137]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; plasma membrane [GO:0005886]MFUNCTION: Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding. {ECO:0000269|PubMed:20427278, ECO:0000269|PubMed:23376921}.O60828PQBP1Polyglutamine-binding protein 1OSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:23512658}. Nucleus speckle {ECO:0000250}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. {ECO:0000250}.Falternative mRNA splicing, via spliceosome [GO:0000380]; cilium morphogenesis [GO:0060271]; neuron projection development [GO:0031175]; regulation of dendrite morphogenesis [GO:0048814]; regulation of RNA splicing [GO:0043484]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]yDNA binding [GO:0003677]; ribonucleoprotein complex binding [GO:0043021]; transcription coactivator activity [GO:0003713] centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; primary cilium [GO:0072372]FUNCTION: Probably functions as scaffold protein that is part of numerous complexes and thereby plays a role in pre-mRNA splicing, transcription regulation and neuron development. Required for normal alternative splicing of target pre-mRNA species (PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. {ECO:0000269|PubMed:10198427, ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:12062018, ECO:0000269|PubMed:20410308, ECO:0000269|PubMed:23512658}.Q14353GAMT$Guanidinoacetate N-methyltransferasecellular nitrogen compound metabolic process [GO:0034641]; creatine biosynthetic process [GO:0006601]; creatine metabolic process [GO:0006600]; embryonic liver development [GO:1990402]; muscle contraction [GO:0006936]; organ morphogenesis [GO:0009887]; regulation of multicellular organism growth [GO:0040014]; S-adenosylhomocysteine metabolic process [GO:0046498]; S-adenosylmethionine metabolic process [GO:0046500]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]cguanidinoacetate N-methyltransferase activity [GO:0030731]; methyltransferase activity [GO:0008168]P23497SP100Nuclear autoantigen Sp-100$SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm. Note=Differences in the subnuclear localization of the different isoforms seem to exist and may also be cell cycle- and interferon-dependent. Accumulates in the cytoplasm upon FAS activation.; SUBCELLULAR LOCATION: Isoform Sp100-C: Nucleus {ECO:0000269|PubMed:11313457}. Note=Forms a reticulate or track-like nuclear pattern with denser concentrations at the nuclear lamina and surrounding the nucleoli, a pattern reminiscent of heterochromatin-rich regions according to PubMed:11313457.cellular protein metabolic process [GO:0044267]; chromatin remodeling [GO:0006338]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of cellular component movement [GO:0051271]; negative regulation of DNA binding [GO:0043392]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of viral transcription [GO:0032897]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of angiogenesis [GO:0045765]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of Fas signaling pathway [GO:1902044]; response to cytokine [GO:0034097]; response to interferon-gamma [GO:0034341]; response to retinoic acid [GO:0032526]; response to type I interferon [GO:0034340]; retinoic acid receptor signaling pathway [GO:0048384]; telomere maintenance [GO:0000723]; transcription, DNA-templated [GO:0006351]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]chromatin binding [GO:0003682]; chromo shadow domain binding [GO:0070087]; DNA binding [GO:0< 003677]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; nuclear periphery [GO:0034399]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation. {ECO:0000269|PubMed:11909962, ECO:0000269|PubMed:14647468, ECO:0000269|PubMed:15247905, ECO:0000269|PubMed:15592518, ECO:0000269|PubMed:15767676, ECO:0000269|PubMed:16177824, ECO:0000269|PubMed:17245429, ECO:0000269|PubMed:21274506, ECO:0000269|PubMed:21880768}.Q9UBI4STML1Stomatin-like protein 1bSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.-SMAD protein signal transduction [GO:0060395]Q01459DIACDi-N-acetylchitobiaseUchitin catabolic process [GO:0006032]; oligosaccharide catabolic process [GO:0009313]<chitinase activity [GO:0004568]; chitin binding [GO:0008061]~extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]FUNCTION: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.Q9H074PAIP13Polyadenylate-binding protein-interacting protein 1,gene expression [GO:0010467]; mRNA stabilization [GO:0048255]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of translation [GO:0045727]; translational initiation [GO:0006413]ERNA binding [GO:0003723]; translation activator activity [GO:0008494]{FUNCTION: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:9548260}.Q969G6RIFKRiboflavin kinaseapoptotic process [GO:0006915]; FMN biosynthetic process [GO:0009398]; positive regulation of NAD(P)H oxidase activity [GO:0033864]; reactive oxygen species metabolic process [GO:0072593]; riboflavin biosynthetic process [GO:0009231]; riboflavin metabolic process [GO:0006771]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]aATP binding [GO:0005524]; metal ion binding [GO:0046872]; riboflavin kinase activity [GO:0008531]FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase. {ECO:0000269|PubMed:19641494}.Q9H2K0IF3M1Translation initiation factor IF-3, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational initiation [GO:0070124]; organelle organization [GO:0006996]; ribosome disassembly [GO:0032790]ribosomal small subunit binding [GO:0043024]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]FUNCTION: IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins. {ECO:0000269|PubMed:12095986}.P22570ADRO/NADPH:adrenodoxin oxidoreductase, mitochondrial Steroid metabolismC21-steroid hormone biosynthetic process [GO:0006700]; cholesterol metabolic process [GO:0008203]; generation of precursor metabolites and energy [GO:0006091]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202]; sterol metabolic process [GO:0016125]; ubiquinone biosynthetic process [GO:0006744]; xenobiotic metabolic process [GO:0006805]cferredoxin-NADP+ reductase activity [GO:0004324]; NADPH-adrenodoxin reductase activity [GO:0015039]8FUNCTION: Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.Q15031SYLM,Probable leucine--tRNA ligase, mitochondrialgene expression [GO:0010467]; leucyl-tRNA aminoacylation [GO:0006429]; tRNA aminoacylation for protein translation [GO:0006418]qaminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; leucine-tRNA ligase activity [GO:0004823]Q9UPU5UBP24(Ubiquitin carboxyl-terminal hydrolase 24proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation. {ECO:0000269|PubMed:23159851}.Q9BZM1PG12A%Group XIIA secretory phospholipase A2fSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12522102}. Cytoplasm {ECO:0000269|PubMed:12522102}. glycerophospholipid biosynthetic process [GO:0046474]; lipid catabolic process [GO:0016042]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152]; phosphatidylglycerol acyl-chain remodeling [GO:0036148]; phosphatidylinositol acyl-chain remodeling [GO:0036149]; phosphatidylserine acyl-chain remodeling [GO:0036150]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]Zcalcium-dependent phospholipase A2 activity [GO:0047498]; calcium ion binding [GO:0005509]cendoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine. {ECO:0000269|PubMed:12522102}.P27701CD82 CD82 antigen%inhibition of angiogenesis/metastasis`FUNCTION: Associates w< ith CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway.Q4KMQ2ANO6 Anoctamin-6rSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows an intracellular localization according to PubMed:22075693.`activation of blood coagulation via clotting cascade [GO:0002543]; bleb assembly [GO:0032060]; blood coagulation [GO:0007596]; bone mineralization involved in bone maturation [GO:0035630]; calcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; calcium activated phosphatidylserine scrambling [GO:0061589]; calcium ion transmembrane transport [GO:0070588]; cation transport [GO:0006812]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; dendritic cell chemotaxis [GO:0002407]; ion transmembrane transport [GO:0034220]; negative regulation of cell volume [GO:0045794]; phosphatidylserine exposure on blood platelet [GO:0097045]; phospholipid scrambling [GO:0017121]; pore complex assembly [GO:0046931]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone mineralization [GO:0030501]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of ion transmembrane transport [GO:0034767]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of phagocytosis, engulfment [GO:0060100]; purinergic nucleotide receptor signaling pathway [GO:0035590]; regulation of anion transmembrane transport [GO:1903959]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]calcium activated cation channel activity [GO:0005227]; intracellular calcium activated chloride channel activity [GO:0005229]; phospholipid scramblase activity [GO:0017128]; voltage-gated chloride channel activity [GO:0005247]; voltage-gated ion channel activity [GO:0005244]cell surface [GO:0009986]; chloride channel complex [GO:0034707]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; membrane [GO:0016020]; plasma membrane [GO:0005886]EFUNCTION: Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets and osteoblasts. Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization. Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes. {ECO:0000250|UniProtKB:Q6P9J9, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539, ECO:0000269|PubMed:22006324, ECO:0000269|PubMed:22946059}.Q14318FKBP8)Peptidyl-prolyl cis-trans isomerase FKBP8SUBCELLULAR LOCATION: Isoform 1: Mitochondrion membrane; Single-pass membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion membrane; Single-pass membrane protein; Cytoplasmic side.Hapoptotic process [GO:0006915]; camera-type eye development [GO:0043010]; cell fate specification [GO:0001708]; chaperone-mediated protein folding [GO:0061077]; dorsal/ventral neural tube patterning [GO:0021904]; intracellular signal transduction [GO:0035556]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; positive regulation of BMP signaling pathway [GO:0030513]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of gene expression [GO:0010468]; smoothened signaling pathway [GO:0007224]; viral process [GO:0016032]FK506 binding [GO:0005528]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]FUNCTION: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. {ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:15757646, ECO:0000269|PubMed:16176796}.Q96GQ7DDX27)Probable ATP-dependent RNA helicase DDX27.FUNCTION: Probable ATP-dependent RNA helicase.P62873GBB1@Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1uadenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; blood coagulation [GO:0007596]; cardiac muscle cell apoptotic process [GO:0010659]; cell proliferation [GO:0008283]; cellular response to catecholamine stimulus [GO:0071870]; cellular response to glucagon stimulus [GO:0071377]; cellular response to hypoxia [GO:0071456]; cellular response to prostaglandin E stimulus [GO:0071380]; energy reserve metabolic process [GO:0006112]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; phospholipase C-activating G-protein coupled receptor signaling pathway [GO:0007200]; phototransduction, visible light [GO:0007603]; platelet activation [GO:0030168]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; Ras protein signal transduction [GO:0007265]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; retina development in camera-type eye [GO:0060041]; rhodopsin mediated signaling pathway [GO:0016056]; sensory perception of taste [GO:0050909]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]GTPase activity [GO:0003924]; GTPase binding [GO:0051020]; protein complex binding [GO:0032403]; signal transducer activity [GO:0004871]cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; heterotrimeric G-protein complex [GO:0005834]; intracellular [GO:0005622]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; myelin sheath [GO:0043209]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]6FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. {ECO:0000269|PubMed:18611381}.Q5PRF9SMAG2Protein Smaug homolog 2eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20510020}. Nucleus {ECO:0000269|PubMed:20510020}.FUNCTION: Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A. {ECO:0000269|PubMed:20510020}.P43897EFTS#Elongation factor Ts, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; organelle organization [GO:0006996]; regulation of DNA-templated transcription, elongation [GO:0032784]; translational elongation [GO:0006414]Upoly(A) RNA binding [GO:0044822]; translation elongation factor activity [GO:0003746]mmitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. {ECO:0000255|HAMAP-Rule:MF_03135}.Q12905ILF2%Interleukin enhancer-binding factor 2< SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.immune response [GO:0006955]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; transferase activity [GO:0016740]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. {ECO:0000269|PubMed:10574923, ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:9442054}.Q6N069NAA164N-alpha-acetyltransferase 16, NatA auxiliary subunitnegative regulation of apoptotic process [GO:0043066]; N-terminal protein amino acid acetylation [GO:0006474]; positive regulation of transcription, DNA-templated [GO:0045893]; protein stabilization [GO:0050821]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; NatA complex [GO:0031415]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity.Q8NBM8PCYXLPrenylcysteine oxidase-likeoxidation-reduction process [GO:0055114]; prenylated protein catabolic process [GO:0030327]; prenylcysteine catabolic process [GO:0030328],prenylcysteine oxidase activity [GO:0001735]Xextracellular region [GO:0005576]; membrane [GO:0016020]; vacuolar membrane [GO:0005774]1FUNCTION: Probable oxidoreductase. {ECO:0000250}.Q14197ICT1+Peptidyl-tRNA hydrolase ICT1, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20186120, ECO:0000269|PubMed:23908630}.mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; rescue of stalled ribosome [GO:0072344]aminoacyl-tRNA hydrolase activity [GO:0004045]; ribosome binding [GO:0043022]; translation release factor activity, codon nonspecific [GO:0016150]mitochondrial inner membrane [GO:0005743]; mitochondrial large ribosomal subunit [GO:0005762]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit. Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes. {ECO:0000269|PubMed:20186120}.Q9P2D3HTR5B!HEAT repeat-containing protein 5BP19022CADH2 Cadherin-2adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; glial cell differentiation [GO:0010001]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; muscle cell differentiation [GO:0042692]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; neuroligin clustering involved in postsynaptic membrane assembly [GO:0097118]; neuronal stem cell maintenance [GO:0097150]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of synaptic vesicle clustering [GO:2000809]; protein heterooligomerization [GO:0051291]; regulation of axonogenesis [GO:0050770]; regulation of myelination [GO:0031641]; regulation of postsynaptic density protein 95 clustering [GO:1902897]; regulation of Rho protein signal transduction [GO:0035023]; striated muscle cell differentiation [GO:0051146]alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; calcium ion binding [GO:0005509]; gamma-catenin binding [GO:0045295]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; catenin complex [GO:0016342]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; synapse [GO:0045202]xFUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density (By similarity). {ECO:0000250}.O43716GATC<Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrialcSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.glutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681]; mitochondrial translation [GO:0032543]; regulation of translational fidelity [GO:0006450]`ATP binding [GO:0005524]; glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity [GO:0050567]>FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.P98172EFNB1 Ephrin-B1 ligand/RTKaxon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; embryonic pattern specification [GO:0009880]; ephrin receptor signaling pathway [GO:0048013]; neural crest cell migration [GO:0001755]; positive regulation of T cell proliferation [GO:0042102]$ephrin receptor binding [GO:0046875]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]%FUNCTION: Binds to the receptor tyrosine kinases EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity). {ECO:0000250}.; FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the< orientation of longitudinally projecting axons (By similarity). {ECO:0000250}.P21291CSRP1#Cysteine and glycine-rich protein 1!platelet aggregation [GO:0070527]Uextracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]4FUNCTION: Could play a role in neuronal development.Q5ZPR3CD276 CD276 antigenB7-H2/H3cell proliferation [GO:0008283]; immune response [GO:0006955]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interferon-gamma biosynthetic process [GO:0045077]; negative regulation of interleukin-2 biosynthetic process [GO:0045085]; negative regulation of T cell proliferation [GO:0042130]; positive regulation of bone mineralization [GO:0030501]; positive regulation of interferon-gamma biosynthetic process [GO:0045078]; positive regulation of interleukin-2 secretion [GO:1900042]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of T cell proliferation [GO:0042102]; regulation of immune response [GO:0050776]; T cell activation [GO:0042110]~external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]FUNCTION: May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling. {ECO:0000269|PubMed:11224528, ECO:0000269|PubMed:12906861, ECO:0000269|PubMed:14764704, ECO:0000269|PubMed:15314238, ECO:0000269|PubMed:15682454, ECO:0000269|PubMed:15961727}.O75955FLOT1 Flotillin-1SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Melanosome. Endosome. Note=Membrane-associated protein of caveolae. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.axonogenesis [GO:0007409]; cellular response to exogenous dsRNA [GO:0071360]; dsRNA transport [GO:0033227]; establishment of protein localization to plasma membrane [GO:0090002]; extracellular matrix disassembly [GO:0022617]; membrane raft assembly [GO:0001765]; plasma membrane raft assembly [GO:0044854]; positive regulation of cell adhesion molecule production [GO:0060355]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; positive regulation of cell junction assembly [GO:1901890]; positive regulation of cytokine production [GO:0001819]; positive regulation of endocytosis [GO:0045807]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of protein binding [GO:0032092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of synaptic transmission, dopaminergic [GO:0032226]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; protein homooligomerization [GO:0051260]; protein kinase C signaling [GO:0070528]; protein localization to membrane raft [GO:1903044]; regulation of receptor internalization [GO:0002090]; regulation of Rho protein signal transduction [GO:0035023]; response to endoplasmic reticulum stress [GO:0034976]Oprotease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell adherens junction [GO:0005913]; cell-cell contact zone [GO:0044291]; centriolar satellite [GO:0034451]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; flotillin complex [GO:0016600]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lamellipodium [GO:0030027]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; uropod [GO:0001931]FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.O14519CDKA1.Cyclin-dependent kinase 2-associated protein 1cell cycle [GO:0007049]; DNA-dependent DNA replication [GO:0006261]; positive regulation of protein phosphorylation [GO:0001934]#DNA polymerase binding [GO:0070182]Bnucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]JFUNCTION: specific inhibitor of the cell-cycle kinase CDK2. {ECO:0000250}.P55201BRPF1PeregrinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358}. Cytoplasm {ECO:0000269|PubMed:18794358}. Note=Localization to the nucleus depends on KAT6A, ING5 and MEAF6.chromatin organization [GO:0006325]; histone H3 acetylation [GO:0043966]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]7DNA binding [GO:0003677]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2. {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.Q9NVV4PAPD1%Poly(A) RNA polymerase, mitochondrialyhistone mRNA catabolic process [GO:0071044]; mRNA polyadenylation [GO:0006378]; transcription, DNA-templated [GO:0006351].ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; poly(A) RNA binding [GO:0044822]; polynucleotide adenylyltransferase activity [GO:0004652]; protein homodimerization activity [GO:0042803]; UTP binding [GO:0002134]Qintracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]BFUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA. {ECO:0000269|PubMed:15547249, ECO:0000269|PubMed:15769737, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}.Q9HD15SRA1 Steroid receptor RNA activator 1eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12565891}. Cytoplasm {ECO:0000269|PubMed:12565891}.+apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; positive regulation of receptor activity [GO:2000273]; regulation of apoptotic process [GO:0042981]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:0030529]FUNCTION: Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of< steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis. {ECO:0000269|PubMed:10199399, ECO:0000269|PubMed:12943696, ECO:0000269|PubMed:14517287, ECO:0000269|PubMed:15147866, ECO:0000269|PubMed:15351741}.P61599NAA20N-alpha-acetyltransferase 20eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18570629}. Nucleus {ECO:0000269|PubMed:18570629}.ccytoplasm [GO:0005737]; intracellular [GO:0005622]; NatB complex [GO:0031416]; nucleus [GO:0005634]FUNCTION: Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration. {ECO:0000269|PubMed:18570629}.Q8WW12PCNP2PEST proteolytic signal-containing nuclear protein<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12176013}.cell cycle [GO:0007049]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]3FUNCTION: May be involved in cell cycle regulation.O76071CIAO1=Probable cytosolic iron-sulfur protein assembly protein CIAO1chromosome segregation [GO:0007059]; iron-sulfur cluster assembly [GO:0016226]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; small molecule metabolic process [GO:0044281]3CIA complex [GO:0097361]; MMXD complex [GO:0071817]FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation. {ECO:0000255|HAMAP-Rule:MF_03037, ECO:0000269|PubMed:17937914, ECO:0000269|PubMed:20797633}.P22102PUR25Trifunctional purine biosynthetic protein adenosine-3yde novo' IMP biosynthetic process [GO:0006189]; brainstem development [GO:0003360]; cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; glycine metabolic process [GO:0006544]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; response to inorganic substance [GO:0010035]; response to organic substance [GO:0010033]; small molecule metabolic process [GO:0044281]; tetrahydrofolate biosynthetic process [GO:0046654]$ATP binding [GO:0005524]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641]; phosphoribosylglycinamide formyltransferase activity [GO:0004644]Q13137CACO2;Calcium-binding and coiled-coil domain-containing protein 2lSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi apparatus. Cytoplasm, cytoskeleton. Note=According to PubMed:7540613, localizes to nuclear dots. According to PubMed:9230084 and PubMed:12869526, it is not a nuclear dot-associated protein but localizes predominantly in the cytoplasm with a coarse-grained distribution preferentially close to the nucleus.Eresponse to interferon-gamma [GO:0034341]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion. {ECO:0000269|PubMed:17635994}.O75976CBPDCarboxypeptidase Dmetallocarboxypeptidase activity [GO:0004181]; serine-type carboxypeptidase activity [GO:0004185]; zinc ion binding [GO:0008270]P62195PRS8!26S protease regulatory subunit 8ESUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of programmed cell death [GO:0043069]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of inclusion body assembly [GO:0090261]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032](ATPase activity [GO:0016887]; ATP binding [GO:0005524]; proteasome-activating ATPase activity [GO:0036402]; TBP-class protein binding [GO:0017025]; thyrotropin-releasing hormone receptor binding [GO:0031531]; transcription cofactor activity [GO:0003712]; transcription factor binding [GO:0008134]blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular exosome [GO:0070062]; inclusion body [GO:0016234]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]Q66K74MAP1S!Microtubule-associated protein 1SkSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Note=Detected in filopodia-like protrusions and synapses (By similarity). Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the nucleus in cells exhibiting apoptosis. Associated specifically with microtubules stabilized by paclitaxel and colocalizes with RASSF1 isoform A. In interphase cells, shows a diffuse cytoplasmic staining with partial localization to the microtubules. During the different stages of mitosis detected at the spindle microtubules. {ECO:0000250}.Bapoptotic process [GO:0006915]; autophagy [GO:0006914]; brain development [GO:0007420]; microtubule bundle formation [GO:0001578< ]; mitochondrion transport along microtubule [GO:0047497]; nervous system development [GO:0007399]; neuron projection morphogenesis [GO:0048812]; regulation of chromatin disassembly [GO:0010848]actin filament binding [GO:0051015]; beta-tubulin binding [GO:0048487]; DNA binding [GO:0003677]; microtubule binding [GO:0008017]; tubulin binding [GO:0015631]@cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]; synapse [GO:0045202]TFUNCTION: Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). {ECO:0000250}.P23246SFPQ,Splicing factor, proline- and glutamine-richVSUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm. Note=Predominantly in nuclear matrix.alternative mRNA splicing, via spliceosome [GO:0000380]; double-strand break repair via homologous recombination [GO:0000724]; histone H3 deacetylation [GO:0070932]; mRNA processing [GO:0006397]; negative regulation of circadian rhythm [GO:0042754]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of sister chromatid cohesion [GO:0045876]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; histone deacetylase binding [GO:0042826]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; transcription regulatory region DNA binding [GO:0044212]; transcription regulatory region sequence-specific DNA binding [GO:0000976]chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; paraspeckles [GO:0042382]; RNA polymerase II transcription factor complex [GO:0090575] FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}.Q96CU9FXRD18FAD-dependent oxidoreductase domain-containing protein 1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20858599, ECO:0000305|PubMed:25678554}; Single-pass membrane protein {ECO:0000255}. Note=According to a report, it is associated with the matrix face of the mitochondrial inner membrane and does not contain any transmembrane region. However, one transmembrane domain is clearly predicted by different methods (Probable). {ECO:0000305|PubMed:25678554}.FUNCTION: Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) (PubMed:20858599, PubMed:25678554). Involved in mid-late stages of complex I assembly (PubMed:25678554). {ECO:0000269|PubMed:20858599, ECO:0000269|PubMed:25678554}.Q9UK58CCNL1 Cyclin-L1SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. {ECO:0000250}.regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of transcription, DNA-templated [GO:0006355]; RNA processing [GO:0006396]; transcription, DNA-templated [GO:0006351]0nuclear speck [GO:0016607]; nucleus [GO:0005634]FUNCTION: Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Seems to be involved in the regulation of RNA polymerase II (pol II). Functions in association with cyclin-dependent kinases (CDKs) and has a role in the second step of splicing. May be a candidate proto-oncogene in head and neck squamous cell carcinomas (HNSCC). Inhibited by the CDK-specific inhibitor p21. {ECO:0000269|PubMed:11980906, ECO:0000269|PubMed:12414649, ECO:0000269|PubMed:15700036}.O95249GOSR1$Golgi SNAP receptor complex member 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network (By similarity). Enriched on vesicular components at the terminal rims of the Golgi. Found in Golgi microtubules at low temperature (15 degrees Celsius). {ECO:0000250}.ER to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane fusion [GO:0061025]; protein transport [GO:0015031]; retrograde transport, en< dosome to Golgi [GO:0042147]cis-Golgi network [GO:0005801]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; SNARE complex [GO:0031201]FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:21860593}.P40937RFC5Replication factor C subunit 5base-excision repair [GO:0006284]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]OATP binding [GO:0005524]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]GDNA replication factor C complex [GO:0005663]; nucleoplasm [GO:0005654]FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. {ECO:0000269|PubMed:8999859}.Q86YR5GPSM1G-protein-signaling modulator 1AGS3SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side.cell differentiation [GO:0030154]; nervous system development [GO:0007399]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]0GDP-dissociation inhibitor activity [GO:0005092]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction. {ECO:0000269|PubMed:11024022, ECO:0000269|PubMed:12642577}.Q9H8G2CAAP1*Caspase activity and apoptosis inhibitor 1FUNCTION: Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop. {ECO:0000269|PubMed:21980415}.O75494SRS10'Serine/arginine-rich splicing factor 10mSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11684676}. Cytoplasm {ECO:0000269|PubMed:11684676}.cytoplasmic transport [GO:0016482]; mRNA export from nucleus [GO:0006406]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RS domain binding [GO:0050733]; unfolded protein binding [GO:0051082]FUNCTION: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator. {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:12419250, ECO:0000269|PubMed:14765198}.Q9UBQ5EIF3K4Eukaryotic translation initiation factor 3 subunit KSUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010, ECO:0000269|PubMed:15327989}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010, ECO:0000269|PubMed:15327989}.Rribosome binding [GO:0043022]; translation initiation factor activity [GO:0003743]$cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]O43815STRNStriatinbicellular tight junction assembly [GO:0070830]; dendrite development [GO:0016358]; locomotory behavior [GO:0007626]; negative regulation of cell proliferation [GO:0008285]; Wnt signaling pathway [GO:0016055]armadillo repeat domain binding [GO:0070016]; calmodulin binding [GO:0005516]; estrogen receptor binding [GO:0030331]; protein complex binding [GO:0032403]; protein phosphatase 2A binding [GO:0051721]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]FUNCTION: Calmodulin-binding protein which may function as scaffolding or signaling protein and may play a role in dendritic Ca(2+) signaling.Q8NFW8NEUA&N-acylneuraminate cytidylyltransferase<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11602804}.cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; N-acetylneuraminate metabolic process [GO:0006054]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]<N-acylneuraminate cytidylyltransferase activity [GO:0008781]Emembrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]=FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).P61604CH10(10 kDa heat shock protein, mitochondrial Chaperoninsactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; osteoblast differentiation [GO:0001649]; protein folding [GO:0006457]; response to unfolded protein [GO:0006986]ATP binding [GO:0005524]; chaperone binding [GO:0051087]; poly(A) RNA binding [GO:0044822]; unfolded protein binding [GO:0051082]xextracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.Q09019DMWD1Dystrophia myotonica WD repeat-containing proteinTFUNCTION: Could have a regulatory function in meiosis. {ECO:0000269|PubMed:8499920}.Q15020SART37Squamous cell carcinoma antigen recognized by T-cells 3+SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:10463607, ECO:0000269|PubMed:11959860, ECO:0000269|PubMed:12578909}. Nucleus, Cajal body < {ECO:0000269|PubMed:12578909}. Nucleus speckle {ECO:0000269|PubMed:11959860}. Cytoplasm {ECO:0000269|PubMed:10463607, ECO:0000269|PubMed:11959860}.cell morphogenesis [GO:0000902]; hematopoietic stem cell proliferation [GO:0071425]; homeostasis of number of cells [GO:0048872]; mRNA splicing, via spliceosome [GO:0000398]; nucleosome assembly [GO:0006334]; positive regulation of histone deubiquitination [GO:1903586]; regulation of gene expression [GO:0010468]; spliceosomal snRNP assembly [GO:0000387]; spliceosomal tri-snRNP complex assembly [GO:0000244]histone binding [GO:0042393]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; U4 snRNA binding [GO:0030621]; U6atac snRNA binding [GO:0030624]; U6 snRNA binding [GO:0017070]; ubiquitin-specific protease binding [GO:1990381]{Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity). {ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085, ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.; FUNCTION: Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication. {ECO:0000269|PubMed:11959860}.Q9UBF2COPG2Coatomer subunit gamma-2 SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Tends to be more abundant in the trans-Golgi network compared to the cis-Golgi. {ECO:0000250}.intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]Q9BUE0MED186Mediator of RNA polymerase II transcription subunit 18FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.P11908PRPS2$Ribose-phosphate pyrophosphokinase 2$ Metabolic intermediate biosynthesis5-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; nucleobase-containing compound metabolic process [GO:0006139]; nucleotide biosynthetic process [GO:0009165]; ribonucleoside monophosphate biosynthetic process [GO:0009156]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; ribose phosphate diphosphokinase activity [GO:0004749]sFUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.A1L0T0ILVBL"Acetolactate synthase-like protein=SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.rmagnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976]; transferase activity [GO:0016740]O60826CCD22(Coiled-coil domain-containing protein 22cellular copper ion homeostasis [GO:0006878]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; Golgi to plasma membrane transport [GO:0006893]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; protein transport [GO:0015031]*cullin family protein binding [GO:0097602]endosome [GO:0005768]FUNCTION: Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via assocation with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10 (PubMed:23563313). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (PubMed:25355947). {ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:25355947}.Q9UKS6PACN3AProtein kinase C and casein kinase substrate in neurons protein 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11179684}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Detected at the inner aspect of the plasma membrane in myotubes. {ECO:0000250}.Ccytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; membrane tubulation [GO:0097320]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of endocytosis [GO:0045806]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; regulation of endocytosis [GO:0030100]calcium channel inhibitor activity [GO:0019855]; cytoskeletal protein binding [GO:0008092]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]cytoplasm [GO:0005737]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; membrane-bounded vesicle [GO:0031988]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]6FUNCTION: Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity (By similarity). {ECO:0000250}.Q6V1X1DPP8Dipeptidyl peptidase 8xSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12534281, ECO:0000269|PubMed:12662155}.6immune response [GO:0006955]; proteolysis [GO:0006508]Wdipeptidyl-peptidase activity [GO:0008239]; serine-type peptidase activity [GO:0008236]Gcytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function. {ECO:0000269|PubMed:11012666}.Q5JVF3PCID2PCI domain-containing protein 2negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptida< se activity [GO:2000117]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of mRNA stability [GO:0043488]; spleen development [GO:0048536]FUNCTION: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability. R-loop accumulation does not increase in PCID2-depleted cells. {ECO:0000250, ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:24896180}.Q14814MEF2D#Myocyte-specific enhancer factor 2DSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15743823}. Note=Translocated by HDAC4 to nuclear dots.adult heart development [GO:0007512]; apoptotic process [GO:0006915]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; muscle organ development [GO:0007517]; nervous system development [GO:0007399]; osteoblast differentiation [GO:0001649]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; skeletal muscle cell differentiation [GO:0035914]; transcription, DNA-templated [GO:0006351]Tactivating transcription factor binding [GO:0033613]; histone deacetylase binding [GO:0042826]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; sequence-specific DNA binding transcription factor activity [GO:0003700]4FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity). {ECO:0000250}.Q9UMZ2SYNRGSynergin gammaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associates with membranes via the adapter protein complex AP-1. Colocalizes with AP1G1 (By similarity). {ECO:0000250}.Fendocytosis [GO:0006897]; intracellular protein transport [GO:0006886]WAP-1 adaptor complex [GO:0030121]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]FUNCTION: May play a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN). May act by linking the adapter protein complex AP-1 to other proteins.Q5JRX3PREP#Presequence protease, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16849325}.qpositive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]; proteolysis [GO:0006508]qenzyme activator activity [GO:0008047]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]FUNCTION: ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. {ECO:0000269|PubMed:16849325}.O75534CSDE1'Cold shock domain-containing protein E1male gonad development [GO:0008584]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:0070966]; regulation of transcription, DNA-templated [GO:0006355]CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]FUNCTION: RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:15314026}.P42229STA5A3Signal transducer and activator of transcription 5ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15534001}. Nucleus {ECO:0000269|PubMed:15534001}. Note=Translocated into the nucleus in response to phosphorylation. 2-oxoglutarate metabolic process [GO:0006103]; allantoin metabolic process [GO:0000255]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; citrate metabolic process [GO:0006101]; creatine metabolic process [GO:0006600]; creatinine metabolic process [GO:0046449]; development of secondary female sexual characteristics [GO:0046543]; development of secondary male sexual characteristics [GO:0046544]; epithelial cell differentiation involved in prostate gland development [GO:0060742]; fatty acid metabolic process [GO:0006631]; female pregnancy [GO:0007565]; isoleucine metabolic process [GO:0006549]; JAK-STAT cascade [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; lactation [GO:0007595]; lipid storage [GO:0019915]; luteinization [GO:0001553]; mammary gland epithelium development [GO:0061180]; natural killer cell differentiation [GO:0001779]; negative regulation of erythrocyte differentiation [GO:0045647]; negative regulation of mast cell apoptotic process [GO:0033026]; oxaloacetate metabolic process [GO:0006107]; peptidyl-tyrosine phosphorylation [GO:0018108]; Peyer's patch development [GO:0048541]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-2 biosynthetic process [GO:0045086]; positive regulation of mast cell differentiation [GO:0060376]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; prolactin signaling pathway [GO:0038161]; prostate gland epithelium morphogenesis [GO:0060740]; regulation of epithelial cell differentiation [GO:0030856]; regulation of multicellular organism growth [GO:0040014]; regulation of steroid metabolic process [GO:0019218]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; succinate metabolic process [GO:0006105]; taurine metabolic process [GO:0019530]; T cell differentiation in thymus [GO:0033077]; T cell homeostasis [GO:0043029]; transcription, DNA-templated [GO:0006351]; valine metabolic process [GO:0006573]RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871].cytosol [GO:0005829]; nucleoplasm [GO:0005654]< FUNCTION: Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation. {ECO:0000269|PubMed:11773439, ECO:0000269|PubMed:15534001}.Q9NY27PP4R2;Serine/threonine-protein phosphatase 4 regulatory subunit 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Note=Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2.cellular protein modification process [GO:0006464]; mRNA processing [GO:0006397]; regulation of catalytic activity [GO:0050790]; regulation of double-strand break repair via homologous recombination [GO:0010569]; RNA splicing [GO:0008380]bprotein binding, bridging [GO:0030674]; protein phosphatase type 4 regulator activity [GO:0030362]centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein phosphatase 4 complex [GO:0030289]{FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. {ECO:0000269|PubMed:10769191, ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:20154705}.Q8N1G0ZN687Zinc finger protein 687Q96BF6NACC2&Nucleus accumbens-associated protein 2jSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22926524}. Note=Predominantly associated with chromatin.cellular protein complex localization [GO:0034629]; histone deacetylation [GO:0016575]; negative regulation of cell proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle by negative regulation of transcription from RNA polymerase II promoter [GO:1900477]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cell proliferation [GO:0008284]; positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902231]; posttranscriptional regulation of gene expression [GO:0010608]; protein homooligomerization [GO:0051260]; transcription, DNA-templated [GO:0006351]histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II transcription factor binding transcription factor activity [GO:0001076]Onuclear body [GO:0016604]; nuclear chromatin [GO:0000790]; nucleus [GO:0005634] FUNCTION: Functions as a transcriptional repressor through its association with the NuRD complex. Recruits the NuRD complex to the promoter of MDM2, leading to the repression of MDM2 transcription and subsequent stability of p53/TP53. {ECO:0000269|PubMed:22926524}.Q9BV38WDR18WD repeat-containing protein 18SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000250}.QFUNCTION: May play a role during development (By similarity). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000250, ECO:0000269|PubMed:22872859}.O60547GMDSGDP-mannose 4,6 dehydratasede novo' GDP-L-fucose biosynthetic process [GO:0042351]; GDP-mannose metabolic process [GO:0019673]; Notch signaling pathway [GO:0007219]MGDP-mannose 4,6-dehydratase activity [GO:0008446]; NADP+ binding [GO:0070401]WFUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.P84095RHOG$Rho-related GTP-binding protein RhoGactin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell chemotaxis [GO:0060326]; platelet activation [GO:0030168]; positive regulation of cell proliferation [GO:0008284]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of transcription, DNA-templated [GO:0045893]; Rac protein signal transduction [GO:0016601]; regulation of ruffle assembly [GO:1900027]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]FUNCTION: Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry. {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17074883, ECO:0000269|PubMed:17875742, ECO:0000269|PubMed:20679435}.Q8IWZ8SUGP1,SURP and G-patch domain-containing protein 1;nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681],FUNCTION: Plays a role in pre-mRNA splicing.Q9Y584TIM22=Mitochondrial import inner membrane translocase subunit Tim22cellular protein metabolic process [GO:0044267]; protein import into mitochondrial inner membrane [GO:0045039]; protein targeting to mitochondrion [GO:0006626]%protein channel activity [GO:0015266]FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). {ECO:0000250}.Q96G03PGM2Phosphoglucomutase-27carbohydrate metabolic process [GO:0005975]; deoxyribose phosphate catabolic process [GO:0046386]; galactose catabolic process [GO:0019388]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; small molecule metabolic process [GO:0044281]vmagnesium ion binding [GO:0000287]; phosphoglucomutase activity [GO:0004614]; phosphopentomutase activity [GO:0008973]GFUNCTION: Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity. {ECO:0000269|PubMed:17804405}.P04792HSPB1Heat shock protein beta-1Transcriptional.SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear spl< icing speckles.cellular response to vascular endothelial growth factor stimulus [GO:0035924]; gene expression [GO:0010467]; intracellular signal transduction [GO:0035556]; movement of cell or subcellular component [GO:0006928]; negative regulation of apoptotic process [GO:0043066]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of protein kinase activity [GO:0006469]; platelet aggregation [GO:0070527]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [GO:0038033]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of tumor necrosis factor biosynthetic process [GO:0042535]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; regulation of translational initiation [GO:0006446]; response to unfolded protein [GO:0006986]; response to virus [GO:0009615]; retina homeostasis [GO:0001895]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein kinase C inhibitor activity [GO:0008426]; ubiquitin binding [GO:0043130]*cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]; spindle [GO:0005819]; Z disc [GO:0030018]?FUNCTION: Involved in stress resistance and actin organization.Q96AB3ISOC2:Isochorismatase domain-containing protein 2, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:17658461}. Nucleus {ECO:0000269|PubMed:17658461}. Note=Localizes to the nucleus in the presence of CDKN2A.Hcytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]H7BZ55CROL3;Putative ciliary rootlet coiled-coil protein-like 3 proteinP54098DPOG1DNA polymerase subunit gamma-1Base excision repair (BER)aging [GO:0007568]; base-excision repair, gap-filling [GO:0006287]; cellular response to glucose stimulus [GO:0071333]; DNA biosynthetic process [GO:0071897]; DNA-dependent DNA replication [GO:0006261]; DNA metabolic process [GO:0006259]; mitochondrial DNA replication [GO:0006264]; response to gamma radiation [GO:0010332]; response to hyperoxia [GO:0055093]; response to light stimulus [GO:0009416]3'-5' exonuclease activity [GO:0008408]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; protease binding [GO:0002020]extracellular exosome [GO:0070062]; gamma DNA polymerase complex [GO:0005760]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; protein complex [GO:0043234]; terminal bouton [GO:0043195]^FUNCTION: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA.P43034LIS1;Platelet-activating factor acetylhydrolase IB subunit alphaEther lipid metabolism#SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. {ECO:0000250}.% acrosome assembly [GO:0001675]; actin cytoskeleton organization [GO:0030036]; adult locomotory behavior [GO:0008344]; ameboidal-type cell migration [GO:0001667]; auditory receptor cell development [GO:0060117]; brain morphogenesis [GO:0048854]; cerebral cortex development [GO:0021987]; cerebral cortex neuron differentiation [GO:0021895]; cochlea development [GO:0090102]; corpus callosum morphogenesis [GO:0021540]; cortical microtubule organization [GO:0043622]; establishment of centrosome localization [GO:0051660]; establishment of mitotic spindle orientation [GO:0000132]; establishment of planar polarity of embryonic epithelium [GO:0042249]; G2/M transition of mitotic cell cycle [GO:0000086]; hippocampus development [GO:0021766]; layer formation in cerebral cortex [GO:0021819]; learning or memory [GO:0007611]; lipid catabolic process [GO:0016042]; microtubule-based process [GO:0007017]; microtubule cytoskeleton organization [GO:0000226]; microtubule cytoskeleton organization involved in establishment of planar polarity [GO:0090176]; microtubule organizing center organization [GO:0031023]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of JNK cascade [GO:0046329]; negative regulation of neuron projection development [GO:0010977]; neuroblast proliferation [GO:0007405]; neuromuscular process controlling balance [GO:0050885]; neuron migration [GO:0001764]; nuclear envelope disassembly [GO:0051081]; nuclear migration [GO:0007097]; organelle organization [GO:0006996]; osteoclast development [GO:0036035]; platelet activating factor metabolic process [GO:0046469]; positive regulation of axon extension [GO:0045773]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of embryonic development [GO:0040019]; positive regulation of mitotic cell cycle [GO:0045931]; protein secretion [GO:0009306]; regulation of GTPase activity [GO:0043087]; regulation of microtubule cytoskeleton organization [GO:0070507]; retrograde axon cargo transport [GO:0008090]; small GTPase mediated signal transduction [GO:0007264]; stem cell division [GO:0017145]; synaptic transmission [GO:0007268]; transmission of nerve impulse [GO:0019226]; vesicle transport along microtubule [GO:0047496]dynactin binding [GO:0034452]; dynein binding [GO:0045502]; heparin binding [GO:0008201]; microtubule binding [GO:0008017]; phospholipase binding [GO:0043274]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]astral microtubule [GO:0000235]; axon [GO:0030424]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; motile primary cilium [GO:0031512]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at th< e nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. {ECO:0000250, ECO:0000269|PubMed:15173193}.O95372LYPA2Acyl-protein thioesterase 2)fatty acid metabolic process [GO:0006631]FUNCTION: May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43. {ECO:0000250, ECO:0000269|PubMed:21152083}.Q06323PSME1&Proteasome activator complex subunit 1-endopeptidase activator activity [GO:0061133]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; proteasome activator complex [GO:0008537]; proteasome complex [GO:0000502]Q9BQ04RBM4BRNA-binding protein 4B%circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; mRNA processing [GO:0006397]; positive regulation of gene expression [GO:0010628]; regulation of translation [GO:0006417]; RNA splicing [GO:0008380]nucleolus [GO:0005730]FUNCTION: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA (By similarity). {ECO:0000250}.Q96C23GALMAldose 1-epimerasePgalactose metabolic process [GO:0006012]; glucose metabolic process [GO:0006006]Kaldose 1-epimerase activity [GO:0004034]; carbohydrate binding [GO:0030246]FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity). {ECO:0000250}.Q96AX1VP33A/Vacuolar protein sorting-associated protein 33ASUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q63615}. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24554770}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}.autophagosome fusion [GO:0000046]; autophagosome maturation [GO:0097352]; endosome to lysosome transport [GO:0008333]; lysosome localization [GO:0032418]; melanosome localization [GO:0032400]; platelet formation [GO:0030220]; protein transport [GO:0015031]; regulation of developmental pigmentation [GO:0048070]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192]early endosome [GO:0005769]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS16 but not VIPAS39 (PubMed:25783203). The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG (PubMed:24554770). {ECO:0000269|PubMed:24554770, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.O43164PJA2#E3 ubiquitin-protein ligase Praja-2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Golgi apparatus membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus. Expressed in the postsynaptic density region of synapses (By similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane. {ECO:0000250}.hippo signaling [GO:0035329]; long-term memory [GO:0007616]; protein ubiquitination [GO:0016567]; regulation of protein kinase A signaling [GO:0010738]ligase activity [GO:0016874]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cell junction [GO:0030054]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]YFUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes. {ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:21423175}.Q96AY4TTC28#Tetratricopeptide repeat protein 28ZSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}. Note=At interphase, localizes to centrosomes. At prometaphase and metaphase, associated with spindle microtubules and spindle poles. At anaphase, accumulates in the spindle midzone. At telophase, condensed on central spindles. During cytokinesis, condensed on the midbody where it colocalizes with AURKB (By similarity). {ECO:0000250}.pcell division [GO:0051301]; mitotic nuclear division [GO:0007067]; regulation of mitotic cell cycle [GO:0007346]`centrosome [GO:0005813]; cytoplasm [GO:0005737]; midbody [GO:0030496]; spindle pole [GO:0000922]FUNCTION: During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody. {ECO:0000269|PubMed:23036704}.Q9H1C7CYTM1;Cysteine-rich and transmembrane domain-containing protein 1Q9NP72RAB18Ras-related protein Rab-18;brain development [GO:0007420]; endoplasmic reticulum tubular network organization [GO:0071786]; eye development [GO:0001654]; intracellular protein transport [GO:0006886]; lipid particle organization [GO:0034389]; Rab protein signal transduction [GO:0032482]; small GTPase mediated signal transduction [GO:0007264]endoplasmic reticulum tubular network [GO:0071782]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration. {ECO:0000269|PubMed:21473985}.Q13769THOC5THO complex subunit 5 homologSUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000305}. Cytoplasm {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm.hmonocyte differentiation [GO:0030224]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; negative regulation of DNA damage checkpoi< nt [GO:2000002]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; primitive hemopoiesis [GO:0060215]; RNA splicing [GO:0008380]; viral mRNA export from host cell nucleus [GO:0046784]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; THO complex [GO:0000347]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346]FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.; FUNCTION: Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development.P04179SODM(Superoxide dismutase [Mn], mitochondrial&age-dependent response to reactive oxygen species [GO:0001315]; negative regulation of cell proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; oxygen homeostasis [GO:0032364]; protein homotetramerization [GO:0051289]; regulation of blood pressure [GO:0008217]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; release of cytochrome c from mitochondria [GO:0001836]; removal of superoxide radicals [GO:0019430]; response to reactive oxygen species [GO:0000302]; response to superoxide [GO:0000303]; superoxide metabolic process [GO:0006801]; vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure [GO:0003069]videntical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; superoxide dismutase activity [GO:0004784]FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:10334867}.Q9Y2G8DJC16"DnaJ homolog subfamily C member 16aSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.O76021RL1D1(Ribosomal L1 domain-containing protein 1SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}. Note=Colocalizes with ING1 in the nucleolus after UV stress. {ECO:0000269|PubMed:22419112}.osteoblast differentiation [GO:0001649]; regulation of apoptotic process [GO:0042981]; regulation of cellular senescence [GO:2000772]; regulation of protein localization [GO:0032880]FUNCTION: Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}.Q00169PIPNA3Phosphatidylinositol transfer protein alpha isoformaxon guidance [GO:0007411]; lipid metabolic process [GO:0006629]; phospholipid transport [GO:0015914]; visual perception [GO:0007601]lipid binding [GO:0008289]; phosphatidylcholine transporter activity [GO:0008525]; phosphatidylinositol transporter activity [GO:0008526]Vcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]UFUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.Q9Y3X0CCDC9'Coiled-coil domain-containing protein 9P48509CD151 CD151 antigencell adhesion [GO:0007155]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581]; T cell proliferation [GO:0042098]integrin binding [GO:0005178]basement membrane [GO:0005604]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney. {ECO:0000269|PubMed:15265795}.P19634SL9A1Sodium/hydrogen exchanger 1PSUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Colocalizes with CHP1 at the reticulum endoplasmic (By similarity). Colocalizes with CHP1 and CHP2 at the plasma membrane. {ECO:0000250}.C carbohydrate metabolic process [GO:0005975]; cardiac muscle cell contraction [GO:0086003]; cardiac muscle cell differentiation [GO:0055007]; cell growth [GO:0016049]; cell migration [GO:0016477]; cellular response to acidic pH [GO:0071468]; cellular response to antibiotic [GO:0071236]; cellular response to electrical stimulus [GO:0071257]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to mechanical stimulus [GO:0071260]; cellular sodium ion homeostasis [GO:0006883]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; hydrogen ion transmembrane transport [GO:1902600]; ion transport [GO:0006811]; maintenance of cell polarity [GO:0030011]; negative regulation of apoptotic process [GO:0043066]; neuron death [GO:0070997]; positive regulation of action potential [GO:0045760]; positive regulation of apoptotic process [GO:0043065]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of calcium:sodium antiporter activity [GO:1903281]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell growth [GO:0030307]; positive regulation of mitochondrial membrane permeability [GO:0035794]; positive regulation of NFAT protein import into nucleus [GO:0051533]; positive regulation of the force of heart contraction [GO:0098735]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein oligomerization [GO:0051259]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of focal adhesion assembly [GO:0051893]; regulation of intracellular pH [GO:0051453]; regulation of pH [GO:0006885]; regulation of sensory perception of pain [GO:0051930]; regulation of stress fiber assembly [GO:0051492]; regulation of the force of heart contraction by cardiac conduction [GO:0086092]; response to acidic pH [GO:0010447]; response to drug [GO:0042493]; response to muscle stretch [GO:0035994]; small molecule metabolic process [GO:0044281]; sodium ion export [GO:0071436]; sodium ion import across plasma membrane [GO:0098719]; transmembrane transport [GO:0055085]calcium-dependent protein binding [GO:0048306]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein binding, bridging [GO:0030674]; protein complex scaffold [GO:0032947]; protein phosphatase 2B binding [GO:0030346]; sodium:proton antiporter activity [GO:0015385]; sodium:proton antiporter activity involved in regulation of cardiac muscle < cell membrane potential [GO:0086040]; solute:proton antiporter activity [GO:0015299]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cation-transporting ATPase complex [GO:0090533]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]^FUNCTION: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. {ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}.Q9NRG7D39U1 Epimerase family protein SDR39U1@FUNCTION: Putative NADP-dependent oxidoreductase. {ECO:0000305}.Q99487PAFA29Platelet-activating factor acetylhydrolase 2, cytoplasmiclipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; negative regulation of apoptotic process [GO:0043066]g1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; phospholipid binding [GO:0005543]FUNCTION: Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme.O60573IF4E22Eukaryotic translation initiation factor 4E type 2cytokine-mediated signaling pathway [GO:0019221]; in utero embryonic development [GO:0001701]; negative regulation of translation [GO:0017148]poly(A) RNA binding [GO:0044822]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]; ubiquitin protein ligase binding [GO:0031625];cytosol [GO:0005829]; mRNA cap binding complex [GO:0005845]FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.Q6XUX3DUSTY1Dual serine/threonine and tyrosine protein kinaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17123648, ECO:0000269|PubMed:23862974}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000269|PubMed:23862974}. Basolateral cell membrane {ECO:0000269|PubMed:23862974}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}. Note=Detected at apical cell-cell junctions. Colocalized with FGF receptors to the cell membrane (By similarity). Detected in basolateral and apical membranes of all tubular epithelia. {ECO:0000250|UniProtKB:Q6XUX1, ECO:0000269|PubMed:23862974}. cellular response to fibroblast growth factor stimulus [GO:0044344]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of kinase activity [GO:0033674]ATP binding [GO:0005524]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cytoplasm [GO:0005737]FUNCTION: Acts as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. {ECO:0000269|PubMed:15178406, ECO:0000269|PubMed:23862974}.O15061SYNEMSyneminSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.<intermediate filament cytoskeleton organization [GO:0045104]intermediate filament binding [GO:0019215]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]; vinculin binding [GO:0017166]adherens junction [GO:0005912]; costamere [GO:0043034]; intermediate filament [GO:0005882]; membrane [GO:0016020]; neurofilament cytoskeleton [GO:0060053]5FUNCTION: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells. {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:18028034}.Q8TEQ0SNX29Sorting nexin-29Q9H936GHC1!Mitochondrial glutamate carrier 1TL-glutamate transmembrane transport [GO:0089711]; L-glutamate transport [GO:0015813]\L-glutamate transmembrane transporter activity [GO:0005313]; symporter activity [GO:0015293]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Involved in the transport of glutamate across the inner mitochondrial membrane. Glutamate is cotransported with H(+). {ECO:0000269|PubMed:11897791}.Q8TD43TRPM4@Transient receptor potential cation channel subfamily M member 4SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum. Golgi apparatus.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum. Golgi apparatus.calcium ion transmembrane transport [GO:0070588]; cardiac conduction [GO:0061337]; dendritic cell chemotaxis [GO:0002407]; ion transmembrane transport [GO:0034220]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell proliferation [GO:0008284]; protein sumoylation [GO:0016925]; regulation of membrane potential [GO:0042391]; regulation of T cell cytokine production [GO:0002724]; transmembrane transport [GO:0055085]; vasoconstriction [GO:0042310]wATP binding [GO:0005524]; calcium activated cation channel activity [GO:0005227]; calcium channel activity [GO:0005262]endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]GFUNCTION: Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. {ECO:0000269|PubMed:12015988, ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:15121803, ECO:0000269|PubMed:15472118, ECO:0000269|PubMed:15550671, ECO:0000269|PubMed:16806463, ECO:0000269|PubMed:20625999, ECO:0000269|PubMed:20656926}.Q99439CNN2 Calponin-2actomyosin structure organization [G< O:0031032]; cellular response to mechanical stimulus [GO:0071260]; cytoskeleton organization [GO:0007010]; hemopoiesis [GO:0030097]; negative regulation of cell migration [GO:0030336]; negative regulation of phagocytosis [GO:0050765]; positive regulation of gene expression [GO:0010628]; regulation of actin filament-based process [GO:0032970]; regulation of cell proliferation [GO:0042127]; wound healing [GO:0042060]cell-cell junction [GO:0005911]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; stress fiber [GO:0001725]FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.P17812PYRG1CTP synthase 1de novo' CTP biosynthetic process [GO:0044210]; B cell proliferation [GO:0042100]; CTP biosynthetic process [GO:0006241]; glutamine metabolic process [GO:0006541]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; response to drug [GO:0042493]; small molecule metabolic process [GO:0044281]; T cell proliferation [GO:0042098]<ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity. {ECO:0000269|PubMed:16179339, ECO:0000269|PubMed:24870241}.Q96I36COX14+Cytochrome c oxidase assembly protein COX14SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:22243966, ECO:0000269|PubMed:22356826}; Single-pass membrane protein {ECO:0000269|PubMed:22243966, ECO:0000269|PubMed:22356826}.@mitochondrial respiratory chain complex IV assembly [GO:0033617]lintegral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]FUNCTION: Plays a role in the assembly or stability of the cytochrome c oxidase complex (COX). Requires for coordination of the early steps of COX assembly with the synthesis of MT-CO1. {ECO:0000269|PubMed:22243966, ECO:0000269|PubMed:22356826}.Q9HB20PKHA37Pleckstrin homology domain-containing family A member 3SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15107860}; Peripheral membrane protein {ECO:0000269|PubMed:15107860}.N1-phosphatidylinositol binding [GO:0005545]; phospholipid binding [GO:0005543]3Golgi apparatus [GO:0005794]; membrane [GO:0016020]FUNCTION: Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferentially to phosphatidylinositol 4-phosphate (PtdIns4P). {ECO:0000269|PubMed:15107860}.Q86UT6NLRX1NLR family member X1nSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313}.innate immune response [GO:0045087]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of inflammatory response [GO:0050728]; negative regulation of innate immune response [GO:0045824]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of RIG-I signaling pathway [GO:0039536]; negative regulation of type I interferon production [GO:0032480]; viral process [GO:0016032])mitochondrial outer membrane [GO:0005741]FUNCTION: Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Has no inhibitory function on NF-Kappa-B and type 1 interferon signaling pathways, but enhances NF-Kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313). {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313}.P0C7P0CISD3<CDGSH iron-sulfur domain-containing protein 3, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17376863}.M2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]A6NHR9SMHD1PStructural maintenance of chromosomes flexible hinge domain-containing protein 1[SUBCELLULAR LOCATION: Chromosome {ECO:0000250}. Note=Localizes to Barr body. {ECO:0000250}.bchromosome organization [GO:0051276]; inactivation of X chromosome by DNA methylation [GO:0060821]Barr body [GO:0001740]rFUNCTION: Required for maintenance of X inactivation in females and hypermethylation of CpG islands associated with inactive X. Involved in a pathway that mediates the methylation of a subset of CpG islands slowly and requires the de novo methyltransferase DNMT3B (By similarity). Required for DUX4 silencing in somatic cells. {ECO:0000250, ECO:0000269|PubMed:23143600}.Q8N7R7CCYL1Cyclin-Y-like protein 1Tregulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]Q9UPN9TRI33"E3 ubiquitin-protein ligase TRIM33SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}. Note=In discrete nuclear dots resembling nuclear bodies. {ECO:0000250}.#gene expression [GO:0010467]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; protein ubiquitination [GO:0016567]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]co-SMAD binding [GO:0070410]; DNA binding [GO:0003677]; ligase activity [GO:0016874]; R-SMAD binding [GO:0070412]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade). {ECO:0000250, ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}.P08579RU2B&U2 small nuclear ribonucleoprotein B''gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of defense response to virus by host [GO:0002230]; RNA splicing [GO:0008380];nucleotide binding [GO:0000166]; snRNA binding [GO:0017069]catalytic step 2 spliceosome [GO:0071013]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]FUNCTION: Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA only in presence of the U2A' protein.Q9HD34LYRM4LYR motif-containing protein 4-SUBCELLULAR LOCATION: Mitochondrion. Nucleus.-small molecule metabolic process [GO:0044281]7mitochondrial matrix [GO:0005759]; nucleus [GO:0005634]FUNCTION: Required for nuclear and mitochondrial iron-sulfur protein biosynthesis. {ECO:000< 0269|PubMed:17331979, ECO:0000269|PubMed:19454487}.Q9H267VP33B/Vacuolar protein sorting-associated protein 33BoSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:15052268}; Peripheral membrane protein; Cytoplasmic side. Lysosome membrane {ECO:0000269|PubMed:15052268}; Peripheral membrane protein; Cytoplasmic side. Early endosome {ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21411634}. Recycling endosome {ECO:0000269|PubMed:22753090}. Note=Colocalizes in clusters with VIPAS39 at cytoplasmic organelles (PubMed:19109425). Colocalizes with RAB11A and VIPAS39 on recycling endosomes (PubMed:22753090). Colocalizes with AP-3, clathrin, Rab5 and Rab7b (PubMed:21411634). Colocalizes with M.tuberculosis PtpA in the cytosol of tuberculosis-infected macrophages and associates with phagosomes (PubMed:18474358). {ECO:0000269|PubMed:18474358, ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:22753090}.lysosome localization [GO:0032418]; melanosome localization [GO:0032400]; membrane fusion [GO:0061025]; platelet alpha granule organization [GO:0070889]; protein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192].clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]; platelet alpha granule [GO:0031091]FUNCTION: May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages (PubMed:18474358). Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity). {ECO:0000250|UniProtKB:P59016, ECO:0000269|PubMed:18474358, ECO:0000305|PubMed:20190753, ECO:0000305|PubMed:23918659}.Q9NX08COMD8 COMM domain-containing protein 8O43772MCAT5Mitochondrial carnitine/acylcarnitine carrier protein|carnitine shuttle [GO:0006853]; cellular lipid metabolic process [GO:0044255]; small molecule metabolic process [GO:0044281]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]FUNCTION: Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway.Q9UI26IPO11 Importin-11eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11032817}. Nucleus {ECO:0000269|PubMed:11032817}.2ribosomal protein import into nucleus [GO:0006610])protein transporter activity [GO:0008565]dFUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBE2E3, and of RPL12 (By similarity). {ECO:0000250}.O15372EIF3H4Eukaryotic translation initiation factor 3 subunit HBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.>cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; extracellular exosome [GO:0070062]; membrane [GO:0016020]Q9UHX1PUF60%Poly(U)-binding-splicing factor PUF60SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:17579712}. Note=Colocalizes partially with TROVE2.apoptotic process [GO:0006915]; mRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]zGolgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]FUNCTION: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA. {ECO:0000269|PubMed:10606266, ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11239393, ECO:0000269|PubMed:16452196, ECO:0000269|PubMed:16628215, ECO:0000269|PubMed:17579712}.O75521ECI2*Enoyl-CoA delta isomerase 2, mitochondrialrSUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Peroxisome matrix.Qfatty acid beta-oxidation [GO:0006635]; fatty acid catabolic process [GO:0009062]xdodecenoyl-CoA delta-isomerase activity [GO:0004165]; fatty-acyl-CoA binding [GO:0000062]; receptor binding [GO:0005102]intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; peroxisomal matrix [GO:0005782]FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity). {ECO:0000250}.Q8WUD1RAB2BRas-related protein Rab-2BSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}.intracellular protein transport [GO:0006886]; positive regulation of exocytosis [GO:0045921]; Rab protein signal transduction [GO:0032482]; vesicle-mediated transport [GO:0016192]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]lFUNCTION: Required for protein transport from the endoplasmic reticulum to the Golgi complex. {ECO:0000305}.P55809SCOT1?Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial Ketone metabolismadipose tissue development [GO:0060612]; brain development [GO:0007420]; cellular ketone body metabolic process [GO:00469< 50]; cellular lipid metabolic process [GO:0044255]; heart development [GO:0007507]; ketone body catabolic process [GO:0046952]; ketone catabolic process [GO:0042182]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; response to activity [GO:0014823]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to hormone [GO:0009725]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]_3-oxoacid CoA-transferase activity [GO:0008260]; protein homodimerization activity [GO:0042803]FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.Q9UKV3ACINU7Apoptotic chromatin condensation inducer in the nucleusSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.}activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; apoptotic chromosome condensation [GO:0030263]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; erythrocyte differentiation [GO:0030218]; mRNA processing [GO:0006397]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of apoptotic process [GO:0043065]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of monocyte differentiation [GO:0045657]; programmed cell death [GO:0012501]; RNA splicing [GO:0008380]ATPase activity [GO:0016887]; enzyme binding [GO:0019899]; nucleic acid binding [GO:0003676]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]ASAP complex [GO:0061574]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]<FUNCTION: Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. {ECO:0000269|PubMed:10490026, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}.Q15121PEA15 Astrocytic phosphoprotein PEA-15CSUBCELLULAR LOCATION: Cytoplasm. Note=Associated with microtubules.apoptotic process [GO:0006915]; carbohydrate transport [GO:0008643]; DNA damage checkpoint [GO:0000077]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of glucose import [GO:0046325]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; response to morphine [GO:0043278]; transport [GO:0006810]Ccytoplasm [GO:0005737]; microtubule associated complex [GO:0005875]FUNCTION: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface. {ECO:0000250, ECO:0000269|PubMed:10442631, ECO:0000269|PubMed:9670003}.Q15036SNX17Sorting nexin-17}SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side.0cholesterol catabolic process [GO:0006707]; endosomal transport [GO:0016197]; intracellular protein transport [GO:0006886]; receptor-mediated endocytosis [GO:0006898]; regulation of endocytosis [GO:0030100]; retrograde transport, endosome to plasma membrane [GO:1990126]; signal transduction [GO:0007165]low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol binding [GO:0035091]; protein C-terminus binding [GO:0008022]; receptor binding [GO:0005102]hcytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; protein complex [GO:0043234]FUNCTION: Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). {ECO:0000269|PubMed:15121882, ECO:0000269|PubMed:15769472, ECO:0000269|PubMed:16712798, ECO:0000269|PubMed:19005208, ECO:0000269|PubMed:21512128, ECO:0000269|PubMed:22492727}.Q8IUS5EPHX4Epoxide hydrolase 4Q99460PSMD1.26S proteasome non-ATPase regulatory subunit 1P48163MAOXNADP-dependent malic enzyme=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8187880}.zcarbohydrate metabolic process [GO:0005975]; cellular lipid metabolic process [GO:0044255]; malate metabolic process [GO:0006108]; NADP biosynthetic process [GO:0006741]; protein tetramerization [GO:0051262]; regulation of NADP metabolic process [GO:1902031]; response to carbohydrate [GO:0009743]; response to hormone [GO:0009725]; small molecule metabolic process [GO:0044281]zADP binding [GO:0043531]; electron carrier activity [GO:0009055]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; malic enzyme activity [GO:0004470]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxaloacetate decarboxylase activity [GO:0008948]P42345MTOR$Serine/threonine-protein kinase mTOR kinase mTor SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB. {ECO:0000250}. de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; cardiac cell development [GO:0055006]; cell cycle arrest [GO:0007050]; cell growth [GO:0016049]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to nutr< ient levels [GO:0031669]; double-strand break repair via homologous recombination [GO:0000724]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; germ cell development [GO:0007281]; growth [GO:0040007]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; negative regulation of autophagy [GO:0010507]; negative regulation of cell size [GO:0045792]; negative regulation of macroautophagy [GO:0016242]; negative regulation of mitochondrion degradation [GO:1903147]; negative regulation of NFAT protein import into nucleus [GO:0051534]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of gene expression [GO:0010628]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription from RNA polymerase III promoter [GO:0045945]; positive regulation of translation [GO:0045727]; protein autophosphorylation [GO:0046777]; protein catabolic process [GO:0030163]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of carbohydrate utilization [GO:0043610]; regulation of cellular response to heat [GO:1900034]; regulation of fatty acid beta-oxidation [GO:0031998]; regulation of glycogen biosynthetic process [GO:0005979]; regulation of GTPase activity [GO:0043087]; regulation of myelination [GO:0031641]; regulation of osteoclast differentiation [GO:0045670]; regulation of protein kinase activity [GO:0045859]; regulation of response to food [GO:0032095]; response to amino acid [GO:0043200]; response to nutrient [GO:0007584]; response to stress [GO:0006950]; ruffle organization [GO:0031529]; signal transduction [GO:0007165]; T cell costimulation [GO:0031295]; TOR signaling [GO:0031929]; transcription initiation from RNA polymerase II promoter [GO:0006367]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; drug binding [GO:0008144]; kinase activity [GO:0016301]; phosphoprotein binding [GO:0051219]; protein dimerization activity [GO:0046983]; protein serine/threonine kinase activity [GO:0004674]; ribosome binding [GO:0043022]; RNA polymerase III type 1 promoter DNA binding [GO:0001030]; RNA polymerase III type 2 promoter DNA binding [GO:0001031]; RNA polymerase III type 3 promoter DNA binding [GO:0001032]; TFIIIC-class transcription factor binding [GO:0001156]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endomembrane system [GO:0012505]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]; PML body [GO:0016605]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]] FUNCTION: Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogensis by adjusting the expression of CEBPB isoforms (By similarity). {ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704}.P24928RPB1+DNA-directed RNA polymerase II subunit RPB17-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of RNA splicing [GO:0033120]; positive regulation of viral transcription [GO:0050434]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA-directed RNA polymerase activity [GO:0003968]; ubiquitin protein ligase binding [GO:0031625]iDNA-directed R< NA polymerase II, core complex [GO:0005665]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as an RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome. {ECO:0000269|PubMed:18032511, ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:9852112}.Q9H0P05NT3ACytosolic 5'-nucleotidase 3AgSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum._dephosphorylation [GO:0016311]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide metabolic process [GO:0009117]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside catabolic process [GO:0046135]; pyrimidine nucleoside metabolic process [GO:0006213]; small molecule metabolic process [GO:0044281]2'-phosphotransferase activity [GO:0008665]; 5'-nucleotidase activity [GO:0008253]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]lcytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]AFUNCTION: Can act both as nucleotidase and as phosphotransferase.Q96EH3MASU1;Mitochondrial assembly of ribosomal large subunit protein 1,SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16548050, ECO:0000269|PubMed:22238375, ECO:0000269|PubMed:22238376, ECO:0000269|PubMed:22829778}. Note=Colocalizes with MRPL12 (PubMed:22238375) and/or MRPL14 (PubMed:22829778). {ECO:0000269|PubMed:22238375, ECO:0000269|PubMed:22829778}.negative regulation of mitochondrial translation [GO:0070130]; negative regulation of ribosome biogenesis [GO:0090071]; ribosomal large subunit biogenesis [GO:0042273],ribosomal large subunit binding [GO:0043023]!FUNCTION: May function as a ribosomal silencing factor. Addition to isolated mitochondrial ribosomal subunits partially inhibits translation. Interacts with mitochondrial ribosomal protein L14 (MRPL14), probably blocking formation of intersubunit bridge B8, preventing association of the 28S and 39S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. May also participate in the assembly and/or regulation of the stability of the large subunit of the mitochondrial ribosome. {ECO:0000269|PubMed:22238376}.Q9BV57MTND41,2-dihydroxy-3-keto-5-methylthiopentene dioxygenaseSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the plasma membrane when complexed to MMP14. cellular nitrogen compound metabolic process [GO:0034641]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; polyamine metabolic process [GO:0006595]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]acireductone dioxygenase [iron(II)-requiring] activity [GO:0010309]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]xFUNCTION: Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line. {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:15938715}.Q14320FA50AProtein FAM50Aspermatogenesis [GO:0007283]_FUNCTION: May be a DNA-binding protein or transcriptional factor. {ECO:0000269|PubMed:9339379}.P51571SSRD+Translocon-associated protein subunit deltacellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]vextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; Sec61 translocon complex [GO:0005784]FUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.Q03518TAP1Antigen peptide transporter 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=The transmembrane segments seem to form a pore in the membrane.antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cytosol to ER transport [GO:0046967]; defense response [GO:0006952]; intracellular transport of viral protein in host cell [GO:0019060]; peptide transport [GO:0015833]; protection from natural killer cell mediated cytotoxicity [GO:0042270]; transmembrane transport [GO:0055085]ADP binding [GO:0043531]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; MHC class Ib protein binding [GO:0023029]; peptide antigen binding [GO:0042605]; peptide transporter activity [GO:0015197]; peptide-transporting ATPase activity [GO:0015440]; protein homodimerization activity [GO:0042803]; TAP1 binding [GO:0046978]; TAP2 binding [GO:0046979]endoplasmic reticulum membrane [GO:0005789]; host cell [GO:0043657]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrion [GO:0005739]; TAP complex [GO:0042825]&FUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the < transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.Q7Z2K6ERMP1(Endoplasmic reticulum metallopeptidase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6UPR8}; Multi-pass membrane protein {ECO:0000255}.Fmetal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]FUNCTION: Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. {ECO:0000250|UniProtKB:Q6UPR8}.Q9Y4E8UBP15(Ubiquitin carboxyl-terminal hydrolase 15SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:24526689}. Nucleus {ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:24526689}.BBMP signaling pathway [GO:0030509]; histone H2B conserved C-terminal lysine deubiquitination [GO:0035616]; monoubiquitinated protein deubiquitination [GO:0035520]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]; transforming growth factor beta receptor signaling pathway [GO:0007179]cysteine-type endopeptidase activity [GO:0004197]; identical protein binding [GO:0042802]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitinated histone binding [GO:0061649]; ubiquitin-specific protease activity [GO:0004843]FUNCTION: Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B (PubMed:24526689). Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway. {ECO:0000269|PubMed:16005295, ECO:0000269|PubMed:17318178, ECO:0000269|PubMed:19553310, ECO:0000269|PubMed:19576224, ECO:0000269|PubMed:19826004, ECO:0000269|PubMed:21947082, ECO:0000269|PubMed:22344298, ECO:0000269|PubMed:24526689}.Q96EQ0SGTBESmall glutamine-rich tetratricopeptide repeat-containing protein betaqFUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000250}.Q14671PUM1Pumilio homolog 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body {ECO:0000305|PubMed:20818387}. Cytoplasmic granule {ECO:0000269|PubMed:25340845}. Note=Recruited to cytoplasmic stress granules upon viral infection. {ECO:0000269|PubMed:25340845}.adult locomotory behavior [GO:0008344]; membrane organization [GO:0061024]; mRNA destabilization [GO:0061157]; positive regulation of gene silencing by miRNA [GO:2000637]; positive regulation of RIG-I signaling pathway [GO:1900246]; post-Golgi vesicle-mediated transport [GO:0006892]; posttranscriptional gene silencing [GO:0016441]; regulation of cell cycle [GO:0051726]; regulation of gene silencing by miRNA [GO:0060964]; spermatogenesis [GO:0007283]; stem cell differentiation [GO:0048863]lcytoplasmic mRNA processing body [GO:0000932]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]FUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (PubMed:21572425, PubMed:18328718, PubMed:21653694, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387, PubMed:20860814, PubMed:22345517). Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (PubMed:20818387). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery (PubMed:25768905). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem cell renewal by facilitating the exit from the ground state: acts by targeting mRNAs coding for naive pluripotency transcription factors and accelerates their down-regulation at the onset of differentiation (By similarity). {ECO:0000250|UniProtKB:Q80U78, ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:20818387, ECO:0000269|PubMed:20860814, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425, ECO:0000269|PubMed:21653694, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25768905}.Q2PZI1D19L1&Probable C-mannosyltransferase DPY19L1gintegral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]P49427UB2R1"Ubiquitin-conjugating enzyme E2 R1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.=cellular protein modification process [GO:0006464]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of cAMP-mediated signaling [GO:0043951]; positive regulation of inclusion body assembly [GO:0090261]; positive regulation of neuron apoptotic process [GO:0043525]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; response to growth factor [GO:0070848]AFUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIga< mma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes. {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10373550, ECO:0000269|PubMed:10871850, ECO:0000269|PubMed:11675391, ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:15652359, ECO:0000269|PubMed:17461777, ECO:0000269|PubMed:17698585, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19126550, ECO:0000269|PubMed:19945379, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421}.Q96CM3RUSD48RNA pseudouridylate synthase domain-containing protein 4$pseudouridine synthesis [GO:0001522]Npoly(A) RNA binding [GO:0044822]; pseudouridine synthase activity [GO:0009982]P10398ARAF%Serine/threonine-protein kinase A-Raf.cellular protein modification process [GO:0006464]; negative regulation of apoptotic process [GO:0043066]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of TOR signaling [GO:0032006]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; receptor signaling protein activity [GO:0005057]FUNCTION: Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade. {ECO:0000269|PubMed:22609986}.; FUNCTION: Isoform 2: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation. {ECO:0000269|PubMed:22609986}.O94842TOX4+TOX high mobility group box family member 4\SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20516061}. Note=Associated with chromatin.Zchromatin remodeling [GO:0006338]; regulation of transcription, DNA-templated [GO:0006355]Zchromatin [GO:0000785]; nucleoplasm [GO:0005654]; PTW/PP1 phosphatase complex [GO:0072357]FUNCTION: Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. {ECO:0000269|PubMed:20516061}.Q9BY42RTF2Protein RTF2 homologQ9UHY7ENOPHEnolase-phosphatase E1mSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.-cellular nitrogen compound metabolic process [GO:0034641]; dephosphorylation [GO:0016311]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; polyamine metabolic process [GO:0006595]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]Oacireductone synthase activity [GO:0043874]; magnesium ion binding [GO:0000287]FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). {ECO:0000255|HAMAP-Rule:MF_03117, ECO:0000269|PubMed:15843022}.Q96GK7FAH2A:Fumarylacetoacetate hydrolase domain-containing protein 2A5FUNCTION: May have hydrolase activity. {ECO:0000250}.Q8IWR0Z3H7A-Zinc finger CCCH domain-containing protein 7AQ9NSK0KLC4Kinesin light chain 4Ncytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874]Q8IY81SPB1!pre-rRNA processing protein FTSJ3SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22195017}.2enzyme-directed rRNA 2'-O-methylation [GO:0000453]Npoly(A) RNA binding [GO:0044822]; rRNA methyltransferase activity [GO:0008649]FUNCTION: Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:22195017}.Q53HC9TSSC1 Protein TSSC1Q9BZX2UCK2Uridine-cytidine kinase 2"CMP salvage [GO:0006238]; CTP salvage [GO:0044211]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside salvage [GO:0043097]; small molecule metabolic process [GO:0044281]; UMP salvage [GO:0044206]gATP binding [GO:0005524]; nucleoside kinase activity [GO:0019206]; uridine kinase activity [GO:0004849]FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.P18583SON Protein SONSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:1424986, ECO:0000269|PubMed:21504830}. Note=Colocalizes with the pre-mRNA splicing factor SRSF2. cytokinesis [GO:0000910]; microtubule cytoskeleton organization [GO:0000226]; mRNA processing [GO:0006397]; negative regulation of apoptotic process [GO:0043066]; regulation of cell cycle [GO:0051726]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]wDNA binding [GO:0003677]; nucleic acid binding [GO:0003676]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]FUNCTION: RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. {ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830}.O15305PMM2Phosphomannomutase 2bcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; GDP-mannose biosynthetic process [GO:0009298]; mannose biosynthetic process [GO:0019307]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279](phosphomannomutase activity [GO:0004615]Ycytosol [GO:0005829]; extracellular exosome [GO:0070062]; neuronal cell body [GO:0043025]FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250}.O00400ACATNAcetyl-coenzyme A transporter 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:9096318}; Multi-pass membrane protein {ECO:0000305|PubMed:9096318}.acetyl-CoA transport [GO:0015876]; BMP signaling pathway [GO:0030509]; proton transport [GO:0015992]; SMAD protein signal transduction [GO:0060395]; transmembrane transport [GO:0055085]; transport [GO:0006810][acetyl-CoA transporter activity [GO:0008521]; solute:proton symporter activity [GO:0015295]endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]FUNCTION: Probable acetyl-CoA transporter necessary for O-acetylation of gangliosides (PubMed:9096318). Negatively regulates BMP signaling (PubMed:25402622). {ECO:0000269|PubMed:25402622, ECO:0000269|PubMed:9096318}.P10599THIO Thioredoxin< SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Secreted. Note=Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus.activation of protein kinase B activity [GO:0032148]; cell-cell signaling [GO:0007267]; cell proliferation [GO:0008283]; cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; gene expression [GO:0010467]; glycerol ether metabolic process [GO:0006662]; innate immune response [GO:0045087]; movement of cell or subcellular component [GO:0006928]; negative regulation of hydrogen peroxide-induced cell death [GO:1903206]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; oxidation-reduction process [GO:0055114]; positive regulation of DNA binding [GO:0043388]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein kinase B signaling [GO:0051897]; protein folding [GO:0006457]; regulation of protein import into nucleus, translocation [GO:0033158]; response to radiation [GO:0009314]; response to reactive oxygen species [GO:0000302]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sulfate assimilation [GO:0000103]; transcription initiation from RNA polymerase II promoter [GO:0006367]oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; peptide disulfide oxidoreductase activity [GO:0015037]; poly(A) RNA binding [GO:0044822]; protein disulfide oxidoreductase activity [GO:0015035]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.; FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).Q10713MPPA0Mitochondrial-processing peptidase subunit alphacellular protein metabolic process [GO:0044267]; protein processing involved in protein targeting to mitochondrion [GO:0006627]; protein targeting to mitochondrion [GO:0006626]; proteolysis [GO:0006508]extracellular space [GO:0005615]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]P78509RELNReelinassociative learning [GO:0008306]; axon guidance [GO:0007411]; brain development [GO:0007420]; cell adhesion [GO:0007155]; cell morphogenesis involved in differentiation [GO:0000904]; central nervous system development [GO:0007417]; cerebral cortex tangential migration [GO:0021800]; dendrite development [GO:0016358]; glial cell differentiation [GO:0010001]; hippocampus development [GO:0021766]; lateral motor column neuron migration [GO:0097477]; layer formation in cerebral cortex [GO:0021819]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; neuron migration [GO:0001764]; N-methyl-D-aspartate receptor clustering [GO:0097114]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity [GO:2000969]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of excitatory postsynaptic membrane potential [GO:2000463]; positive regulation of lateral motor column neuron migration [GO:1902078]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of neuron projection development [GO:0010976]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; positive regulation of synapse maturation [GO:0090129]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of TOR signaling [GO:0032008]; postsynaptic density protein 95 clustering [GO:0097119]; receptor localization to synapse [GO:0097120]; reelin-mediated signaling pathway [GO:0038026]; regulation of behavior [GO:0050795]; regulation of N-methyl-D-aspartate selective glutamate receptor activity [GO:2000310]; regulation of synaptic transmission [GO:0050804]; response to pain [GO:0048265]; spinal cord patterning [GO:0021511]; ventral spinal cord development [GO:0021517]lipoprotein particle receptor binding [GO:0070325]; metal ion binding [GO:0046872]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; serine-type peptidase activity [GO:0008236]; very-low-density lipoprotein particle receptor binding [GO:0070326]cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]MFUNCTION: Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (By similarity). {ECO:0000250}.P13051UNGUracil-DNA glycosylaseZSUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Nucleus.+base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; depyrimidination [GO:0045008]; DNA repair [GO:0006281]; somatic hypermutation of immunoglobulin genes [GO:0016446]; somatic recombination of immunoglobulin gene segments [GO:0016447]; viral process [GO:0016032].uracil DNA N-glycosylase activity [GO:0004844]FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.P05423RPC4,DNA-directed RNA polymerase III subunit RPC4defense response to virus [GO:0051607]; gene expression [GO:0010467]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of type I interferon production [GO:0032481]; termination of RNA polymerase III transcription [GO:0006386]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription from RNA polymerase III promoter [GO:0006383]kchromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]|cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleoplasm [GO:0005654]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteri< a and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}.P38571LICH1Lysosomal acid lipase/cholesteryl ester hydrolase(cell morphogenesis [GO:0000902]; cell proliferation [GO:0008283]; cytokine production [GO:0001816]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; lipid catabolic process [GO:0016042]; lung development [GO:0030324]; tissue remodeling [GO:0048771]Clipase activity [GO:0016298]; sterol esterase activity [GO:0004771]uFUNCTION: Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation.Q0JRZ9FCHO2FCH domain only protein 2SSUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similarity). {ECO:0000250}.clathrin coat assembly [GO:0048268]; clathrin-mediated endocytosis [GO:0072583]; membrane invagination [GO:0010324]; protein localization to plasma membrane [GO:0072659]phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol binding [GO:0035091]; phosphatidylserine binding [GO:0001786][clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; plasma membrane [GO:0005886]&FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. {ECO:0000269|PubMed:17540576, ECO:0000269|PubMed:20448150, ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290}.Q8WVC6DCAKD.Dephospho-CoA kinase domain-containing proteinJcoenzyme A biosynthetic process [GO:0015937]; phosphorylation [GO:0016310]DATP binding [GO:0005524]; dephospho-CoA kinase activity [GO:0004140]Q9BXF6RFIP5"Rab11 family-interacting protein 5SUBCELLULAR LOCATION: Cytoplasm. Recycling endosome membrane; Peripheral membrane protein. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Mitochondrion membrane; Peripheral membrane protein.#cellular response to acidic pH [GO:0071468]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; negative regulation of adiponectin secretion [GO:0070164]; regulated secretory pathway [GO:0045055]; regulation of protein localization to cell surface [GO:2000008]Cgamma-tubulin binding [GO:0043015]; Rab GTPase binding [GO:0017137]cytoplasm [GO:0005737]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; microtubule organizing center [GO:0005815]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; secretory granule [GO:0030141]; transport vesicle membrane [GO:0030658].FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis. {ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:20717956}.Q92947GCDH)Glutaryl-CoA dehydrogenase, mitochondrial Amino-acid metabolismQcellular nitrogen compound metabolic process [GO:0034641]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty-acyl-CoA biosynthetic process [GO:0046949]; lipid homeostasis [GO:0055088]; lysine catabolic process [GO:0006554]; small molecule metabolic process [GO:0044281]; tryptophan metabolic process [GO:0006568]electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; glutaryl-CoA dehydrogenase activity [GO:0004361]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]dFUNCTION: Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive. {ECO:0000269|PubMed:17176108, ECO:0000269|PubMed:6423663, ECO:0000269|PubMed:8541831}.Q8WUD4CCD12(Coiled-coil domain-containing protein 12Q12768STRUM WASH complex subunit strumpellinzSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20833645}. Endoplasmic reticulum {ECO:0000269|PubMed:20833645}. Early endosome {ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}. Note=Colocalizes with SYP/synaptophysin in the external molecular layer of the dentate gyrus and in motoneurons of the ventral horn of spinal cord. {ECO:0000269|PubMed:20833645}.oocyte maturation [GO:0001556]; polar body extrusion after meiotic divisions [GO:0040038]; protein transport [GO:0015031]; spindle assembly involved in meiosis [GO:0090306]pcytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; WASH complex [GO:0071203]FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). May be involved in axonal outgrowth. Involved in cellular localization of ADRB2 (PubMed:23085491). Involved in cellular trafficking of BLOC-1 complex cargos such as ATP7A and VAMP7 (PubMed:23676666). {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:23085491, ECO:0000269|PubMed:23676666}.Q9NX76CKLF6:CKLF-like MARVEL transmembrane domain-containing protein 6chemotaxis [GO:0006935]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; membrane [GO:0016020]Q6UXH1CREL2,Cysteine-rich with EGF-like domain protein 2bSUBCELLULAR LOCATION: Secreted {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:16238698}.bendoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]QFUNCTION: May regulate transport of alpha4-beta2 neuronal acetylcholine receptor.O14979HNRDL.Heterogeneous nuclear ribonucleoprotein D-likezSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner.regulation of gene expression [GO:0010468]; regulation of transcription, DNA-templated [GO:0006355]; RNA processing [GO:0006396]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; < nucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; poly(G) binding [GO:0034046]; single-stranded DNA binding [GO:0003697]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}.Q8IYU8MICU2'Calcium uptake protein 2, mitochondrialsSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:24560927}.mitochondrial calcium ion transport [GO:0006851]; negative regulation of mitochondrial calcium ion concentration [GO:0051562]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]Rcalcium ion binding [GO:0005509]; protein heterodimerization activity [GO:0046982]calcium channel complex [GO:0034704]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; uniplex complex [GO:1990246]FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) required to limit calcium uptake by MCU when cytoplasmic calcium is low. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, respectively. MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting Ca(2+), avoiding energy dissipation and cell-death triggering. {ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927}.Q9BX67JAM3Junctional adhesion molecule CSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, desmosome. Secreted, extracellular space. Note=In epithelial cells, it is expressed at desmosomes but not at tight junctions. Localizes at the cell surface of endothelial cells; treatment of endothelial cells with vascular endothelial growth factor stimulates recruitment of JAM3 to cell-cell contacts.adaptive immune response [GO:0002250]; angiogenesis [GO:0001525]; axon regeneration [GO:0031103]; blood coagulation [GO:0007596]; cell-matrix adhesion [GO:0007160]; establishment of cell polarity [GO:0030010]; extracellular matrix organization [GO:0030198]; leukocyte migration [GO:0050900]; leukocyte migration involved in inflammatory response [GO:0002523]; myelination [GO:0042552]; myeloid progenitor cell differentiation [GO:0002318]; neutrophil homeostasis [GO:0001780]; regulation of actin cytoskeleton organization by cell-cell adhesion [GO:0090138]; regulation of neutrophil chemotaxis [GO:0090022]; spermatid development [GO:0007286]; transmission of nerve impulse [GO:0019226]8bicellular tight junction [GO:0005923]; cell-cell contact zone [GO:0044291]; desmosome [GO:0030057]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; paranodal junction [GO:0033010]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]kFUNCTION: Participates in cell-cell adhesion. It is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). The soluble form is a mediator of angiogenesis. {ECO:0000269|PubMed:12208882, ECO:0000269|PubMed:15194813, ECO:0000269|PubMed:20592283}.Q6QNY0BL1S3=Biogenesis of lysosome-related organelles complex 1 subunit 3{anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; endosome to melanosome transport [GO:0035646]; eye development [GO:0001654]; melanosome organization [GO:0032438]; melanosome transport [GO:0032402]; membrane organization [GO:0061024]; neuron projection development [GO:0031175]; pigmentation [GO:0043473]; platelet activation [GO:0030168]; platelet dense granule organization [GO:0060155]; positive regulation of natural killer cell activation [GO:0032816]; post-Golgi vesicle-mediated transport [GO:0006892]; response to drug [GO:0042493]; secretion of lysosomal enzymes [GO:0033299]QBLOC-1 complex [GO:0031083]; cytosol [GO:0005829]; transport vesicle [GO:0030133]IFUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. {ECO:0000269|PubMed:16385460, ECO:0000269|PubMed:17182842}.Q8IUH4ZDH13Palmitoyltransferase ZDHHC13USUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi vesicles. {ECO:0000250|UniProtKB:Q9CWU2}.magnesium ion transport [GO:0015693]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]magnesium ion transmembrane transporter activity [GO:0015095]; palmitoyltransferase activity [GO:0016409]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; signal transducer activity [GO:0004871]; zinc ion binding [GO:0008270]endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle membrane [GO:0030660]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]tFUNCTION: Palmitoyltransferase for HD and GAD2. May play a role in Mg(2+) transport. {ECO:0000250|UniProtKB:Q9CWU2}.Q29983MICA*MHC class I polypeptide-related sequence ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}; Single-pass type I membrane protein {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}. Cytoplasm {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}. Note=Expressed on the cell surface in gastric epithelium, endothelial cells and fibroblasts and in the cytoplasm in keratinocytes and monocytes. Infection with human adenovirus 5 suppresses cell surface expression due to the adenoviral E3-19K protein which causes retention in the endoplasmic reticulum. {ECO:0000269|PubMed:10363723, ECO:0000269|PubMed:18287244, ECO:0000269|PubMed:8901601}.\antigen processing and presentation [GO:0019882]; cellular response to DNA damage stimulus [GO:0006974]; cytolysis [GO:0019835]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; gamma-delta T cell activation [GO:0046629]; immune response to tumor cell [GO:0002418]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of natural killer cell activation [GO:0032815]; negative regulation of natural killer cell mediated cytotoxicity [GO:0045953]; response to heat [GO:0009408]; T cell mediated cytotoxicity [GO:0001913]; viral process [GO:0016032]=natural killer cell lectin-like receptor binding [GO:0046703]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]fFUNCTION: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gam< ma delta T-cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis. {ECO:0000269|PubMed:10426993, ECO:0000269|PubMed:11224526, ECO:0000269|PubMed:11491531, ECO:0000269|PubMed:11777960, ECO:0000269|PubMed:9497295}.Q14160SCRIBProtein scribble homolog.SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell junction, adherens junction. Cell projection, lamellipodium. Cytoplasm. Note=Targeting to cell-cell junctions which is CDH1-dependent is required for the pro-apoptotic activity. Localizes to neuronal post- and pre-synaptic regions.activation of GTPase activity [GO:0090630]; apoptotic process involved in morphogenesis [GO:0060561]; astrocyte cell migration [GO:0043615]; asymmetric protein localization [GO:0008105]; auditory receptor cell stereocilium organization [GO:0060088]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cochlear nucleus development [GO:0021747]; establishment of apical/basal cell polarity [GO:0035089]; mammary gland duct morphogenesis [GO:0060603]; negative regulation of mitotic cell cycle [GO:0045930]; neural tube closure [GO:0001843]; positive chemotaxis [GO:0050918]; positive regulation of apoptotic process [GO:0043065]; positive regulation of receptor recycling [GO:0001921]; protein localization to adherens junction [GO:0071896]; single organismal cell-cell adhesion [GO:0016337]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle targeting [GO:0016080]; viral process [GO:0016032]; wound healing [GO:0042060]Dbasolateral plasma membrane [GO:0016323]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; myelin sheath abaxonal region [GO:0035748]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; Scrib-APC-beta-catenin complex [GO:0034750]MFUNCTION: Scaffold protein involved in different aspects of polarized cells differentiation regulating epithelial and neuronal morphogenesis. Most probably functions in the establishment of apico-basal cell polarity. May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium. May also function in cell migration and adhesion and hence regulate cell invasion through MAPK signaling. May play a role in exocytosis and in the targeting synaptic vesicles to synapses. Functions as an activator of Rac GTPase activity. {ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15775968, ECO:0000269|PubMed:16344308, ECO:0000269|PubMed:16965391, ECO:0000269|PubMed:18641685, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.O00258WRB,Tail-anchored protein insertion receptor WRBSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:9544840}; Multi-pass membrane protein {ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:9544840}.Ftail-anchored membrane protein insertion into ER membrane [GO:0071816]nendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]FUNCTION: Receptor for ASNA1/TRC40-mediated insertion of tail-anchored (TA) proteins into the ER membrane. {ECO:0000269|PubMed:21444755}.Q96G21IMP41U3 small nucleolar ribonucleoprotein protein IMP4dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:16533400}.IrRNA primary transcript binding [GO:0042134]; snoRNA binding [GO:0030515]YMpp10 complex [GO:0034457]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]Q96B26EXOS8Exosome complex component RRP43SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17545563}. Nucleus {ECO:0000269|PubMed:17545563}. Nucleus, nucleolus {ECO:0000250}.exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; rRNA processing [GO:0006364]$AU-rich element binding [GO:0017091]cytoplasm [GO:0005737]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs. {ECO:0000269|PubMed:16912217, ECO:0000269|PubMed:17545563}.Q8IZQ5SELHSelenoprotein H?poly(A) RNA binding [GO:0044822]; selenium binding [GO:0008430]DFUNCTION: May be involved in a redox-related process. {ECO:0000305}.Q9UK41VPS286Vacuolar protein sorting-associated protein 28 homologSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11916981}. Late endosome membrane {ECO:0000269|PubMed:11916981}; Peripheral membrane protein {ECO:0000269|PubMed:11916981}.endosomal transport [GO:0016197]; intracellular transport of virus [GO:0075733]; membrane organization [GO:0061024]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of ubiquitin-dependent endocytosis [GO:2000397]; protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]Dprotein complex binding [GO:0032403]; ubiquitin binding [GO:0043130]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]xFUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. {ECO:0000269|PubMed:11916981}.Q9BX68HINT2;Histidine triad nucleotide-binding protein 2, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16762638, ECO:0000269|PubMed:18653718}.Iapoptotic process [GO:0006915]; steroid biosynthetic process [GO:0006694]@hydrolase activity [GO:0016787]; nucleotide binding [GO:0000166]FUNCTION: Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity. {ECO:0000269|PubMed:16762638, ECO:0000269|PubMed:18653718}.Q7Z7A3CTU1'Cytoplasmic tRNA 2-thiolation protein 1sprotein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble uridine modification [GO:0002098]Gnucleotidyltransferase activity [GO:0016779]; tRNA binding [GO:0000049]FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs< and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:19017811}.P51159RB27ARas-related protein Rab-27ASUBCELLULAR LOCATION: Membrane; Lipid-anchor. Melanosome. Late endosome. Lysosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles.antigen processing and presentation [GO:0019882]; blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; complement-dependent cytotoxicity [GO:0097278]; cytotoxic T cell degranulation [GO:0043316]; exocytosis [GO:0006887]; exosomal secretion [GO:1990182]; intracellular protein transport [GO:0006886]; melanocyte differentiation [GO:0030318]; melanosome localization [GO:0032400]; melanosome transport [GO:0032402]; multivesicular body organization [GO:0036257]; multivesicular body sorting pathway [GO:0071985]; natural killer cell degranulation [GO:0043320]; positive regulation of constitutive secretory pathway [GO:1903435]; positive regulation of exocytosis [GO:0045921]; positive regulation of gene expression [GO:0010628]; positive regulation of phagocytosis [GO:0050766]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of regulated secretory pathway [GO:1903307]; protein secretion [GO:0009306]; protein targeting [GO:0006605]; Rab protein signal transduction [GO:0032482]; synaptic vesicle transport [GO:0048489]; vesicle docking involved in exocytosis [GO:0006904]apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; exocytic vesicle [GO:0070382]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; melanosome [GO:0042470]; multivesicular body membrane [GO:0032585]; photoreceptor outer segment [GO:0001750]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667]; Weibel-Palade body [GO:0033093]FUNCTION: Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. {ECO:0000269|PubMed:18812475}.Q5JTD0TJAP1#Tight junction-associated protein 1SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Note=Recruited to tight junctions (TJ) during late stages of maturation of the TJ complexes. Excluded from adherens junctions and desmosomes (By similarity). {ECO:0000250}.bicellular tight junction [GO:0005923]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]P54886P5CS(Delta-1-pyrroline-5-carboxylate synthase|cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; citrulline biosynthetic process [GO:0019240]; glutamate metabolic process [GO:0006536]; L-proline biosynthetic process [GO:0055129]; ornithine biosynthetic process [GO:0006592]; proline biosynthetic process [GO:0006561]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; glutamate 5-kinase activity [GO:0004349]; glutamate-5-semialdehyde dehydrogenase activity [GO:0004350]; poly(A) RNA binding [GO:0044822]]cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]FUNCTION: Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. {ECO:0000269|PubMed:10037775, ECO:0000269|PubMed:11092761}.Q9H7Z7PGES2Prostaglandin E synthase 2SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12835322}; Single-pass membrane protein {ECO:0000269|PubMed:12835322}.; SUBCELLULAR LOCATION: Prostaglandin E synthase 2 truncated form: Cytoplasm, perinuclear region. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region.cell redox homeostasis [GO:0045454]; positive regulation of transcription, DNA-templated [GO:0045893]; prostaglandin biosynthetic process [GO:0001516]; secretion [GO:0046903]DNA binding [GO:0003677]; electron carrier activity [GO:0009055]; glutathione binding [GO:0043295]; heme binding [GO:0020037]; lyase activity [GO:0016829]; prostaglandin-E synthase activity [GO:0050220]; protein disulfide oxidoreductase activity [GO:0015035]cytosol [GO:0005829]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2). {ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:18198127}.Q96RP9EFGM"Elongation factor G, mitochondrial Protein biosynthesisFSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; organelle organization [GO:0006996]FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:19716793}.Q9NQ55SSF1Suppressor of SWI4 1 homolog-ribosomal large subunit assembly [GO:0000027];poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]_nucleolus [GO:0005730]; nucleus [GO:0005634]; preribosome, large subunit precursor [GO:0030687])FUNCTION: May have a role in cell growth.Q8TDW0LRC8C-Volume-regulated anion channel subunit LRRC8CSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.Afat cell differentiation [GO:0045444]; ion transport [GO:0006811]FUNCTION: Component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8C constitutes a pore-forming subunit or whether it is closely associated with the pore. May play a role in adipogenesis (By similarity). {ECO:0000250}.Q15011HERP1]Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 proteinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10922362}; Multi-pass membrane protein {ECO:0000269|PubMed:10922362}.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; PERK-mediated unfolded protein response [GO:0036499]; positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; positive regulation of protein binding [GO:0032092]; regulation of protein ubiquitination [GO:0031396]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]; retrograde prote< in transport, ER to cytosol [GO:0030970]; ubiquitin-dependent protein catabolic process [GO:0006511]calcium channel complex [GO:0034704]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Lewy body core [GO:1990037]; membrane [GO:0016020]FUNCTION: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated beta-amyloid protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed:18307982). {ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:18307982}.Q00403TF2B#Transcription initiation factor IIB;gene expression [GO:0010467]; regulation of transcription, DNA-templated [GO:0006355]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]core promoter binding [GO:0001047]; thyroid hormone receptor binding [GO:0046966]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]xFUNCTION: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.Q8TDD1DDX54 ATP-dependent RNA helicase DDX54]intracellular estrogen receptor signaling pathway [GO:0030520]; negative regulation of nucleic acid-templated transcription [GO:1903507]; regulation of transcription, DNA-templated [GO:0006355]; RNA metabolic process [GO:0016070]; RNA processing [GO:0006396]; RNA secondary structure unwinding [GO:0010501]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; estrogen receptor binding [GO:0030331]; poly(A) RNA binding [GO:0044822]; receptor binding [GO:0005102]; transcription corepressor activity [GO:0003714]FUNCTION: Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors. {ECO:0000269|PubMed:12466272}.Q96Q15SMG1$Serine/threonine-protein kinase SMG1eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15175154}. Cytoplasm {ECO:0000269|PubMed:15175154}.double-strand break repair via homologous recombination [GO:0000724]; gene expression [GO:0010467]; mRNA export from nucleus [GO:0006406]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; peptidyl-serine phosphorylation [GO:0018105]; phosphatidylinositol phosphorylation [GO:0046854]; protein autophosphorylation [GO:0046777]; response to stress [GO:0006950]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein dimerization activity [GO:0046983]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. {ECO:0000269|PubMed:11331269, ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:15175154, ECO:0000269|PubMed:16452507}.Q08211DHX9ATP-dependent RNA helicase ASUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm.cellular response to heat [GO:0034605]; circadian rhythm [GO:0007623]; CRD-mediated mRNA stabilization [GO:0070934]; DNA duplex unwinding [GO:0032508]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; positive regulation of type I interferon production [GO:0032481]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; ATP-dependent RNA helicase activity [GO:0004004]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; RNA helicase activity [GO:0003724]; RNA polymerase II transcription factor binding [GO:0001085]2centrosome [GO:0005813]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD-mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Positively regulates HIV-1 LTR-directed gene expression. {ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:22190748}.Q9UIW2PLXA1 Plexin-A1eSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000250}.axon guidance [GO:0007411]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; multicellular organismal development [GO:0007275]; regulation of smooth muscle cell migration [GO:0014910]Ireceptor activity [GO:0004872]; semaphorin receptor activity [GO:0017154]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity). {ECO:0000250}.Q6UXM1LRIG3>Leucine-rich repeats and immunoglobulin-like domains protein 3SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Detected in cytoplasmic vesicles when coexpressed with ERBB4. {ECO:0000250}."otolith morphogenesis [GO:0032474]cytoplasmic vesicle membrane [GO:0030659]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]&FUNCTION: May play a role in craniofacial and inner ear morphogenesis during embryonic development. May act within the otic vesicle epithelium to control formation of the lateral semicircular canal in the inner ear, possibly by restricting the expression of NTN1 (By similarity). {ECO:0000250}.O43865SAHH2!Putative adenosylhomocysteinase 2ZSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q80SW1}. Cyto< plasm, cytosol {ECO:0000250|UniProtKB:Q80SW1}. Microsome {ECO:0000250|UniProtKB:Q80SW1}. Apical cell membrane {ECO:0000250|UniProtKB:B5DFN2}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000250|UniProtKB:Q80SW1}.angiotensin-activated signaling pathway [GO:0038166]; mRNA polyadenylation [GO:0006378]; one-carbon metabolic process [GO:0006730]; positive regulation of sodium ion transport [GO:0010765]; protein export from nucleus [GO:0006611]; regulation of anion transport [GO:0044070]; regulation of ion transmembrane transporter activity [GO:0032412]; regulation of mRNA 3'-end processing [GO:0031440]; response to calcium ion [GO:0051592]; S-adenosylmethionine cycle [GO:0033353]9hydrolase activity [GO:0016787]; RNA binding [GO:0003723]apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]FUNCTION: Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). {ECO:0000250|UniProtKB:B5DFN2, ECO:0000250|UniProtKB:Q80SW1, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:16793548, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:20584908, ECO:0000269|PubMed:25237103}.Q8IUR0TPPC5.Trafficking protein particle complex subunit 5\endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; TRAPP complex [GO:0030008]Q9Y2R0COA3=Cytochrome c oxidase assembly factor 3 homolog, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23260140}; Single-pass membrane protein {ECO:0000269|PubMed:23260140}.mitochondrial respiratory chain complex IV assembly [GO:0033617]; positive regulation of mitochondrial translation [GO:0070131][integral component of mitochondrial inner membrane [GO:0031305]; mitochondrion [GO:0005739]FUNCTION: Component of some MITRAC complex, a cytochrome c oxidase (COX) assembly intermediate complex that regulates COX assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly. {ECO:0000269|PubMed:23260140}.Q9HBH5RDH14Retinol dehydrogenase 14Oosteoblast differentiation [GO:0001649]; retinol metabolic process [GO:0042572]3alcohol dehydrogenase (NADP+) activity [GO:0008106]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. No steroid dehydrogenase activity detected. {ECO:0000269|PubMed:12226107}.Q96TC7RMD3+Regulator of microtubule dynamics protein 3ASUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. Mitochondrion outer membrane. Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles.papoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cellular calcium ion homeostasis [GO:0006874]integral component of membrane [GO:0016021]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Involved in cellular calcium homeostasis regulation. May participate in differentiation and apoptosis of keratinocytes. Overexpression induces apoptosis. {ECO:0000269|PubMed:16820967, ECO:0000269|PubMed:22131369}.Q9P241AT10D,Probable phospholipid-transporting ATPase VDSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B.cation transport [GO:0006812]; intracellular protein transport [GO:0006886]; ion transmembrane transport [GO:0034220]; phospholipid translocation [GO:0045332]; transmembrane transport [GO:0055085]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). {ECO:0000305}.Q96B96TM159 PromethinQ7Z7L1SLN11Schlafen family member 11<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22927417}.qdefense response to virus [GO:0051607]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]3ATP binding [GO:0005524]; tRNA binding [GO:0000049]^aggresome [GO:0016235]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]VFUNCTION: Interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis. Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon-usage-dependent manner. Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides. The exact inhibition mechanism is unclear: may either sequesters tRNAs, prevents their maturation via post-transcriptional processing or accelerates their deacylation. Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA. May play a role in cell cycle arrest and/or induction of apoptosis in response to exogenously induced DNA damage. {ECO:0000269|PubMed:22927417, ECO:0000269|PubMed:23000900}.Q99613EIF3C4Eukaryotic translation initiation factor 3 subunit CBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.Q15796SMAD2)Mothers against decapentaplegic homolog 2R Smad<SUBCELLULAR LOCATION: Cyt< oplasm. Nucleus. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1.^activin receptor signaling pathway [GO:0032924]; anterior/posterior pattern specification [GO:0009952]; cell fate commitment [GO:0045165]; common-partner SMAD protein phosphorylation [GO:0007182]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic foregut morphogenesis [GO:0048617]; endoderm formation [GO:0001706]; gastrulation [GO:0007369]; gene expression [GO:0010467]; insulin secretion [GO:0030073]; intracellular signal transduction [GO:0035556]; in utero embryonic development [GO:0001701]; lung development [GO:0030324]; mesoderm formation [GO:0001707]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; nodal signaling pathway [GO:0038092]; organ growth [GO:0035265]; palate development [GO:0060021]; pancreas development [GO:0031016]; paraxial mesoderm morphogenesis [GO:0048340]; pericardium development [GO:0060039]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry [GO:1900224]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-embryonic development [GO:0009791]; primary miRNA processing [GO:0031053]; regulation of binding [GO:0051098]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to cholesterol [GO:0070723]; response to glucose [GO:0009749]; SMAD protein complex assembly [GO:0007183]; SMAD protein signal transduction [GO:0060395]; somatic stem cell maintenance [GO:0035019]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; zygotic specification of dorsal/ventral axis [GO:0007352]activating transcription factor binding [GO:0033613]; chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; double-stranded DNA binding [GO:0003690]; enhancer binding [GO:0035326]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; phosphatase binding [GO:0019902]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding transcription factor activity [GO:0003700]; SMAD binding [GO:0046332]; transcription factor binding [GO:0008134]; transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity [GO:0030618]; transforming growth factor beta receptor binding [GO:0005160]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin protein ligase binding [GO:0031625]$activin responsive factor complex [GO:0032444]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMAD2-SMAD3 protein complex [GO:0071144]; SMAD protein complex [GO:0071141]; transcription factor complex [GO:0005667]FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:9892009}.P80723BASP1Brain acid soluble protein 1SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection, growth cone. Note=Associated with the membranes of growth cones that form the tips of elongating axons. diaphragm development [GO:0060539]; glomerular visceral epithelial cell differentiation [GO:0072112]; gonad development [GO:0008406]; mesenchymal to epithelial transition [GO:0060231]; metanephric mesenchyme development [GO:0072075]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of heart growth [GO:0060421]; positive regulation of metanephric ureteric bud development [GO:2001076]; substantia nigra development [GO:0021762]; thorax and anterior abdomen determination [GO:0007356]protein domain specific binding [GO:0019904]; transcription corepressor activity [GO:0003714]; transcription regulatory region DNA binding [GO:0044212]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982]Q6NUK1SCMC15Calcium-binding mitochondrial carrier protein SCaMC-1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:22015608}; Multi-pass membrane protein {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:22015608}.ATP transport [GO:0015867]; cellular response to calcium ion [GO:0071277]; cellular response to oxidative stress [GO:0034599]; mitochondrial transport [GO:0006839]; regulation of cell death [GO:0010941]UATP transmembrane transporter activity [GO:0005347]; calcium ion binding [GO:0005509]FUNCTION: Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress-induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix. {ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:22015608}.Q76N32CEP68Centrosomal protein of 68 kDawSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}.centriole-centriole cohesion [GO:0010457]; centrosome organization [GO:0051297]; protein localization to organelle [GO:0033365]Qprotein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]cell junction [GO:0030054]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]P04040CATACatalaseaerobic respiration [GO:0009060]; aging [GO:0007568]; cellular response to growth factor stimulus [GO:0071363]; cholesterol metabolic process [GO:0008203]; hemoglobin metabolic process [GO:0020027]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of apoptotic process [GO:0043066]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; nucleobase-containing small molecule metabolic process [GO:0055086]; osteoblast differentiation [GO:0001649]; positive regulation of cell division [GO:0051781]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; protein homotetramerization [GO:00512< 89]; protein tetramerization [GO:0051262]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide catabolic process [GO:0006195]; response to activity [GO:0014823]; response to cadmium ion [GO:0046686]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to fatty acid [GO:0070542]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to hypoxia [GO:0001666]; response to inactivity [GO:0014854]; response to insulin [GO:0032868]; response to L-ascorbic acid [GO:0033591]; response to lead ion [GO:0010288]; response to light intensity [GO:0009642]; response to ozone [GO:0010193]; response to phenylpropanoid [GO:0080184]; response to reactive oxygen species [GO:0000302]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to vitamin E [GO:0033197]; small molecule metabolic process [GO:0044281]; triglyceride metabolic process [GO:0006641]; ureteric bud development [GO:0001657]; UV protection [GO:0009650]maminoacylase activity [GO:0004046]; antioxidant activity [GO:0016209]; catalase activity [GO:0004096]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]AFUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. {ECO:0000269|PubMed:7882369}.O00151PDLI1PDZ and LIM domain protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associates with the actin stress fibers. {ECO:0000250}.regulation of transcription, DNA-templated [GO:0006355]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]Ntranscription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]ycytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; transcription factor complex [GO:0005667]xFUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton.Q96MG8PCMD1FProtein-L-isoaspartate O-methyltransferase domain-containing protein 1Q13188STK3!Serine/threonine-protein kinase 3MAPKKKKSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between nucleus and cytoplasm (By similarity). Phosphorylation at Thr-117 leads to inhibition of nuclear translocation. {ECO:0000250, ECO:0000269|PubMed:19525978}.Kactivation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; cell differentiation involved in embryonic placenta development [GO:0060706]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; hepatocyte apoptotic process [GO:0097284]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell proliferation [GO:0008285]; negative regulation of organ growth [GO:0046621]; neural tube formation [GO:0001841]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein binding [GO:0032092]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; primitive hemopoiesis [GO:0060215]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of cell differentiation involved in embryonic placenta development [GO:0060800]; regulation of mitotic cell cycle [GO:0007346]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]6ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein dimerization activity [GO:0046983]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]OFUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38. {ECO:0000250, ECO:0000269|PubMed:15688006, ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19525978, ECO:0000269|PubMed:20212043, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:21104395, ECO:0000269|PubMed:8566796, ECO:0000269|PubMed:8816758}.O60551NMT2*Glycylpeptide N-tetradecanoyltransferase 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9506952}. Membrane {ECO:0000269|PubMed:9506952}; Peripheral membrane protein {ECO:0000269|PubMed:9506952}.lintracellular transport of virus [GO:0075733]; N-terminal peptidyl-glycine N-myristoylation [GO:0018008]; phototransduction, visible light [GO:0007603]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; rhodopsin mediated signaling pathway [GO:0016056]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9506952}.P02749APOHBeta-2-glycoprotein 1blood coagulation, intrinsic pathway [GO:0007597]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood coagulation [GO:00301< 95]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of myeloid cell apoptotic process [GO:0033033]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; organ regeneration [GO:0031100]; plasminogen activation [GO:0031639]; positive regulation of blood coagulation [GO:0030194]; positive regulation of lipoprotein lipase activity [GO:0051006]; regulation of fibrinolysis [GO:0051917]; triglyceride metabolic process [GO:0006641]; triglyceride transport [GO:0034197]glycoprotein binding [GO:0001948]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipoprotein lipase activator activity [GO:0060230]; phospholipid binding [GO:0005543]cell surface [GO:0009986]; chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.Q969Z3,Mitochondrial amidoxime reducing component 2jSUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome {ECO:0000250}.detoxification of nitrogen compound [GO:0051410]; nitrate metabolic process [GO:0042126]; oxidation-reduction process [GO:0055114]molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase activity [GO:0008940]; pyridoxal phosphate binding [GO:0030170]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]VFUNCTION: As a component of the benzamidoxime prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. {ECO:0000269|PubMed:21029045}.Q96AC1FERM2Fermitin family homolog 20SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250}. Cell surface {ECO:0000250}. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides.cell junction assembly [GO:0034329]; cell-matrix adhesion [GO:0007160]; focal adhesion assembly [GO:0048041]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; protein localization to membrane [GO:0072657]; regulation of cell shape [GO:0008360]; substrate adhesion-dependent cell spreading [GO:0034446]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055]=phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]lcell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; I band [GO:0031674]; lamellipodium membrane [GO:0031258]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; stress fiber [GO:0001725]FUNCTION: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling. {ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18458155, ECO:0000269|PubMed:21325030, ECO:0000269|PubMed:22030399, ECO:0000269|PubMed:22078565, ECO:0000269|PubMed:22699938}.O95164UBL3Ubiquitin-like protein 3\extracellular exosome [GO:0070062]; intracellular [GO:0005622]; plasma membrane [GO:0005886]Q9UJ14GGT7Gamma-glutamyltransferase 7aSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.glutathione biosynthetic process [GO:0006750]; glutathione metabolic process [GO:0006749]; leukotriene biosynthetic process [GO:0019370]\gamma-glutamyltransferase activity [GO:0003840]; glutathione hydrolase activity [GO:0036374]panchored component of external side of plasma membrane [GO:0031362]; integral component of membrane [GO:0016021]8FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}.Q8N3P4VPS85Vacuolar protein sorting-associated protein 8 homologCSUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:25266290}.%endosomal vesicle fusion [GO:0034058]early endosome [GO:0005769]FUNCTION: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:25266290). Functions predominantly in APPL1-containing endosomes (PubMed:25266290). {ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}.P50851LRBA;Lipopolysaccharide-responsive and beige-like anchor proteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Lysosome {ECO:0000250}.<cytoplasmic membrane-bounded vesicle [GO:0016023]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: May be involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules. {ECO:0000250}.Q9NW82WDR70WD repeat-containing protein 70Q96P48ARAP1JArf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1$SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cell membrane. Note=Associated with Golgi stacks in resting cells. Throughout the cytoplasm and in surface protrusion in cells that are in the process of attaching to a surface and spreading.actin filament reorganization involved in cell cycle [GO:0030037]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of receptor recycling [GO:0001921]; regulation of cell shape [GO:0008360]; regulation of cellular component movement [GO:0051270]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]GTPase activator activity [GO:0005096]; metal ion < binding [GO:0046872]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity). {ECO:0000250}.Q6VMQ6MCAF17Activating transcription factor 7-interacting protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19106100}.chromatin organization [GO:0006325]; DNA methylation [GO:0006306]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045898]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]MATPase activity [GO:0016887]; transcription corepressor activity [GO:0003714]qcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells. {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:19106100}.Q86VM9ZCH18-Zinc finger CCCH domain-containing protein 18P08133ANXA6 Annexin A6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.apoptotic signaling pathway [GO:0097190]; calcium ion transport [GO:0006816]; ion transmembrane transport [GO:0034220]; mitochondrial calcium ion homeostasis [GO:0051560]; protein homooligomerization [GO:0051260]; regulation of muscle contraction [GO:0006937]=calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; cholesterol binding [GO:0015485]; GTP binding [GO:0005525]; ligand-gated ion channel activity [GO:0015276]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]`FUNCTION: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.Q9P209CEP72Centrosomal protein of 72 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:19536135}. Note=Localizes to the centrosome and centrosome-surrounding particles throughout the cell cycle. These particles disappear after microtubules are depolymerized using nocodazole, suggesting that CEP72-associating particles localize in a microtubule- dependent manner.G2/M transition of mitotic cell cycle [GO:0000086]; gamma-tubulin complex localization [GO:0033566]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; spindle organization [GO:0007051]-centrosome [GO:0005813]; cytosol [GO:0005829]FUNCTION: Involved in the recruitment of key centrosomal proteins to the centrosome. Provides centrosomal microtubule-nucleation activity on the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles in forming a focused bipolar spindle, which is needed for proper tension generation between sister chromatids. Required for localization of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs). {ECO:0000269|PubMed:19536135}.Q13164MK07"Mitogen-activated protein kinase 7nSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body. Note=Translocates to the nucleus upon activation.cAMP-mediated signaling [GO:0019933]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to transforming growth factor beta stimulus [GO:0071560]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of cAMP catabolic process [GO:0030821]; negative regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051344]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of NFAT protein import into nucleus [GO:0051534]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of response to cytokine stimulus [GO:0060761]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter in response to stress [GO:0036003]; regulation of angiogenesis [GO:0045765]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]qATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; mitogen-activated protein kinase binding [GO:0051019]scytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction. {ECO:0000269|PubMed:11254654, ECO:0000269|PubMed:11278431, ECO:0000269|PubMed:22869143, ECO:0000269|PubMed:9384584, ECO:0000269|PubMed:9790194}.< Q96HS1PGAM59Serine/threonine-protein phosphatase PGAM5, mitochondrialhSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18387606}; Single-pass membrane protein {ECO:0000269|PubMed:18387606}. Note=Isoform 2 overexpression results in the formation of disconnected punctuate mitochondria distributed throughout the cytoplasm. Isoform 1 overexpression results in the clustering of mitochondria around the nucleus.dephosphorylation [GO:0016311]; intracellular signal transduction [GO:0035556]; necroptotic process [GO:0070266]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; protein localization to mitochondrion [GO:0070585]GTPase activator activity [GO:0005096]; phosphatase activity [GO:0016791]; protein complex binding [GO:0032403]; receptor signaling protein serine/threonine phosphatase activity [GO:0009400]'FUNCTION: Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore. {ECO:0000269|PubMed:18387606, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:22265414}.Q5TGZ0MIC10MICOS complex subunit MIC10 SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:22114354}; Single-pass membrane protein {ECO:0000269|PubMed:22114354}. Note=The C-terminus is located in the intermembrane space (By similarity), while the location of the N-terminus has not been determined yet. As some programs predict the presence of 2 closely apposed membrane domains, it has been proposed that the protein may cross the membrane twice and that both termini may face the intermembrane space (PubMed:22114354). {ECO:0000250, ECO:0000269|PubMed:22114354}.FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. {ECO:0000269|PubMed:22114354}.Q9Y2X7GIT1"ARF GTPase-activating protein GIT1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11896197}. Note=Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes towards the leading edge, while, when cells adhere, it is found in vinculin-containing adhesions. Recruitment to adhesions may be mediated by active tyrosine-phosphorylated paxillin.axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; regulation of cytokinesis [GO:0032465]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]xaggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; membrane [GO:0016020]FUNCTION: GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes. Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13 (By similarity). {ECO:0000250|UniProtKB:Q68FF6, ECO:0000269|PubMed:11896197}.Q9BPW8NIPS1Protein NipSnap homolog 1'sensory perception of pain [GO:0019233]%neurotransmitter binding [GO:0042165]emitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; synaptic membrane [GO:0097060]Q8WYK1CNTP5#Contactin-associated protein-like 5FUNCTION: May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication.Q9HBL7PLRKTPlasminogen receptor (KT)SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21940822}; Multi-pass membrane protein {ECO:0000269|PubMed:21940822}. Note=Colocalizes on the cell surface with urokinase plasminogen activator surface receptor/PLAUR. {ECO:0000250}.wchemotaxis [GO:0006935]; inflammatory response [GO:0006954]; positive regulation of plasminogen activation [GO:0010756]Nintegral component of plasma membrane [GO:0005887]; mitochondrion [GO:0005739]FUNCTION: Receptor for plasminogen. Regulates urokinase plasminogen activator-dependent and stimulates tissue-type plasminogen activator-dependent cell surface plasminogen activation. Proposed to be part of a local catecholaminergic cell plasminogen activation system that regulates neuroendocrine prohormone processing. Involved in regulation of inflammatory response; regulates monocyte chemotactic migration and matrix metallproteinase activation, such as of MMP2 and MMP9. {ECO:0000269|PubMed:21940822}.Q6Y2X3DJC14"DnaJ homolog subfamily C member 14endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. {ECO:0000250}.P26572MGAT1FAlpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferaseWcarbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; in utero embryonic development [GO:0001701]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-N-acetylglucosamine catabolic process [GO:0006049]acetylglucosaminyltransferase activity [GO:0008375]; alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity [GO:0003827]; metal ion binding [GO:0046872]extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.Q6P2H3CEP85Centrosomal protein of 85 kDa}SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21399614}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:21399614}. Nucleus, nucleolus {ECO:0000269|PubMed:21399614}. Note=Localizes to centrosomes and nucleolus in interphase. Upon entry into mitosis, relocates from nucleolus and accumulates at spindle poles.centrosome [GO:0005813]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; spindle pole [GO:0000922]P15735PHKG2BPhosphorylase b kinase gamma catalytic chain, liver/testis isoformcarbohydrate metabolic process [GO:0005975]; generation of precursor metabolites and energy [GO:0006091]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; positive regulation of glycogen catabolic process [GO:0045819]; protein phosphorylation [GO:0006468]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; phosphorylase kinase activity [GO:0004689]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]?cytosol [GO:0005829]; phosphorylase kinase complex [GO:0005964]EFUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro,< phosphorylates PYGM (By similarity). {ECO:0000250}.Q9Y534CSDC2'Cold shock domain-containing protein C2SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=PIPPin-RNA complexes are located to the nucleus. {ECO:0000250}.UmRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]2DNA binding [GO:0003677]; RNA binding [GO:0003723]#FUNCTION: RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). {ECO:0000250}.O75084FZD7 Frizzled-7SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. canonical Wnt signaling pathway [GO:0060070]; cellular response to retinoic acid [GO:0071300]; mesenchymal to epithelial transition [GO:0060231]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of ectodermal cell fate specification [GO:0042666]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway via JNK cascade [GO:0038031]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of catenin import into nucleus [GO:0035412]; regulation of transcription, DNA-templated [GO:0006355]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; somatic stem cell division [GO:0048103]; stem cell maintenance [GO:0019827]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell differentiation in thymus [GO:0033077]frizzled binding [GO:0005109]; G-protein coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]; Wnt-activated receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.P43007SATT Neutral amino acid transporter ASUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17081065}; Multi-pass membrane protein {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.nactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; amino acid transport [GO:0006865]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; cognition [GO:0050890]; glutamine transport [GO:0006868]; hydroxyproline transport [GO:0034589]; ion transport [GO:0006811]; L-alanine transport [GO:0015808]; L-cystine transport [GO:0015811]; L-serine transport [GO:0015825]; proline transmembrane transport [GO:0035524]; proline transport [GO:0015824]; synaptic transmission, glutamatergic [GO:0035249]; threonine transport [GO:0015826]; transmembrane transport [GO:0055085]chloride channel activity [GO:0005254]; L-alanine transmembrane transporter activity [GO:0015180]; L-cystine transmembrane transporter activity [GO:0015184]; L-glutamine transmembrane transporter activity [GO:0015186]; L-hydroxyproline transmembrane transporter activity [GO:0034590]; L-proline transmembrane transporter activity [GO:0015193]; L-serine transmembrane transporter activity [GO:0015194]; L-threonine transmembrane transporter activity [GO:0015195]; sodium:dicarboxylate symporter activity [GO:0017153]cell surface [GO:0009986]; centrosome [GO:0005813]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; intermediate filament [GO:0005882]; melanosome [GO:0042470]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]_FUNCTION: Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence.Q96SW2CRBNProtein cereblonSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20223979}. Nucleus {ECO:0000269|PubMed:20223979}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.<negative regulation of ion transmembrane transport [GO:0034766]; negative regulation of protein homooligomerization [GO:0032463]; positive regulation of protein homodimerization activity [GO:0090073]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]MATP-dependent peptidase activity [GO:0004176]; metal ion binding [GO:0046872]Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. Binding of pomalidomide and other thalidomide-related drugs changes the substrate specificity of the human protein, leading to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3. {ECO:0000269|PubMed:18414909, ECO:0000269|PubMed:20223979, ECO:0000269|PubMed:24328678, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, ECO:0000305}.P62745RHOB$Rho-related GTP-binding protein RhoBaSUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Nucleus. Cleavage furrow. Note=Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to ionizing radiation [GO:0071479]; cytokinesis [GO:0000910]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; negative regulation of cell cycle [GO:0045786]; platelet activation [GO:0030168]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic process [GO:0043065]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; transformed cell apoptotic process [GO:0006927] cleavage furrow [GO:0032154]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; late endosome membrane [GO:0031902]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a < negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells. {ECO:0000269|PubMed:10508588, ECO:0000269|PubMed:15226397, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:21373644, ECO:0000269|PubMed:9478917}.Q8N5M9JAGN1Protein jagunal homolog 1~SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25129144}; Multi-pass membrane protein {ECO:0000255}.wdefense response to fungus [GO:0050832]; endoplasmic reticulum organization [GO:0007029]; exocytosis [GO:0006887]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; neutrophil differentiation [GO:0030223]; neutrophil mediated immunity [GO:0002446]; neutrophil migration [GO:1990266]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]|endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]FUNCTION: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil function, probably via its role in vesicle-mediated transport: required for defense against fungal pathogens and for granulocyte colony-stimulating factor (GM-CSF) signaling pathway; possibly by regulating glycosylation and/or targeting of proteins contributing to the viability and migration of neutrophils. {ECO:0000269|PubMed:25129144, ECO:0000305}.P30825CTR1/High affinity cationic amino acid transporter 1}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10485994}; Multi-pass membrane protein {ECO:0000303|PubMed:10485994}.amino acid transport [GO:0006865]; ion transport [GO:0006811]; L-arginine import across plasma membrane [GO:0097638]; L-lysine transmembrane transport [GO:1903401]; L-ornithine transmembrane transport [GO:1903352]; transmembrane transport [GO:0055085]; transport [GO:0006810]antiporter activity [GO:0015297]; arginine transmembrane transporter activity [GO:0015181]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]gintegral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues. May also function as an ecotropic retroviral leukemia receptor. {ECO:0000269|PubMed:10485994}.P68402PA1B2:Platelet-activating factor acetylhydrolase IB subunit betabrain development [GO:0007420]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; positive regulation of macroautophagy [GO:0016239]; spermatogenesis [GO:0007283]1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; platelet-activating factor acetyltransferase activity [GO:0047179]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]iFUNCTION: Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.P84157MXRA7&Matrix-remodeling-associated protein 7Q07812BAXApoptosis regulator BAXSUBCELLULAR LOCATION: Isoform Alpha: Mitochondrion membrane; Single-pass membrane protein. Cytoplasm. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane.; SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm.; SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm.; SUBCELLULAR LOCATION: Isoform Delta: Cytoplasm {ECO:0000305}.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of signaling protein activity involved in unfolded protein response [GO:0006987]; apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; apoptotic process involved in patterning of blood vessels [GO:1902262]; apoptotic signaling pathway [GO:0097190]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; B cell homeostatic proliferation [GO:0002358]; B cell negative selection [GO:0002352]; B cell receptor apoptotic signaling pathway [GO:1990117]; blood vessel remodeling [GO:0001974]; cellular respiration [GO:0045333]; cellular response to UV [GO:0034644]; cerebral cortex development [GO:0021987]; development of secondary sexual characteristics [GO:0045136]; ectopic germ cell programmed cell death [GO:0035234]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; fertilization [GO:0009566]; germ cell development [GO:0007281]; glial cell apoptotic process [GO:0034349]; glycosphingolipid metabolic process [GO:0006687]; homeostasis of number of cells within a tissue [GO:0048873]; hypothalamus development [GO:0021854]; inner mitochondrial membrane organization [GO:0007007]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial fusion [GO:0008053]; mitochondrion morphogenesis [GO:0070584]; myeloid cell homeostasis [GO:0002262]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of protein binding [GO:0032091]; neuron apoptotic process [GO:0051402]; neuron migration [GO:0001764]; odontogenesis of dentin-containing tooth [GO:0042475]; outer mitochondrial membrane organization [GO:0007008]; ovarian follicle development [GO:0001541]; positive regulation of apoptotic DNA fragmentation [GO:1902512]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic process involved in mammary gland involution [GO:0060058]; positive regulation of B cell apoptotic process [GO:0002904]; positive regulation of developmental pigmentation [GO:0048087]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein oligo< merization [GO:0032461]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; post-embryonic camera-type eye morphogenesis [GO:0048597]; programmed cell death [GO:0012501]; protein homooligomerization [GO:0051260]; protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:0001844]; protein oligomerization [GO:0051259]; regulation of cell cycle [GO:0051726]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of mitochondrial membrane permeability involved in programmed necrotic cell death [GO:1902445]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of nitrogen utilization [GO:0006808]; regulation of protein heterodimerization activity [GO:0043497]; regulation of protein homodimerization activity [GO:0043496]; release of cytochrome c from mitochondria [GO:0001836]; release of matrix enzymes from mitochondria [GO:0032976]; response to axon injury [GO:0048678]; response to cocaine [GO:0042220]; response to copper ion [GO:0046688]; response to corticosterone [GO:0051412]; response to drug [GO:0042493]; response to gamma radiation [GO:0010332]; response to salt stress [GO:0009651]; response to toxic substance [GO:0009636]; retina development in camera-type eye [GO:0060041]; retinal cell apoptotic process [GO:1990009]; retinal cell programmed cell death [GO:0046666]; Sertoli cell proliferation [GO:0060011]; spermatid differentiation [GO:0048515]; T cell homeostatic proliferation [GO:0001777]; thymocyte apoptotic process [GO:0070242]; transformed cell apoptotic process [GO:0006927]; vagina development [GO:0060068]; viral process [GO:0016032]BH3 domain binding [GO:0051434]; channel activity [GO:0015267]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]BAX complex [GO:0097144]; Bcl-2 family protein complex [GO:0097136]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrial permeability transition pore complex [GO:0005757]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; pore complex [GO:0046930]-FUNCTION: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. {ECO:0000269|PubMed:10772918, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:18948948, ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:8358790, ECO:0000269|PubMed:8521816}.Q6NUP7PP4R4;Serine/threonine-protein phosphatase 4 regulatory subunit 4>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18715871}.negative regulation of phosphoprotein phosphatase activity [GO:0032515]; regulation of protein serine/threonine phosphatase activity [GO:0080163]3protein phosphatase regulator activity [GO:0019888]Qcytoplasm [GO:0005737]; protein serine/threonine phosphatase complex [GO:0008287]PFUNCTION: Putative regulatory subunit of serine/threonine-protein phosphatase 4.O14744ANM5&Protein arginine N-methyltransferase 5cell proliferation [GO:0008283]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; endothelial cell activation [GO:0042118]; gene expression [GO:0010467]; histone arginine methylation [GO:0034969]; histone H4-R3 methylation [GO:0043985]; liver regeneration [GO:0097421]; ncRNA metabolic process [GO:0034660]; negative regulation of cell differentiation [GO:0045596]; negative regulation of nucleic acid-templated transcription [GO:1903507]; peptidyl-arginine methylation [GO:0018216]; peptidyl-arginine methylation, to symmetrical-dimethyl arginine [GO:0019918]; peptidyl-arginine N-methylation [GO:0035246]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of DNA methylation [GO:0044030]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of mitotic nuclear division [GO:0007088]; regulation of transcription, DNA-templated [GO:0006355]; spliceosomal snRNP assembly [GO:0000387]; transcription, DNA-templated [GO:0006351]|core promoter sequence-specific DNA binding [GO:0001046]; histone-arginine N-methyltransferase activity [GO:0008469]; methyltransferase activity [GO:0008168]; protein-arginine omega-N symmetric methyltransferase activity [GO:0035243]; protein heterodimerization activity [GO:0046982]; ribonucleoprotein complex binding [GO:0043021]; transcription corepressor activity [GO:0003714]cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone methyltransferase complex [GO:0035097]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter. {ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:12411503, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951}.Q9H1P3OSBL2+Oxysterol-binding protein-related protein 2FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (PubMed:11279184). Binds 25-hydroxycholesterol (PubMed:17428193). {ECO:0000269|PubMed:11279184, ECO:0000269|PubMed:17428193}.Q96CD0FBXL8F-box/LRR-repeat protein 8FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. {ECO:0000250}.Q86VI1EX3L1(Exocyst complex component 3-like proteinSUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Colocalizes with insulin granules. {ECO:0000250}.bexocyst localization [GO:0051601]; exocytosis [GO:0006887]; peptide hormone secretion [GO< :0030072]Texocyst [GO:0000145]; secretory granule [GO:0030141]; transport vesicle [GO:0030133]mFUNCTION: As part of the exocyst, may play a role in regulated exocytosis of insulin granules. {ECO:0000250}.Q5VYK3ECM29+Proteasome-associated protein ECM29 homologSUBCELLULAR LOCATION: Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate compartment. Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Endosome, multivesicular body. Cytoplasmic vesicle.centrosome [GO:0005813]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ER to Golgi transport vesicle [GO:0030134]; late endosome [GO:0005770]; membrane [GO:0016020]; multivesicular body [GO:0005771]; nucleus [GO:0005634]; proteasome complex [GO:0000502]`FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome, motor proteins and other compartment specific proteins. May couple the proteasome to different compartments including endosome, endoplasmic reticulum and centrosome. May play a role in ERAD and other enhanced proteolyis. {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:20682791}.Q9NQX3GEPHGephyrin;SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Cytoplasmic face of glycinergic postsynaptic membranes. {ECO:0000250}.establishment of synaptic specificity at neuromuscular junction [GO:0007529]; glycine receptor clustering [GO:0072579]; molybdenum incorporation into molybdenum-molybdopterin complex [GO:0018315]; molybdopterin cofactor biosynthetic process [GO:0032324]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin adenylyltransferase activity [GO:0061598]; molybdopterin molybdotransferase activity [GO:0061599]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]FUNCTION: Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. {ECO:0000250}.Q7Z7M9GALT5/Polypeptide N-acetylgalactosaminyltransferase 5cellular protein metabolic process [GO:0044267]; glycosaminoglycan biosynthetic process [GO:0006024]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]CFUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity). {ECO:0000250}.Q9UKY4POMT2 Protein O-mannosyl-transferase 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12460945, ECO:0000269|PubMed:14699049}; Multi-pass membrane protein {ECO:0000269|PubMed:12460945, ECO:0000269|PubMed:14699049}.ldolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; metal ion binding [GO:0046872]FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. {ECO:0000269|PubMed:14699049}.O43252PAPS1=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1Sulfur metabolism3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]; sulfate assimilation [GO:0000103]; xenobiotic metabolic process [GO:0006805]adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; sulfate adenylyltransferase (ATP) activity [GO:0004781]hFUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells.O14867BACH1%Transcription regulator protein BACH1ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.DNA repair [GO:0006281]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; regulation of transcription involved in G2/M transition of mitotic cell cycle [GO:0000117]heme binding [GO:0020037]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001206]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Transcriptional regulator that acts as repressor or activator. Binds, in vitro, to NF-E2 binding sites. Play important roles in coordinating transcription activation and repression by MAFK.Q9C0C9UBE2O+E2/E3 hybrid ubiquitin-protein ligase UBE2OSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24703950}. Nucleus {ECO:0000269|PubMed:24703950}. Note=Mainly localizes to the cytoplasm.positive regulation of BMP signaling pathway [GO:0030513]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; retrograde transport, endosome to Golgi [GO:0042147] ATP binding [GO:0005524]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]+FUNCTION: E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting th< eir subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853). {ECO:0000269|PubMed:23381138, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:23455153, ECO:0000269|PubMed:24703950}.Q9BRR6ADPGKADP-dependent glucokinaseglycolytic process [GO:0006096]NADP-specific glucokinase activity [GO:0043843]; metal ion binding [GO:0046872]\endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency (By similarity). {ECO:0000250}.O95861BPNT1%3'(2'),5'-bisphosphate nucleotidase 1Y3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; dephosphorylation [GO:0016311]; nervous system development [GO:0007399]; nucleobase-containing compound metabolic process [GO:0006139]; phosphatidylinositol phosphorylation [GO:0046854]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]Y3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; metal ion binding [GO:0046872]FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. {ECO:0000269|PubMed:10224133}.Q96KG9NTKLN-terminal kinase-like proteinmSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18556652}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:18556652}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18556652}. Note=Localized to the Endoplasmic reticulum-Golgi intermediate and cis-Golgi in an ARF1-independent manner.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Cytoplasmic throughout the cell cycle.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Cytoplasmic throughout the cell cycle.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic during interphase and centrosomal during mitosis, it localizes to the centrosomes in a microtubule-independent manner.; SUBCELLULAR LOCATION: Isoform 6: Nucleus {ECO:0000269|PubMed:15504359}.peptidyl-tyrosine phosphorylation [GO:0018108]; regulation of transcription, DNA-templated [GO:0006355]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; transcription, DNA-templated [GO:0006351]aATP binding [GO:0005524]; DNA binding [GO:0003677]; protein tyrosine kinase activity [GO:0004713]cis-Golgi network [GO:0005801]; COPI vesicle coat [GO:0030126]; cytoplasm [GO:0005737]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]|FUNCTION: Regulates COPI-mediated retrograde traffic. Has no detectable kinase activity in vitro. {ECO:0000269|PubMed:18556652}.; FUNCTION: Isoform 6 acts as transcriptional activator. It binds to three different types of GC-rich DNA binding sites (box-A, -B and -C) in the beta-polymerase promoter region. It also binds to the TERT promoter region. {ECO:0000269|PubMed:18556652}.P61086UBE2K!Ubiquitin-conjugating enzyme E2 Kpintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; ubiquitin-dependent protein catabolic process [GO:0006511]ATP binding [GO:0005524]; ligase activity [GO:0016874]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-ubiquitin ligase activity [GO:0034450]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; filopodium tip [GO:0032433]; intermediate filament cytoskeleton [GO:0045111]; nucleus [GO:0005634]6FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1. {ECO:0000269|PubMed:10634809, ECO:0000269|PubMed:10675012, ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:16868077, ECO:0000269|PubMed:17873885, ECO:0000269|PubMed:19906396, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:8702625}.P17081RHOQ$Rho-related GTP-binding protein RhoQSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15546864}. Cell membrane {ECO:0000269|PubMed:15546864}; Lipid-anchor {ECO:0000269|PubMed:15546864}.cellular response to insulin stimulus [GO:0032869]; cortical actin cytoskeleton organization [GO:0030866]; GTP metabolic process [GO:0046039]; insulin receptor signaling pathway [GO:0008286]; negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of glucose import [GO:0046326]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]vGBD domain binding [GO:0032427]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; profilin binding [GO:0005522]actin filament [GO:0005884]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi-associated vesicle membrane [GO:0030660]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia. {ECO:0000269|PubMed:15546864}.Q9NP79VTA18Vacuolar protein sorting-associated protein VTA1 homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15644320}. Endosome membrane {ECO:0000305|PubMed:15644320}; Peripheral membrane protein {ECO:0000305|PubMed:15644320}.endosomal transport [GO:0016197]; membrane organization [GO:0061024]; multivesicular body sorting pathway [GO:0071985]; protein transport [GO:0015031]; viral budding [GO:0046755]; viral life cycle [GO:0019058]; viral process [GO:0016032]Xcytosol [GO:0005829]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]`FUNCTION: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane o< f the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding. {ECO:0000250, ECO:0000269|PubMed:15644320}.O15173PGRC25Membrane-associated progesterone receptor component 27steroid hormone mediated signaling pathway [GO:0043401]gheme binding [GO:0020037]; steroid binding [GO:0005496]; steroid hormone receptor activity [GO:0003707]dendomembrane system [GO:0012505]; integral component of membrane [GO:0016021]; membrane [GO:0016020]/FUNCTION: Receptor for steroids. {ECO:0000305}.Q9Y6D5BIG2;Brefeldin A-inhibited guanine nucleotide-exchange protein 2SUBCELLULAR LOCATION: Cytoplasm. Membrane. Golgi apparatus. Cytoplasm, perinuclear region. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, dendrite {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Translocates from cytoplasm to membranes upon cAMP treatment. Localized in recycling endosomes.endomembrane system organization [GO:0010256]; endosome organization [GO:0007032]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; intracellular signal transduction [GO:0035556]; positive regulation of GTPase activity [GO:0043547]; positive regulation of tumor necrosis factor production [GO:0032760]; protein transport [GO:0015031]; receptor recycling [GO:0001881]; regulation of ARF protein signal transduction [GO:0032012]ARF guanyl-nucleotide exchange factor activity [GO:0005086]; GABA receptor binding [GO:0050811]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase A regulatory subunit binding [GO:0034237]asymmetric synapse [GO:0032279]; axonemal microtubule [GO:0005879]; cell junction [GO:0030054]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; symmetric synapse [GO:0032280]; trans-Golgi network [GO:0005802]RFUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extend on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking from the trans-Golgi network (TGN) to endosomes and is required for membrane association of the AP-1 complex and GGA1. Seems to be involved in recycling of the transferrin receptor from recycling endosomes to the plasma membrane. Probably is involved in the exit of GABA(A) receptors from the endoplasmic reticulum. Involved in constitutive release of tumor necrosis factor receptor 1 via exosome-like vesicles; the function seems to involve PKA and specifically PRKAR2B. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. {ECO:0000269|PubMed:12051703, ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15385626, ECO:0000269|PubMed:16477018, ECO:0000269|PubMed:17276987, ECO:0000269|PubMed:18625701, ECO:0000269|PubMed:20360857}.Q8NB91FANCBFanconi anemia group B proteinFanconi anemia<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15502827}.DNA repair [GO:0006281]FFanconi anaemia nuclear complex [GO:0043240]; nucleoplasm [GO:0005654]_FUNCTION: DNA repair protein required for FANCD2 ubiquitination. {ECO:0000269|PubMed:15502827}.P35240MERLMerlinbSUBCELLULAR LOCATION: Isoform 1: Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=In a fibroblastic cell line, isoform 1 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia. Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with VPRBP in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions.; SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 7 is absent from ruffling membranes and filopodia.; SUBCELLULAR LOCATION: Isoform 9: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 9 is absent from ruffling membranes and filopodia.; SUBCELLULAR LOCATION: Isoform 10: Nucleus. Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasmic granule. Cytoplasm, cytoskeleton. Note=In a fibroblastic cell line, isoform 10 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia.\actin cytoskeleton organization [GO:0030036]; cell-cell junction organization [GO:0045216]; ectoderm development [GO:0007398]; hippocampus development [GO:0021766]; lens fiber cell differentiation [GO:0070306]; mesoderm formation [GO:0001707]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cell growth [GO:0030308]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of DNA replication [GO:0008156]; negative regulation of JAK-STAT cascade [GO:0046426]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of tyrosine phosphorylation of Stat3 protein [GO:0042518]; negative regulation of tyrosine phosphorylation of Stat5 protein [GO:0042524]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of cell differentiation [GO:0045597]; positive regulation of stress fiber assembly [GO:0051496]; regulation of hippo signaling [GO:0035330]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of protein localization to nucleus [GO:1900180]; regulation of protein stability [GO:0031647]; Schwann cell proliferation [GO:0014010]; small GTPase mediated signal transduction [GO:0007264]Cadherens junction [GO:0005912]; apical part of cell [GO:0045177]; cleavage furrow [GO:0032154]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; early endosome [GO:0005769]; extrinsic component of membrane [GO:0019898]; filopodium membrane [GO:0031527]; lamellipodium [GO:0030027]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; ruffle membrane [GO:0032587]; synapse [GO:0045202]FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|P< ubMed:20159598, ECO:0000269|PubMed:20178741}.Q9Y3S2ZN330Zinc finger protein 330*SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10593942}. Nucleus, nucleolus {ECO:0000269|PubMed:10593942}. Chromosome, centromere {ECO:0000269|PubMed:10593942}. Note=Predominantly expressed in the nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis.=metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]Ychromosome, centromeric region [GO:0000775]; midbody [GO:0030496]; nucleolus [GO:0005730]Q96SY0VWA93von Willebrand factor A domain-containing protein 9Q6UX72B3GN9=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9qSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}."protein glycosylation [GO:0006486]+galactosyltransferase activity [GO:0008378]Q96K37S35E1"Solute carrier family 35 member E1]anion transmembrane transport [GO:0098656]; carbohydrate transmembrane transport [GO:0034219] antiporter activity [GO:0015297]O15066KIF3BKinesin-like protein KIF3BEanterograde axon cargo transport [GO:0008089]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; determination of left/right symmetry [GO:0007368]; membrane organization [GO:0061024]; microtubule-based movement [GO:0007018]; mitotic centrosome separation [GO:0007100]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; organelle organization [GO:0006996]; plus-end-directed vesicle transport along microtubule [GO:0072383]; positive regulation of cytokinesis [GO:0032467]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; microtubule motor activity [GO:0003777]; Rho GTPase binding [GO:0017048]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intraciliary transport particle [GO:0030990]; kinesin II complex [GO:0016939]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; plus-end kinesin complex [GO:0005873]; primary cilium [GO:0072372]; spindle [GO:0005819]FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). {ECO:0000250}.Q8WUY8NAT14N-acetyltransferase 14vDNA-templated transcription, initiation [GO:0006352]; positive regulation of transcription, DNA-templated [GO:0045893]CDNA binding [GO:0003677]; N-acetyltransferase activity [GO:0008080]Aintegral component of membrane [GO:0016021]; nucleus [GO:0005634]FUNCTION: Probable acetyltransferase that binds the 5'-GGACTACAG-3' sequence of coproporphyrinogen oxidase promoter. Able to activate transcription of a reporter construct in vitro.P01130LDLR Low-density lipoprotein receptorSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Membrane, clathrin-coated pit; Single-pass type I membrane protein. Golgi apparatus. Early endosome. Late endosome. Cell surface. Lysosome. Note=Found distributed from the plasma membrane to intracellular compartments. Localizes to the Golgi apparatus, early and late endosomes/lysosomes and cell surface in the presence of PCSK9.Gcholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; endocytosis [GO:0006897]; intestinal cholesterol absorption [GO:0030299]; lipid metabolic process [GO:0006629]; lipoprotein catabolic process [GO:0042159]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle clearance [GO:0034383]; phospholipid transport [GO:0015914]; phototransduction, visible light [GO:0007603]; positive regulation of triglyceride biosynthetic process [GO:0010867]; receptor-mediated endocytosis [GO:0006898]; regulation of cholesterol homeostasis [GO:2000188]; regulation of phosphatidylcholine catabolic process [GO:0010899]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]; viral process [GO:0016032]#calcium ion binding [GO:0005509]; clathrin heavy chain binding [GO:0032050]; glycoprotein binding [GO:0001948]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein receptor activity [GO:0005041]; very-low-density lipoprotein particle receptor activity [GO:0030229]Lapical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; coated pit [GO:0005905]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; low-density lipoprotein particle [GO:0034362]; lysosome [GO:0005764]; membrane [GO:0016020]; PCSK9-LDLR complex [GO:1990666]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]iFUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. In case of HIV-1 infection, functions as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells.Q9HBL8NMRL1,NmrA-like family domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Note=Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios.Zcytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer. {ECO:0000269|PubMed:17496144, ECO:0000269|PubMed:18263583, ECO:0000269|PubMed:19254724}.P30086PEBP1*Phosphatidylethanolamine-binding protein 1ATP binding [GO:0005524]; enzyme binding [GO:0019899]; phosphatidylethanolamine binding [GO:0008429]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; serine-type endopeptidase inhibitor activity [GO:0004867]FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. {ECO:0000250, ECO:0000269|PubMed:18294816}.; FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). {ECO:0000250}.Q14498RBM39RNA-binding protein 39SUBCELLULAR LOCATION: Nucleus speckle. Note=Concentrated in nuclear speckles. Colocalizes with the core spliceosomal snRNP proteins.mRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]; RNA processing [GO:0006396]; RNA splicing [GO< :0008380]; transcription, DNA-templated [GO:0006351]microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]FUNCTION: Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1 (By similarity). May be involved in pre-mRNA splicing process. {ECO:0000250}.P26885FKBP2)Peptidyl-prolyl cis-trans isomerase FKBP2nSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]Q8TAD7OCC1*Overexpressed in colon carcinoma 1 proteinP55290CAD13 Cadherin-13adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; endothelial cell migration [GO:0043542]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; keratinocyte proliferation [GO:0043616]; lamellipodium assembly [GO:0030032]; localization within membrane [GO:0051668]; low-density lipoprotein particle mediated signaling [GO:0055096]; mitotic cell cycle [GO:0000278]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell proliferation [GO:0008285]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cell migration [GO:0030335]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; Rac protein signal transduction [GO:0016601]; regulation of cell growth [GO:0001558]; regulation of endocytosis [GO:0030100]; regulation of epidermal growth factor receptor signaling pathway [GO:0042058]; Rho protein signal transduction [GO:0007266]; sprouting angiogenesis [GO:0002040]adiponectin binding [GO:0055100]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle binding [GO:0030169]Wanchored component of membrane [GO:0031225]; caveola [GO:0005901]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]:FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth. {ECO:0000269|PubMed:10737605}.Q9UHD9UBQL2 Ubiquilin-2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18199683}. Nucleus {ECO:0000269|PubMed:9853615}. Membrane {ECO:0000250|UniProtKB:Q9QZM0}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19148225}. Note=Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells. {ECO:0000269|PubMed:10983987}.autophagy [GO:0006914]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of clathrin-mediated endocytosis [GO:1900186]; negative regulation of G-protein coupled receptor internalization [GO:1904021]; positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; regulation of autophagosome assembly [GO:2000785]; regulation of macroautophagy [GO:0016241]autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:10983987). Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:24215460, PubMed:18307982). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957). Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (PubMed:18199683). {ECO:0000269|PubMed:10983987, ECO:0000269|PubMed:18199683, ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:24215460}.Q9BRP8WIBGPartner of Y14 and magoSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1.exon-exon junction complex disassembly [GO:1903259]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of translation [GO:0045727]?poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]qcytoplasm [GO:0005737]; exon-exon junction complex [GO:0035145]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC. {ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19410547}.O15063K0355 Uncharacterized protein KIAA0355Q8IY67RAVR1Ribonucleoprotein PTB-binding 1$SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation (By similarity). {ECO:0000250}.FUNCTION: Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). {ECO:0000250}.Q96NB3ZN830Zinc finger protein 830{SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8R1N0}. Note=Excluded from nucleolus. {ECO:0000250|UniProtKB:Q8R1N0}.blastocyst growth [GO:0001832]; cell division [GO:0051301]; chromosome organization [GO:0051276]; intestinal epithelial structure maintenance [GO:0060729]; mitotic DNA damage checkpoint [GO:0044773]; mitotic nuclear division [GO:0007067]; nuclear DNA< replication [GO:0033260]FUNCTION: May act as a regulator of the cell cycle in embryos by participating in control of M phase. {ECO:0000250|UniProtKB:Q8R1N0}.Q9P032NDUF4DNADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18179882}.?mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]GFUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion. {ECO:0000269|PubMed:14871833, ECO:0000269|PubMed:17001319, ECO:0000269|PubMed:18179882}.Q9Y680FKBP7)Peptidyl-prolyl cis-trans isomerase FKBP7mcytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]P43116PE2R2%Prostaglandin E2 receptor EP2 subtypePadenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; cellular response to prostaglandin E stimulus [GO:0071380]; G-protein coupled receptor signaling pathway [GO:0007186]; regulation of cell proliferation [GO:0042127]; response to lipopolysaccharide [GO:0032496]; response to progesterone [GO:0032570].prostaglandin E receptor activity [GO:0004957]Pintegral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle.Q9P2J5SYLC!Leucine--tRNA ligase, cytoplasmicCFUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs. {ECO:0000269|PubMed:19426743}.Q02410APBA1;Amyloid beta A4 precursor protein-binding family A member 10SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531236}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20531236}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only about 5% of the protein is located in the nucleus.; SUBCELLULAR LOCATION: Isoform 2: Golgi apparatus {ECO:0000269|PubMed:23737971}.axon cargo transport [GO:0008088]; cell adhesion [GO:0007155]; gamma-aminobutyric acid secretion [GO:0014051]; glutamate secretion [GO:0014047]; intracellular protein transport [GO:0006886]; in utero embryonic development [GO:0001701]; locomotory behavior [GO:0007626]; multicellular organism growth [GO:0035264]; nervous system development [GO:0007399]; neurotransmitter secretion [GO:0007269]; protein complex assembly [GO:0006461]; regulation of gene expression [GO:0010468]; synaptic transmission [GO:0007268]]beta-amyloid binding [GO:0001540]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; synaptic vesicle [GO:0008021]FUNCTION: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the beta-amyloid precursor protein (APP) and hence formation of beta-APP.Q8IWX8CHERP1Calcium homeostasis endoplasmic reticulum protein^SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Endoplasmic reticulum {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region of both human erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}./cellular calcium ion homeostasis [GO:0006874]; negative regulation of cell proliferation [GO:0008285]; nervous system development [GO:0007399]; positive regulation of NFAT protein import into nucleus [GO:0051533]; release of sequestered calcium ion into cytosol [GO:0051209]; RNA processing [GO:0006396]Bion channel binding [GO:0044325]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum membrane [GO:0033017]FUNCTION: Involved in calcium homeostasis, growth and proliferation. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674}.P34896GLYC*Serine hydroxymethyltransferase, cytosolic2carnitine biosynthetic process [GO:0045329]; cellular nitrogen compound metabolic process [GO:0034641]; folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; protein homotetramerization [GO:0051289]; protein tetramerization [GO:0051262]; purine nucleobase biosynthetic process [GO:0009113]; small molecule metabolic process [GO:0044281]; tetrahydrofolate interconversion [GO:0035999]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]amino acid binding [GO:0016597]; glycine hydroxymethyltransferase activity [GO:0004372]; L-allo-threonine aldolase activity [GO:0008732]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]0FUNCTION: Interconversion of serine and glycine.Q8N9Q2SR1IPProtein SREK1IP1SFUNCTION: Possible splicing regulator involved in the control of cellular survival.O60762DPM10Dolichol-phosphate mannosyltransferase subunit 1,SUBCELLULAR LOCATION: Endoplasmic reticulum.cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichol metabolic process [GO:0019348]; GDP-mannose metabolic process [GO:0019673]; GPI anchor biosynthetic process [GO:0006506]; post-translational protein modification [GO:0043687]; protein mannosylation [GO:0035268]; protein N-linked glycosylation via asparagine [GO:0018279]; protein O-linked mannosylation [GO:0035269]alcohol binding [GO:0043178]; dolichyl-phosphate beta-D-mannosyltransferase activity [GO:0004582]; dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannose binding [GO:0005537]dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleus [GO:0005634]XFUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex.Q9Y6B6SAR1BGTP-binding protein SAR1bOSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region. {ECO:0000250}.0antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; COPII vesicle coating [GO:0048208]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:000578< 9]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi cisterna membrane [GO:0032580]FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.P14866HNRPL)Heterogeneous nuclear ribonucleoprotein Lgene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pronucleus [GO:0045120]; ribonucleoprotein complex [GO:0030529]FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. {ECO:0000269|PubMed:11809897}.Q8WYL5SSH1'Protein phosphatase Slingshot homolog 1LSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cleavage furrow. Midbody. Note=Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to the cleavage furrow and the midbody during cytokinesis.|actin cytoskeleton organization [GO:0030036]; cell morphogenesis [GO:0000902]; cellular response to ATP [GO:0071318]; protein dephosphorylation [GO:0006470]; regulation of actin polymerization or depolymerization [GO:0008064]; regulation of axonogenesis [GO:0050770]; regulation of cellular protein metabolic process [GO:0032268]; regulation of lamellipodium assembly [GO:0010591]actin binding [GO:0003779]; DNA binding [GO:0003677]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:14645219, ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460}.Q9NVV5AIG1Androgen-induced gene 1 proteinIFUNCTION: May play a role in androgen-regulated growth of hair follicles.O60220TIM8A>Mitochondrial import inner membrane translocase subunit Tim8 Acellular protein metabolic process [GO:0044267]; chaperone-mediated protein transport [GO:0072321]; nervous system development [GO:0007399]; protein targeting to mitochondrion [GO:0006626]FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins. Probably necessary for normal neurologic development. {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.Q8WUZ0BCL7C-B-cell CLL/lymphoma 7 protein family member C9FUNCTION: May play an anti-apoptotic role. {ECO:0000250}.Q8WUA2PPIL4*Peptidyl-prolyl cis-trans isomerase-like 4protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of phosphorylation of RNA polymerase II C-terminal domain [GO:1901407]|nucleotide binding [GO:0000166]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.Q14247SRC8Src substrate cortactinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12151401}. Cell projection, lamellipodium {ECO:0000269|PubMed:12151401}. Cell projection, ruffle. Cell projection, dendrite {ECO:0000250}. Cell projection {ECO:0000250|UniProtKB:Q66HL2}. Cell membrane {ECO:0000305|PubMed:17959782}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, podosome {ECO:0000250|UniProtKB:Q01406}. Cell junction {ECO:0000250|UniProtKB:Q66HL2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q66HL2}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q66HL2}. Cell projection, dendritic spine {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12151401}. Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers (By similarity). In the presence of CTTNBP2, localizes at the cell cortex (By similarity). In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft (By similarity). Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity). {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2}.actin cytoskeleton reorganization [GO:0031532]; actin filament polymerization [GO:0030041]; cell motility [GO:0048870]; dendritic spine maintenance [GO:0097062]; focal adhesion assembly [GO:0048041]; intracellular protein transport [GO:0006886]; lamellipodium organization [GO:0097581]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; neuron projection morphogenesis [GO:0048812]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of smooth muscle contraction [GO:0045987]; receptor-mediated endocytosis [GO:0006898]; regulation of axon extension [GO:0030516]; regulation of mitochondrion degradation [GO:1903146]; small GTPase mediated signal transduction [GO:0007264]; substrate-dependent cell migration, cell extension [GO:0006930]scell cortex [GO:0005938]; coated pit [GO:0005905]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; mitotic spindle midzone [GO:1990023]; plasma membrane [GO:0005886]; podosome [GO:0002102]; ruffle [GO:0001726]FUNCTION: Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in the invasiveness of cancer cells, and the formation of metastases (PubMed:16636290). Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated e< ndothelial cell (EC) barrier enhancement (PubMed:20861316). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782). Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (PubMed:23144454). {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:16636290, ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:21296879, ECO:0000269|PubMed:23144454}.Q13155AIMP2EAminoacyl tRNA synthase complex-interacting multifunctional protein 2SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. {ECO:0000250}.Mapoptotic process [GO:0006915]; gene expression [GO:0010467]; negative regulation of cell proliferation [GO:0008285]; positive regulation of neuron death [GO:1901216]; positive regulation of protein ubiquitination [GO:0031398]; tRNA aminoacylation for protein translation [GO:0006418]; Type II pneumocyte differentiation [GO:0060510]Acytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor. {ECO:0000269|PubMed:16135753}.Q9Y5B6PAXB1 PAX3- and PAX7-binding protein 1Qmuscle organ development [GO:0007517]; positive regulation of histone methylation [GO:0031062]; positive regulation of myoblast proliferation [GO:2000288]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of satellite cell proliferation [GO:0014842]; transcription, DNA-templated [GO:0006351]RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with an histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20 (By similarity). {ECO:0000250}.P38159RBMX'RNA-binding motif protein, X chromosomeSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:21327109}. Note=Component of ribonucleosomes. Localizes in numerous small granules in the nucleus.cellular response to interleukin-1 [GO:0071347]; gene expression [GO:0010467]; membrane protein ectodomain proteolysis [GO:0006509]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; osteoblast differentiation [GO:0001649]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein homooligomerization [GO:0051260]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]; transcription from RNA polymerase II promoter [GO:0006366]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727](catalytic step 2 spliceosome [GO:0071013]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; supraspliceosomal complex [GO:0044530]FUNCTION: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment. {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:16707624, ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:21327109}.Q9UL01DSEDermatan-sulfate epimerasekcarbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; small molecule metabolic process [GO:0044281]9chondroitin-glucuronate 5-epimerase activity [GO:0047757]endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]hFUNCTION: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. {ECO:0000269|PubMed:16505484}.A6NIH7U119BProtein unc-119 homolog BSUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:22085962}. Note=Enriched at the transition zone and extended into the proximal end of the cilium.jcilium morphogenesis [GO:0060271]; lipoprotein transport [GO:0042953]; organelle organization [GO:0006996]Wciliary transition zone [GO:0035869]; cytosol [GO:0005829]; primary cilium [GO:0072372]FUNCTION: Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells. {ECO:0000269|PubMed:22085962}.Q8NFJ5RAI3Retinoic acid-induced protein 3SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note=Localized in the plasma membrane and perinuclear vesicles.0G-protein coupled receptor activity [GO:0004930]cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]FUNCTION: Unknown. This G-protein coupled receptor could be involved in modulating differentiation and maintaining homeostasis of epithelial cells. The comparable expression level in fetal lung and kidney with adult tissues suggests a possible role in embryonic development and maturation of these organs. This retinoic acid-inducible GPCR provide evidence for a possible interaction between retinoid and G-protein signaling pathways.Q5VTL8PR38BPre-mRNA-splicing factor 38B< U4/U6(18)%precatalytic spliceosome [GO:0071011]?FUNCTION: May be required for pre-mRNA splicing. {ECO:0000305}.P14621ACYP2Acylphosphatase-2P61011SRP54*Signal recognition particle 54 kDa proteinmSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14729963}. Cytoplasm {ECO:0000269|PubMed:14729963}.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; protein targeting to ER [GO:0045047]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition [GO:0006617]; SRP-dependent cotranslational protein targeting to membrane, translocation [GO:0006616]; translation [GO:0006412]7S RNA binding [GO:0008312]; drug binding [GO:0008144]; endoplasmic reticulum signal peptide binding [GO:0030942]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; ribonucleoprotein complex binding [GO:0043021]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]FUNCTION: Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).Q8N1F8S11IP6Serine/threonine-protein kinase 11-interacting proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11741830}. Note=Some cells show granular or punctuate expression. Colocalizes with STK11/LKB1 and SMAD4 in granular or punctuate structures.!protein localization [GO:0008104]ncytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]vFUNCTION: May regulate STK11/LKB1 function by controlling its subcellular localization. {ECO:0000269|PubMed:11741830}.Q9UHQ9NB5R1NADH-cytochrome b5 reductase 1ppositive regulation of protein targeting to mitochondrion [GO:1903955]; sterol biosynthetic process [GO:0016126]@cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. {ECO:0000250}.Q99623PHB2 Prohibitin-2SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Also cytoplasmic and nuclear. {ECO:0000250}.2mammary gland alveolus development [GO:0060749]; mammary gland branching involved in thelarche [GO:0060744]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of mammary gland epithelial cell proliferation [GO:0033600]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein import into nucleus, translocation [GO:0000060]; protein stabilization [GO:0050821]; regulation of branching involved in mammary gland duct morphogenesis [GO:0060762]; sister chromatid cohesion [GO:0007062]; transcription, DNA-templated [GO:0006351]amide binding [GO:0033218]; estrogen receptor binding [GO:0030331]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]5cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; protein complex [GO:0043234] FUNCTION: Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases (By similarity). Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity. Probably involved in regulating mitochondrial respiration activity and in aging. {ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:10359819, ECO:0000303|PubMed:11302691}.Q86YH6DLP1)Decaprenyl-diphosphate synthase subunit 2isoprenoid biosynthetic process [GO:0008299]; protein heterotetramerization [GO:0051290]; regulation of body fluid levels [GO:0050878]; small molecule metabolic process [GO:0044281]; ubiquinone biosynthetic process [GO:0006744]hprotein heterodimerization activity [GO:0046982]; trans-octaprenyltranstransferase activity [GO:0050347][cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; transferase complex [GO:1990234]FUNCTION: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. {ECO:0000269|PubMed:16262699}.Q6NXT6TAPT1ATransmembrane anterior posterior transformation protein 1 homologembryonic skeletal system development [GO:0048706]; G-protein coupled receptor signaling pathway [GO:0007186]; in utero embryonic development [GO:0001701]; post-embryonic development [GO:0009791]?growth hormone-releasing hormone receptor activity [GO:0016520]+FUNCTION: May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). In case of infection, may act as a fusion receptor for cytomegalovirus (HCMV) strain AD169. {ECO:0000250}.Q8WVS4WDR60WD repeat-containing protein 60SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:23910462}. Note=Located at the base of the primary cilium in serum-starved fibroblasts.Ncell projection organization [GO:0030030]; organelle organization [GO:0006996]{ciliary tip [GO:0097542]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; primary cilium [GO:0072372]IFUNCTION: May play a role in ciliogenesis. {ECO:0000269|PubMed:23910462}.Q7Z7E8UB2Q1"Ubiquitin-conjugating enzyme E2 Q1SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TSS2}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q7TSS2}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7TSS2}.embryo implantation [GO:0007566]; fertilization [GO:0009566]; mating behavior [GO:0007617]; prolactin secretion [GO:0070459]; reproductive system development [GO:0061458]; suckling behavior [GO:0001967]jATP binding [GO:0005524]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]Ccytosol [GO:0005829]; filopodium [GO:0030175]; nucleus [GO:0005634]sFUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (Potential). May be involved in hormonal homeostasis in females (By similarity). Involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation (By similarity). {ECO:0000250|UniProtKB:Q7TSS2, ECO:0000255|PROSITE-ProRule:PRU00388}.Q8NEV8EXPH5 Exophilin-5intracellular protein transport [GO:0006886]; keratinocyte development [GO:0003334]; multivesicular body sorting pathway [GO:0071985]; positive regulation of exocytosis [GO:0045921]; positive regulation of protein secretion [GO:0050714]QFUNCTION: May act as Rab effector protein and play a role in vesicle trafficking.P08670VIMEVimentin upregulated>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21465480}.japoptotic process [GO:0006915]; astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; cellular component disassembly involved in execution < phase of apoptosis [GO:0006921]; intermediate filament organization [GO:0045109]; lens fiber cell development [GO:0070307]; movement of cell or subcellular component [GO:0006928]; muscle filament sliding [GO:0030049]; negative regulation of neuron projection development [GO:0010977]; positive regulation of gene expression [GO:0010628]; programmed cell death [GO:0012501]; SMAD protein signal transduction [GO:0060395]; viral process [GO:0016032]Pdouble-stranded RNA binding [GO:0003725]; glycoprotein binding [GO:0001948]; identical protein binding [GO:0042802]; keratin filament binding [GO:1990254]; protein C-terminus binding [GO:0008022]; scaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of eye lens [GO:0005212]Tcell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neuron projection [GO:0043005]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. {ECO:0000269|PubMed:21746880}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}.P01034CYTC Cystatin-C=SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20189825}.Napoptotic process [GO:0006915]; brain development [GO:0007420]; cell activation [GO:0001775]; cellular response to hydrogen peroxide [GO:0070301]; circadian sleep/wake cycle, REM sleep [GO:0042747]; defense response [GO:0006952]; embryo implantation [GO:0007566]; extracellular fibril organization [GO:0043206]; eye development [GO:0001654]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of cell death [GO:0060548]; negative regulation of collagen catabolic process [GO:0010711]; negative regulation of elastin catabolic process [GO:0060311]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of peptidase activity [GO:0010466]; negative regulation of proteolysis [GO:0045861]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA replication [GO:0045740]; regulation of programmed cell death [GO:0043067]; regulation of tissue remodeling [GO:0034103]; response to axon injury [GO:0048678]; response to carbohydrate [GO:0009743]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to nutrient levels [GO:0031667]; response to toxic substance [GO:0009636]; salivary gland development [GO:0007431]; Sertoli cell development [GO:0060009]beta-amyloid binding [GO:0001540]; cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; identical protein binding [GO:0042802]; protease binding [GO:0002020]axon [GO:0030424]; basement membrane [GO:0005604]; contractile fiber [GO:0043292]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; multivesicular body [GO:0005771]; neuronal cell body [GO:0043025]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.P07327ADH1AAlcohol dehydrogenase 1Aalcohol metabolic process [GO:0006066]; drug metabolic process [GO:0017144]; ethanol oxidation [GO:0006069]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]alcohol dehydrogenase (NAD) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; zinc ion binding [GO:0008270]Q9UJX3APC7$Anaphase-promoting complex subunit 7Mitosis factorssanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K11-linked ubiquitination [GO:0070979]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]manaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.Q9P2E3ZNFX1*NFX1-type zinc finger-containing protein 1Q9BTE1DCTN5Dynactin subunit 5\centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]Q709C8VP13C/Vacuolar protein sorting-associated protein 13C\protein retention in Golgi apparatus [GO:0045053]; protein targeting to vacuole [GO:0006623]cell [GO:0005623]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; intracellular [GO:0005622]P17480UBF1 Nucleolar transcription factor 1chromatin remodeling [GO:0006338]; chromatin silencing at rDNA [GO:0000183]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of transcription from RNA polymerase I promoter [GO:0045943]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription from RNA polymerase I promoter [GO:0006356]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]Zchromatin binding [GO:0003682]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]Ofibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. {ECO:0000269|PubMed:7982918}.Q96HR8NAF15H/ACA ribonucleoprotein complex non-core subunit NAF1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus (By similarity). {ECO:0000250}.dpseudouridine synthesis [GO:0001522]; ribosome biogenesis [GO:0042254]; rRNA processing [GO:0006364]dcytoplasm [GO:0005737]; nucleus [GO:0005634]; small nucleolar ribonucleoprotein complex [GO:0005732]FUNCTION: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4. {ECO:0000269|PubMed:16618814}.Q9NRZ7PLCC41-acyl-sn-glycerol-3-phosphate acyltransferase gammaSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20537980, ECO:0000269|PubMed:21173190}; Multi-pass membrane protein {ECO:0000269|PubMed:20537980}. Nucleus envelope.CDP-diacylglycerol biosynthetic process < [GO:0016024]; cellular lipid metabolic process [GO:0044255]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid biosynthetic process [GO:0008654]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190). Has a preference for arachidonoyl-CoA as a donor. Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity). {ECO:0000250|UniProtKB:Q9D517, ECO:0000269|PubMed:21173190}.Q9NYM9BET1LBET1-like protein>SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Note=Present throughout the Golgi apparatus, with increasing concentration from cis-Golgi to the trans-Golgi face of the stacks. {ECO:0000250}.membrane fusion [GO:0061025]; protein transport [GO:0015031]; regulation of retrograde vesicle-mediated transport, Golgi to ER [GO:2000156]; retrograde transport, endosome to Golgi [GO:0042147]endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; SNARE complex [GO:0031201]FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}.P27361MK03"Mitogen-activated protein kinase 3lSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Autophosphorylation at Thr-207 promotes nuclear localization.ractivation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; BMP signaling pathway [GO:0030509]; cartilage development [GO:0051216]; caveolin-mediated endocytosis [GO:0072584]; cell cycle [GO:0007049]; cellular response to heat [GO:0034605]; cellular response to mechanical stimulus [GO:0071260]; cytokine-mediated signaling pathway [GO:0019221]; DNA damage induced protein phosphorylation [GO:0006975]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; interleukin-1-mediated signaling pathway [GO:0070498]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; lung morphogenesis [GO:0060425]; MAPK cascade [GO:0000165]; MAPK import into nucleus [GO:0000189]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apolipoprotein binding [GO:2000657]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-tyrosine autophosphorylation [GO:0038083]; phosphorylation [GO:0016310]; platelet activation [GO:0030168]; positive regulation of cyclase activity [GO:0031281]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of histone acetylation [GO:0035066]; positive regulation of histone phosphorylation [GO:0033129]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of translation [GO:0045727]; protein complex assembly [GO:0006461]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of cellular response to heat [GO:1900034]; regulation of cytoskeleton organization [GO:0051493]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of Golgi inheritance [GO:0090170]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of stress-activated MAPK cascade [GO:0032872]; response to epidermal growth factor [GO:0070849]; response to exogenous dsRNA [GO:0043330]; response to toxic substance [GO:0009636]; sensory perception of pain [GO:0019233]; small GTPase mediated signal transduction [GO:0007264]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; trachea formation [GO:0060440]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]\ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; phosphatase binding [GO:0019902]caveola [GO:0005901]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; pseudopodium [GO:0031143] FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, C< ASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. {ECO:0000269|PubMed:10393181, ECO:0000269|PubMed:10617468, ECO:0000269|PubMed:12110590, ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:12974390, ECO:0000269|PubMed:15788397, ECO:0000269|PubMed:15952796, ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:8325880, ECO:0000269|PubMed:9155018, ECO:0000269|PubMed:9480836}.Q9BUK6MSTO1Protein misato homolog 1QSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17349998}.Pmitochondrion distribution [GO:0048311]; mitochondrion organization [GO:0007005]GTPase activity [GO:0003924]Acytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]qFUNCTION: Involved in the regulation of mitochondrial distribution and morphology. {ECO:0000269|PubMed:17349998}.Q13206DDX10)Probable ATP-dependent RNA helicase DDX10.FUNCTION: Putative ATP-dependent RNA helicase.P78536ADA17>Disintegrin and metalloproteinase domain-containing protein 17Secretases(6)/ADAMs(4)(10)T B cell differentiation [GO:0030183]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell motility [GO:0048870]; cell surface receptor signaling pathway [GO:0007166]; collagen catabolic process [GO:0030574]; defense response to Gram-positive bacterium [GO:0050830]; epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway [GO:0035625]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; germinal center formation [GO:0002467]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; membrane protein ectodomain proteolysis [GO:0006509]; membrane protein intracellular domain proteolysis [GO:0031293]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neurotrophin TRK receptor signaling pathway [GO:0048011]; neutrophil mediated immunity [GO:0002446]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; PMA-inducible membrane protein ectodomain proteolysis [GO:0051088]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular component movement [GO:0051272]; positive regulation of chemokine production [GO:0032722]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of epidermal growth factor-activated receptor activity [GO:0045741]; positive regulation of leukocyte chemotaxis [GO:0002690]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of T cell chemotaxis [GO:0010820]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; proteolysis [GO:0006508]; regulation of mast cell apoptotic process [GO:0033025]; response to drug [GO:0042493]; response to high density lipoprotein particle [GO:0055099]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; spleen development [GO:0048536]; T cell differentiation in thymus [GO:0033077]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; wound healing, spreading of epidermal cells [GO:0035313]integrin binding [GO:0005178]; interleukin-6 receptor binding [GO:0005138]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; Notch binding [GO:0005112]; PDZ domain binding [GO:0030165]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. {ECO:0000269|PubMed:12441351, ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:24226769, ECO:0000269|PubMed:24227843}.Q96AG4LRC59)Leucine-rich repeat-containing protein 59)SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Nucleus envelope. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1.endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial nucleoid [GO:0042645]; nuclear envelope [GO:0005635]!FUNCTION: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores. {ECO:0000269|PubMed:22321063}.P02760AMBP Protein AMBPcell adhesion [GO:0007155]; female pregnancy [GO:0007565]; heme catabolic process [GO:0042167]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of immune response [GO:0050777]; negative regulation of JNK cascade [GO:0046329]; protein catabolic process [GO:0030163]; protein-chromophore linkage [GO:0018298]; receptor-mediated endocytosis [GO:0006898]; viral process [GO:0016032]calcium channel inhibitor activity [GO:0019855]; calcium oxalate binding [GO:0046904]; heme binding [GO:0020037]; IgA binding [GO:0019862]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867]; small molecule binding [GO:0036094]blood microparticle [GO:0072562]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. {ECO:0000269|PubMed:7676539}.; FUNCTION: Trypstatin is a trypsin inhibitor. {ECO:0000250}.P24844MYL9%Myosin regulatory light polypeptide 9axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; muscle contraction [GO:0006936]; platelet aggregation [GO:0070527]; regulation of muscle contraction [GO:0006937]; small GTPase mediated signal transduction [GO:0007264]hcytosol [GO:0005829]; muscle myosin complex [GO:0005859]; stress fiber [GO:0001725]; Z disc [GO:0030018]FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion.Q9H3Z4DNJC5!DnaJ homolog subfamily C member 5SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.< exocytosis [GO:0006887]; negative regulation of neuron apoptotic process [GO:0043524]; neurotransmitter secretion [GO:0007269]; regulated secretory pathway [GO:0045055]; synaptic transmission [GO:0007268]; synaptic vesicle exocytosis [GO:0016079]=clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]FUNCTION: May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250}.Q7Z3T8ZFY16-Zinc finger FYVE domain-containing protein 163SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11546807}. Early endosome membrane {ECO:0000269|PubMed:11546807}; Peripheral membrane protein {ECO:0000269|PubMed:11546807}. Note=Localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P).BMP signaling pathway [GO:0030509]; endosomal transport [GO:0016197]; protein targeting to lysosome [GO:0006622]; regulation of endocytosis [GO:0030100]; signal transduction [GO:0007165]; vesicle organization [GO:0016050]1-phosphatidylinositol binding [GO:0005545]; metal ion binding [GO:0046872]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein transporter activity [GO:0008565]cytoplasm [GO:0005737]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes. {ECO:0000269|PubMed:11546807, ECO:0000269|PubMed:14613930}.Q15293RCN1Reticulocalbin-1Ucamera-type eye development [GO:0043010]; in utero embryonic development [GO:0001701]Lendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]nFUNCTION: May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.Q9Y3C8UFC1,Ubiquitin-fold modifier-conjugating enzyme 1protein K69-linked ufmylation [GO:1990592]; protein ufmylation [GO:0071569]; response to endoplasmic reticulum stress [GO:0034976]&UFM1 transferase activity [GO:0071568]vFUNCTION: E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. {ECO:0000269|PubMed:15071506}.Q13505MTX1 Metaxin-1SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion outer membrane {ECO:0000250}.FUNCTION: Involved in transport of proteins into the mitochondrion. Essential for embryonic development (By similarity). {ECO:0000250}.P53992SC24C Protein transport protein Sec24CSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10075675}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10075675}. Endoplasmic reticulum membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}.FUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:10329445}.Q6P1A2MBOA5"Lysophospholipid acyltransferase 5SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18195019}; Multi-pass membrane protein {ECO:0000269|PubMed:18195019}.|glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152]; phosphatidylserine acyl-chain remodeling [GO:0036150]; phospholipid metabolic process [GO:0006644]; regulation of plasma lipoprotein particle levels [GO:0097006]; small molecule metabolic process [GO:0044281]C1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]kFUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18195019, ECO:0000269|PubMed:18772128}.Q86Y82STX12 Syntaxin-12=SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.cholesterol efflux [GO:0033344]; intracellular protein transport [GO:0006886]; protein stabilization [GO:0050821]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]endomembrane system [GO:0012505]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane raft [GO:0045121]; phagocytic vesicle [GO:0045335]; SNARE complex [GO:0031201]FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By similarity). {ECO:0000250}.P48449ERG7Lanosterol synthase Terpene metabolismSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14766201, ECO:0000269|PubMed:15525992}; Peripheral membrane protein {ECO:0000269|PubMed:14766201, ECO:0000269|PubMed:15525992}.cholesterol biosynthetic process [GO:0006695]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202])lanosterol synthase activity [GO:0000250]_endoplasmic reticulum membrane [GO:0005789]; lipid particle [GO:0005811]; membrane [GO:0016020]FUNCTION: Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. {ECO:0000269|PubMed:7639730}.Q01650LAT15Large neutral amino acids transporter small subunit 1Recepter essential AasPSUBCELLULAR LOCATION: Cytoplasm, cytosol. Apical cell membrane; Multi-pass membrane protein. Note=Located to the plasma membrane by SLC3A2/4F2hc. Localized to the apical membrane of placental syncytiophoblastic cells. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). {ECO:0000250}.hamino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; blood coagulation [GO:0007596]; cation transmembrane transport [GO:0098655]; cell differentiation [GO:0030154]; cellular amino acid metabolic process [GO:0006520]; ion transport [GO:0006811]; L-alpha-amino acid transmembrane transport [GO:1902475]; leucine transport [GO:0015820]; leukocyte migration [GO:0050900]; nervous system development [GO:0007399]; neutral amino acid transport [GO:0015804]; phenylalanine transport [GO:0015823]; transmembrane transport [GO:0055085]; transport [GO:0006810]; tryptophan transport [GO:0015827]amino acid transmembrane transporter activity [GO:0015171]; antiporter activity [GO:0015297]; L-leucine transmembrane transporter activity [GO:0015190]; L-phenylalanine transmembrane transporter activity [GO:0015192]; L-tryptophan transmembrane transporter activity [GO:0015196]; neutral amino acid transmembrane transporter activity [GO:0015175]; peptide antigen bindi< ng [GO:0042605]Capical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]0FUNCTION: Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L-leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. {ECO:0000269|PubMed:10049700, ECO:0000269|PubMed:10391915, ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:18262359, ECO:0000269|PubMed:9751058}.Q13724MOGS$Mannosyl-oligosaccharide glucosidase[SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein.cellular protein metabolic process [GO:0044267]; oligosaccharide metabolic process [GO:0009311]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]]glucosidase activity [GO:0015926]; mannosyl-oligosaccharide glucosidase activity [GO:0004573]FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner.P619811433G14-3-3 protein gammajapoptotic process [GO:0006915]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway [GO:0097193]; membrane organization [GO:0061024]; mitotic cell cycle [GO:0000278]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; organelle organization [GO:0006996]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; protein targeting [GO:0006605]; regulation of neuron differentiation [GO:0045664]; regulation of signal transduction [GO:0009966]; regulation of synaptic plasticity [GO:0048167]; small GTPase mediated signal transduction [GO:0007264]; transcription initiation from RNA polymerase II promoter [GO:0006367]insulin-like growth factor receptor binding [GO:0005159]; poly(A) RNA binding [GO:0044822]; protein kinase C binding [GO:0005080]; protein kinase C inhibitor activity [GO:0008426]cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; myelin sheath [GO:0043209][FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:16511572}.O60565GREM1 Gremlin-1 apoptotic process [GO:0006915]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell-cell signaling [GO:0007267]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; collagen fibril organization [GO:0030199]; determination of dorsal identity [GO:0048263]; embryonic limb morphogenesis [GO:0030326]; limb development [GO:0060173]; mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003337]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of bone mineralization [GO:0030502]; negative regulation of bone mineralization involved in bone maturation [GO:1900158]; negative regulation of bone remodeling [GO:0046851]; negative regulation of bone trabecula formation [GO:1900155]; negative regulation of branching involved in ureteric bud morphogenesis [GO:0090191]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of monocyte chemotaxis [GO:0090027]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of osteoclast proliferation [GO:0090291]; negative regulation of pathway-restricted SMAD protein phosphorylation [GO:0060394]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of angiogenesis [GO:0045766]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cardiac muscle cell differentiation [GO:2000727]; positive regulation of cell proliferation [GO:0008284]; positive regulation of NF-kappaB import into nucleus [GO:0042346]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-tyrosine autophosphorylation [GO:1900086]; positive regulation of receptor activity [GO:2000273]; positive regulation of receptor internalization [GO:0002092]; positive regulation of telomerase activity [GO:0051973]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation [GO:0003257]; proximal/distal pattern formation [GO:0009954]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; signal transduction [GO:0007165]; ureteric bud formation [GO:0060676]BMP binding [GO:0036122]; morphogen activity [GO:0016015]; receptor agonist activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043184];cell surface [GO:0009986]; extracellular space [GO:0005615]eFUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner. Acts as inhibitor of monocyte chemotaxis (By similarity). {ECO:0000250}.P14373TRI27Zinc finger protein RFPSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17156811}. Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus, PML body {ECO:0000250}. Early endosome {ECO:0000269|PubMed:1437549, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:9247190}. Note=Nuclear or cytoplasmic depending on the cell type (By similarity). Colocalized with PML and EIF3S6 in nuclear bodies. Recruited to retromer-containing endosomes via interaction with MAGEL2 (PubMed:23452853). {ECO:0000250, ECO:0000269|PubMed:23452853}.Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell proliferation [GO:0008283]; innate immune response [GO:0045087]; interferon-gamma secretion [GO:0072643]; negative < regulation of adaptive immune response [GO:0002820]; negative regulation of calcium ion import [GO:0090281]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of interleukin-2 secretion [GO:1900041]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of viral release from host cell [GO:1902187]; negative regulation of viral transcription [GO:0032897]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of actin nucleation [GO:0051127]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein K63-linked ubiquitination [GO:0070534]; protein trimerization [GO:0070206]; retrograde transport, endosome to Golgi [GO:0042147]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; ligase activity [GO:0016874]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]uFUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853). Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. {ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:23452853}.P09496CLCAClathrin light chain Aantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor signaling pathway [GO:0048011]; post-Golgi vesicle-mediated transport [GO:0006892]clathrin coat [GO:0030118]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin complex [GO:0071439]; clathrin vesicle coat [GO:0030125]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]Q9H270VPS116Vacuolar protein sorting-associated protein 11 homolog`SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:20682791}. Late endosome membrane {ECO:0000269|PubMed:11382755, ECO:0000269|PubMed:21148287}; Peripheral membrane protein {ECO:0000269|PubMed:11382755}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:11382755, ECO:0000269|PubMed:17897319}; Peripheral membrane protein {ECO:0000269|PubMed:11382755}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:21148287, ECO:0000305}. Cytoplasmic vesicle {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}.endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of early endosome to late endosome transport [GO:2000643]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of organelle assembly [GO:1902115]; regulation of protein stability [GO:0031647]nucleotide binding [GO:0000166]; protein domain specific binding [GO:0019904]; syntaxin binding [GO:0019905]; zinc ion binding [GO:0008270]endocytic vesicle [GO:0030139]; endosome [GO:0005768]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]yFUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (PubMed:21148287). Involved in the retrograde Shiga toxin transport (PubMed:23593995). {ECO:0000269|PubMed:21148287, ECO:0000269|PubMed:23593995, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:24554770, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.Q9Y2X3NOP58Nucleolar protein 58MSUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm {ECO:0000305}.cell growth [GO:0016049]; rRNA modification [GO:0000154]; rRNA processing [GO:0006364]; snRNP protein import into nucleus [GO:0006608]box C/D snoRNP complex [GO:0031428]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; pre-snoRNP complex [GO:0070761]; small nucleolar ribonucleoprotein complex [GO:0005732]; small-subunit processome [GO:0032040]MFUNCTION: Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs. {ECO:0000250, ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:19620283}.Q7Z3B0SIM15"Small integral membrane protein 15Q8TDM6DLG5Disks large homolog 5SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:12657639}. Cell membrane {ECO:0000269|PubMed:12657639}; Peripheral membrane protein {ECO:0000269|PubMed:12657639}. Note=Localized at sites of cell-cell contact.apical protein localization [GO:0045176]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; intracellular signal transduction [GO:0035556]; metanephric collecting duct development [GO:0072205]; midbrain development [GO:0030901]; negative regulation of cell proliferation [GO:0008285]; polarized epithelial cell differentiation [GO:0030859]; protein complex assembly [GO:0006461]; protein localization to adherens junction [GO:0071896]; regulation of apoptotic process [GO:0042981]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]; zonula adherens assembly [GO:0045186]< beta-catenin binding [GO:0008013]; cytoskeletal protein binding [GO:0008092]; receptor signaling complex scaffold activity [GO:0030159]^cell-cell adherens junction [GO:0005913]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]FUNCTION: May play a role at the plasma membrane in the maintenance of the structure of epithelial cells and in the transmission of extracellular signals to the membrane and cytoskeleton. {ECO:0000269|PubMed:11876824}.O15488GLYG2 Glycogenin-2carbohydrate metabolic process [GO:0005975]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; small molecule metabolic process [GO:0044281]4glycogenin glucosyltransferase activity [GO:0008466]2cytosol [GO:0005829]; lysosomal lumen [GO:0043202]FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.P15104GLNAGlutamine synthetasecell proliferation [GO:0008283]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to starvation [GO:0009267]; glutamate catabolic process [GO:0006538]; glutamine biosynthetic process [GO:0006542]; neurotransmitter uptake [GO:0001504]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of insulin secretion [GO:0032024]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; protein homooligomerization [GO:0051260]; response to glucose [GO:0009749]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]ATP binding [GO:0005524]; glutamate-ammonia ligase activity [GO:0004356]; glutamate binding [GO:0016595]; glutamate decarboxylase activity [GO:0004351]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]?axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; glial cell projection [GO:0097386]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein complex [GO:0043234]; rough endoplasmic reticulum [GO:0005791]0FUNCTION: This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts. {ECO:0000250, ECO:0000269|PubMed:18662667}.P10155RO60 60 kDa SS-A/Ro ribonucleoproteincilium morphogenesis [GO:0060271]; immune system development [GO:0002520]; response to UV [GO:0009411]; smoothened signaling pathway [GO:0007224]; transcription from RNA polymerase III promoter [GO:0006383]Wmetal ion binding [GO:0046872]; RNA binding [GO:0003723]; U2 snRNA binding [GO:0030620]Xcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]CFUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation. {ECO:0000269|PubMed:18056422}.; FUNCTION: May play roles in cilia formation and/or maintenance. {ECO:0000250}.Q8IXI1MIRO2Mitochondrial Rho GTPase 2cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of mitochondrial outer membrane [GO:0031307]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). {ECO:0000250}.Q14554PDIA5Protein disulfide-isomerase A5Gcell redox homeostasis [GO:0045454]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; oxidation-reduction process [GO:0055114]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]Woxidoreductase activity [GO:0016491]; protein disulfide isomerase activity [GO:0003756]Uendoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]P15529MCPMembrane cofactor protein CD46/CD74`SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}; Single-pass type I membrane protein {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}. Note=Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide.adaptive immune response [GO:0002250]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; interleukin-10 production [GO:0032613]; negative regulation of complement activation [GO:0045916]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of memory T cell differentiation [GO:0043382]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transforming growth factor beta production [GO:0071636]; regulation of complement activation [GO:0030449]; regulation of Notch signaling pathway [GO:0008593]; sequestering of extracellular ligand from receptor [GO:0035581]; single fertilization [GO:0007338]; T cell mediated immunity [GO:0002456]; viral process [GO:0016032]cadherin binding [GO:0045296]; endopeptidase activity [GO:0004175]; enzyme inhibitor activity [GO:0004857]; receptor activity [GO:0004872]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; inner acrosomal membrane [GO:0002079]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. A number of viral and bacterial pathogens seem to exploit this property and directly induce an immunosuppressive phenotype in T-cells by binding to CD46. {ECO:0000269|PubMed:10843656, ECO:0000269|PubMed:12540904}.Q9BRZ2TRI56"E3 ubiquitin-protein ligase TRIM56Kdefense response to virus [GO:0051607]; innate immune response [GO:0045087]; interferon-beta production [GO:0032608]; positive regulation of type I interferon production [GO:0032481]; protein K63-linked ubiquitination [GO:0070534]; regulation of type I interferon production [GO:0032479]; response to type I interferon [GO:0034340]ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]aFUNCTION: E3 ubiquitin-protein ligase that mediates 'Lys-63'-linked polyubiquitination of TMEM173/STING, thereby playing a key role in innate immunity. TMEM173/STING 'Lys-63'-linked ubiquitination activates the production of type I interferon IFN-beta following detection of pathogen- and host-derived double-stranded DNA (By similarity). {ECO:0000250}.P08397HEM3Porphobilinogen deaminaseastrocyte differentiation [GO:0048708]; cellular response to amine stimulus [GO:0071418]; cellular response to antibiotic [GO:0071236]; cellular response to arsenic-containing substance < [GO:0071243]; cellular response to cytokine stimulus [GO:0071345]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to lead ion [GO:0071284]; heme biosynthetic process [GO:0006783]; organ regeneration [GO:0031100]; peptidyl-pyrromethane cofactor linkage [GO:0018160]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to amino acid [GO:0043200]; response to carbohydrate [GO:0009743]; response to cobalt ion [GO:0032025]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to methylmercury [GO:0051597]; response to vitamin [GO:0033273]; response to zinc ion [GO:0010043]; small molecule metabolic process [GO:0044281]amine binding [GO:0043176]; carboxylic acid binding [GO:0031406]; coenzyme binding [GO:0050662]; hydroxymethylbilane synthase activity [GO:0004418]; uroporphyrinogen-III synthase activity [GO:0004852]`axon [GO:0030424]; condensed chromosome [GO:0000793]; cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.Q96GD0PLPPPyridoxal phosphate phosphataseSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection, ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Cell membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side {ECO:0000269|PubMed:15580268}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody.Dactin rod assembly [GO:0031247]; cellular response to ATP [GO:0071318]; positive regulation of actin filament depolymerization [GO:0030836]; protein dephosphorylation [GO:0006470]; pyridoxal phosphate catabolic process [GO:0032361]; regulation of cytokinesis [GO:0032465]; regulation of mitotic nuclear division [GO:0007088]heat shock protein binding [GO:0031072]; magnesium ion binding [GO:0000287]; phosphoprotein phosphatase activity [GO:0004721]; phosphoserine phosphatase activity [GO:0004647]; pyridoxal phosphatase activity [GO:0033883]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lamellipodium membrane [GO:0031258]; ruffle membrane [GO:0032587]FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268}.Q9UKU6TRHDE2Thyrotropin-releasing hormone-degrading ectoenzymeESUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.cell-cell signaling [GO:0007267]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217]; signal transduction [GO:0007165]ncytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]9FUNCTION: Specific inactivation of TRH after its release.Q08043ACTN3Alpha-actinin-3focal adhesion assembly [GO:0048041]; muscle filament sliding [GO:0030049]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of glycolytic process [GO:0045820]; negative regulation of oxidative phosphorylation [GO:0090324]; positive regulation of glucose catabolic process to lactate via pyruvate [GO:1904025]; positive regulation of skeletal muscle tissue growth [GO:0048633]; regulation of aerobic respiration [GO:1903715]; regulation of apoptotic process [GO:0042981]; regulation of the force of skeletal muscle contraction [GO:0014728]; response to denervation involved in regulation of muscle adaptation [GO:0014894]; skeletal muscle atrophy [GO:0014732]; transition between fast and slow fiber [GO:0014883]calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; ion channel binding [GO:0044325]; protein homodimerization activity [GO:0042803]; structural constituent of muscle [GO:0008307]actin filament [GO:0005884]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; pseudopodium [GO:0031143]Q13416ORC2$Origin recognition complex subunit 2DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]+DNA replication origin binding [GO:0003688]8centrosome [GO:0005813]; condensed chromosome inner kinetochore [GO:0000939]; heterochromatin [GO:0000792]; membrane [GO:0016020]; nuclear origin of replication recognition complex [GO:0005664]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; origin recognition complex [GO:0000808]; plasma membrane [GO:0005886]*FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3. {ECO:0000269|PubMed:22427655, ECO:0000269|PubMed:22935713}.P10301RRASRas-related protein R-RasSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS).axon guidance [GO:0007411]; face morphogenesis [GO:0060325]; leukocyte differentiation [GO:0002521]; negative regulation of cell migration [GO:0030336]; positive regulation of angiogenesis [GO:0045766]; Ras protein signal transduction [GO:0007265]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of protein kinase B signaling [GO:0051896]; synaptic transmission [GO:0007268]vGDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; protein complex binding [GO:0032403]yextracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; plasma membrane [GO:0005886]^FUNCTION: Regulates the organization of the actin cytoskeleton. {ECO:0000269|PubMed:16537651}.P14678RSMB<Small nuclear ribonucleoprotein-associated proteins B and B':activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; gene expression [GO:0010467]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; positive regulation of defense response to virus by host [GO:0002230]; protein methylation [GO:0006479]; RNA splicing [GO:0008380]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Khistone pre-mRNA DCP bindin< g [GO:0071208]; poly(A) RNA binding [GO:0044822]Tcatalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; histone pre-mRNA 3'end processing complex [GO:0071204]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U4 snRNP [GO:0005687]; U5 snRNP [GO:0005682]; U7 snRNP [GO:0005683]FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:18984161}.Q9H1B7I2BPL3Interferon regulatory factor 2-binding protein-likedevelopment of secondary female sexual characteristics [GO:0046543]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]Pextracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: May contribute to the control of female reproductive function (By similarity). May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter. {ECO:0000250}.Q9Y2H2SAC2&Phosphatidylinositide phosphatase SAC2cardiac muscle hypertrophy in response to stress [GO:0014898]; phosphatidylinositol catabolic process [GO:0031161]; phosphatidylinositol-mediated signaling [GO:0048015]; regulation of protein kinase B signaling [GO:0051896]0phosphoric ester hydrolase activity [GO:0042578]JFUNCTION: Inositol 5-phosphatase which acts on phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Hydrolyzes phosphatidylinositol 4,5-bisphosphate most effectively. Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation. {ECO:0000269|PubMed:11274189, ECO:0000269|PubMed:17322895}.O95602RPA1*DNA-directed RNA polymerase I subunit RPA1gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]jDNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; DNA-directed RNA polymerase I complex [GO:0005736]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). {ECO:0000250}.P15374UCHL30Ubiquitin carboxyl-terminal hydrolase isozyme L3protein catabolic process [GO:0030163]; protein deubiquitination [GO:0016579]; ubiquitin-dependent protein catabolic process [GO:0006511]rpeptidase activity [GO:0008233]; ubiquitin binding [GO:0043130]; ubiquitin-specific protease activity [GO:0004843]FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. {ECO:0000269|PubMed:19154770, ECO:0000269|PubMed:21762696, ECO:0000269|PubMed:22689415, ECO:0000269|PubMed:2530630, ECO:0000269|PubMed:9790970}.Q8IWT0ARCHProtein archeaseEtRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]Mextracellular exosome [GO:0070062]; tRNA-splicing ligase complex [GO:0072669] FUNCTION: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB. Together with DDX1, acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation. {ECO:0000269|PubMed:24870230}.Q9Y3M8STA13&StAR-related lipid transfer protein 13SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet.BGTPase activator activity [GO:0005096]; lipid binding [GO:0008289]Vcytosol [GO:0005829]; lipid particle [GO:0005811]; mitochondrial membrane [GO:0031966]FUNCTION: GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells. {ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:16217026}.P63000RAC1*Ras-related C3 botulinum toxin substrate 1SSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:21693584}. Cytoplasm {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts (By similarity). {ECO:0000250}.= actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; anatomical structure arrangement [GO:0048532]; anatomical structure morphogenesis [GO:0009653]; apoptotic signaling pathway [GO:0097190]; auditory receptor cell morphogenesis [GO:0002093]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell-matrix adhesion [GO:0007160]; cell motility [GO:0048870]; cerebral cortex GABAergic interneuron development [GO:0021894]; cerebral cortex radially oriented cell migration [GO:0021799]; cochlea morphogenesis [GO:0090103]; dendrite morphogenesis [GO:0048813]; dopaminergic neuron differentiation [GO:0071542]; embryonic olfactory bulb interneuron precursor migration [GO:0021831]; engulfment of apoptotic cell [GO:0043652]; ephrin receptor signaling pathway [GO:0048013]; epithelial cell morphogenesis [GO:0003382]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; G-protein coupled receptor signaling pathway [GO:0007< 186]; homeostasis of number of cells within a tissue [GO:0048873]; hyperosmotic response [GO:0006972]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lamellipodium assembly [GO:0030032]; localization within membrane [GO:0051668]; movement of cell or subcellular component [GO:0006928]; negative regulation of interleukin-23 production [GO:0032707]; negative regulation of receptor-mediated endocytosis [GO:0048261]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein localization to plasma membrane [GO:0072659]; regulation of cell migration [GO:0030334]; regulation of cell size [GO:0008361]; regulation of defense response to virus by virus [GO:0050690]; regulation of fibroblast migration [GO:0010762]; regulation of hydrogen peroxide metabolic process [GO:0010310]; regulation of neuron maturation [GO:0014041]; regulation of respiratory burst [GO:0060263]; regulation of small GTPase mediated signal transduction [GO:0051056]; response to wounding [GO:0009611]; ruffle assembly [GO:0097178]; ruffle organization [GO:0031529]; semaphorin-plexin signaling pathway [GO:0071526]; small GTPase mediated signal transduction [GO:0007264]; substrate adhesion-dependent cell spreading [GO:0034446]; synaptic transmission, GABAergic [GO:0051932]; T cell costimulation [GO:0031295]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]enzyme binding [GO:0019899]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; Rho GDP-dissociation inhibitor binding [GO:0051022]; thioesterase binding [GO:0031996]cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extrinsic component of plasma membrane [GO:0019897]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; trans-Golgi network [GO:0005802]YFUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.; FUNCTION: Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.Q9BV44THUM3!THUMP domain-containing protein 3Amethyltransferase activity [GO:0008168]; RNA binding [GO:0003723]P69849NOMO3Nodal modulator 3Q9Y282ERGI3>Endoplasmic reticulum-Golgi intermediate compartment protein 3SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636}; Multi-pass membrane protein {ECO:0000269|PubMed:15308636}. Note=Cycles between the endoplasmic reticulum and the Golgi.endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]\FUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000250}.Q13501SQSTMSequestosome-1SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Cytoplasm, P-body. Note=Sarcomere (By similarity). In cardiac muscles localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies. {ECO:0000250}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; apoptotic signaling pathway [GO:0097190]; autophagy [GO:0006914]; cell differentiation [GO:0030154]; endosomal transport [GO:0016197]; immune system process [GO:0002376]; intracellular signal transduction [GO:0035556]; macroautophagy [GO:0016236]; mitochondrion degradation [GO:0000422]; negative regulation of apoptotic process [GO:0043066]; negative regulation of growth of symbiont in host [GO:0044130]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of macroautophagy [GO:0016239]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein heterooligomerization [GO:0051291]; protein localization [GO:0008104]; protein phosphorylation [GO:0006468]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; regulation of mitochondrion organization [GO:0010821]; regulation of Ras protein signal transduction [GO:0046578]; response to stress [GO:0006950]; ubiquitin-dependent protein catabolic process [GO:0006511]8identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; receptor tyrosine kinase binding [GO:0030971]; SH2 domain binding [GO:0042169]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270]< aggresome [GO:0016235]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; inclusion body [GO:0016234]; late endosome [GO:0005770]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]; PML body [GO:0016605]; pre-autophagosomal structure [GO:0000407]FUNCTION: Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. {ECO:0000250, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12471037, ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:15911346, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:16079148, ECO:0000269|PubMed:16286508, ECO:0000269|PubMed:19931284, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:24128730}.Q9UFG5CS025UPF0449 protein C19orf25Q9H223EHD4EH domain-containing protein 4SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:18331452}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:18331452}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9EQP2}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. cellular response to growth factor stimulus [GO:0071363]; endocytic recycling [GO:0032456]; pinocytosis [GO:0006907]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; protein homooligomerization [GO:0051260]; regulation of endocytosis [GO:0030100]early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]FUNCTION: ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport. {ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:18331452}.O43572AKA10)A-kinase anchor protein 10, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic.blood coagulation [GO:0007596]; protein localization [GO:0008104]; signal transduction [GO:0007165]; termination of G-protein coupled receptor signaling pathway [GO:0038032]fcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity). {ECO:0000250}.O14524T194ATransmembrane protein 194A=SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q6ZQE4}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000250|UniProtKB:B9X187}. Nucleus envelope {ECO:0000250|UniProtKB:Q6ZQE4}. Note=Colocalizes with lamins and RAN-GTP at the nuclear envelope. {ECO:0000250|UniProtKB:Q6ZQE4}.ointegral component of membrane [GO:0016021]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]Q16254E2F4Transcription factor E2F4blood circulation [GO:0008015]; cell volume homeostasis [GO:0006884]; centriole assembly [GO:0098534]; epithelial cell development [GO:0002064]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; motile cilium assembly [GO:0044458]; multi-ciliated epithelial cell differentiation [GO:1903251]; organ morphogenesis [GO:0009887]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell proliferation [GO:0042127]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]DNA binding [GO:0003677]; protein domain specific binding [GO:0019904]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]Cnucleoplasm [GO:0005654]; transcription factor complex [GO:0005667]FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14, ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925}.Q96ME1FXL18F-box/LRR-repeat protein 18P49257LMAN1Protein ERGIC-53SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein.blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum organization [GO:0007029]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; positive regulation of organelle organization [GO:0010638]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]; protein transport [GO:0015031]cmannose binding [GO:0005537]; metal ion binding [GO:0046872]; unfolded protein binding [GO:0051082]endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; host cell perinuclear region of cytoplasm [GO:0044220]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; sarcomere [GO:0030017]}FUNCTION: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a speci< fic cargo receptor for the ER-to-Golgi transport of selected proteins. {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:13130098}.Q8N201INT1Integrator complex subunit 1aSUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.snRNA processing [GO:0016180]integral component of membrane [GO:0016021]; integrator complex [GO:0032039]; membrane [GO:0016020]; nuclear membrane [GO:0031965]IFUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.O60888CUTA Protein CutAEprotein localization [GO:0008104]; response to metal ion [GO:0010038]bFUNCTION: May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).O43292GPAA18Glycosylphosphatidylinositol anchor attachment 1 proteinattachment of GPI anchor to protein [GO:0016255]; cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; post-translational protein modification [GO:0043687]; protein complex assembly [GO:0006461]; protein retention in ER lumen [GO:0006621]FUNCTION: Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. {ECO:0000269|PubMed:9468317}.Q6ZWT7MBOA2"Lysophospholipid acyltransferase 2glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]yFUNCTION: Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO:0000269|PubMed:18772128}.Q9Y232CDYL1Chromodomain Y-like proteinYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18450745, ECO:0000269|PubMed:19808672}.negative regulation of nucleic acid-templated transcription [GO:1903507]; regulation of transcription, DNA-templated [GO:0006355]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]histone acetyltransferase activity [GO:0004402]; methylated histone binding [GO:0035064]; transcription corepressor activity [GO:0003714]hFUNCTION: Acts as a RE1-silencing transcription factor (REST) corepressor that facilitates histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression. Required for chromatin targeting and maximal enzymatic activity of polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes. Has histone acetyltransferase activity, with a preference for histone H4. {ECO:0000269|PubMed:12072557, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:22009739}.O14832PAHX&Phytanoyl-CoA dioxygenase, peroxisomalcellular lipid metabolic process [GO:0044255]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089]; small molecule metabolic process [GO:0044281]cofactor binding [GO:0048037]; electron carrier activity [GO:0009055]; L-ascorbic acid binding [GO:0031418]; metal ion binding [GO:0046872]; phytanoyl-CoA dioxygenase activity [GO:0048244]Tmitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777];FUNCTION: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.O00232PSD12/26S proteasome non-ATPase regulatory subunit 12Q8IZH2XRN15'-3' exoribonuclease 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12515382, ECO:0000269|PubMed:14580940, ECO:0000269|PubMed:9802570}. Note=Discrete foci at the inner surface of the cell membrane.exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; histone mRNA catabolic process [GO:0071044]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; rRNA catabolic process [GO:0016075]c5'-3' exonuclease activity [GO:0008409]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA (By similarity). Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). {ECO:0000250, ECO:0000269|PubMed:18172165}.Q9NU22MDN1Midasin^SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]sFUNCTION: Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. {ECO:0000250}.P17980PRS6A"26S protease regulatory subunit 6ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Cytoplasm, P-body {ECO:0000250}. Note=Colocalizes with TRIM5 in the cytoplasmic bodies. {ECO:0000250}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activit< y involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; proteasome-activating ATPase activity [GO:0036402]; TBP-class protein binding [GO:0017025]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]hcytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540].FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). In case of HIV-1 infection, suppresses Tat-mediated transactivation. {ECO:0000250}.Q86XZ4SPAS20Spermatogenesis-associated serine-rich protein 2Q9H0V1TM168Transmembrane protein 168P16615AT2A23Sarcoplasmic/endoplasmic reticulum calcium ATPase 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.blood coagulation [GO:0007596]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cell adhesion [GO:0007155]; cellular calcium ion homeostasis [GO:0006874]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; epidermis development [GO:0008544]; ER-nucleus signaling pathway [GO:0006984]; ion transmembrane transport [GO:0034220]; negative regulation of heart contraction [GO:0045822]; organelle organization [GO:0006996]; positive regulation of endoplasmic reticulum calcium ion concentration [GO:0032470]; positive regulation of heart rate [GO:0010460]; regulation of calcium ion-dependent exocytosis of neurotransmitter [GO:1903233]; regulation of cardiac muscle cell action potential involved in regulation of contraction [GO:0098909]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of the force of heart contraction [GO:0002026]; relaxation of cardiac muscle [GO:0055119]; response to endoplasmic reticulum stress [GO:0034976]; response to peptide hormone [GO:0043434]; sarcoplasmic reticulum calcium ion transport [GO:0070296]; transition between fast and slow fiber [GO:0014883]; transmembrane transport [GO:0055085]; T-tubule organization [GO:0033292]JATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-transporting ATPase activity [GO:0005388]; calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039]; enzyme binding [GO:0019899]; protein C-terminus binding [GO:0008022]; S100 protein binding [GO:0044548]\calcium ion-transporting ATPase complex [GO:0090534]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; integral component of plasma membrane [GO:0005887]; longitudinal sarcoplasmic reticulum [GO:0014801]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; platelet dense tubular network membrane [GO:0031095]; protein complex [GO:0043234]; ribbon synapse [GO:0097470]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; vesicle membrane [GO:0012506]FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle. {ECO:0000269|PubMed:16402920}.P21953ODBB:2-oxoisovalerate dehydrogenase subunit beta, mitochondrial3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity [GO:0003863]; alpha-ketoacid dehydrogenase activity [GO:0003826]; carboxy-lyase activity [GO:0016831]mitochondrial alpha-ketoglutarate dehydrogenase complex [GO:0005947]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]8FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).Q9UQM7KCC2AACalcium/calmodulin-dependent protein kinase type II subunit alphaGastric acid secretionSUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Postsynaptic lipid rafts. {ECO:0000250}.angiotensin-activated signaling pathway [GO:0038166]; calcium ion transport [GO:0006816]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; G1/S transition of mitotic cell cycle [GO:0000082]; interferon-gamma-mediated signaling pathway [GO:0060333]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cellular response to heat [GO:1900034]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928]; response to ischemia [GO:0002931]; synaptic transmission [GO:0007268]"ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; glutamate receptor binding [GO:0035254]; kinase activity [GO:0016301]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]cell junction [GO:0030054]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; mitochondrion [GO:0005739]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]LFUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity (By similarity). {ECO:0000250}.O95071UBR5 E3 ubiquitin-protein ligase UBR5cell proliferation [GO:0008283]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; negative regulation of double-strand break repair [GO:2000780]; negative regulation of histone H2A K63-linked ubiquitination [GO:1901315]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of catenin import into nucleus [GO:0035413]; positive regulation of protein import into nucleus, translocation [GO:0033160]; progesterone receptor signaling pathway [GO:0050847]; protein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; ubiquitin-dependent protein catabolic process [GO:0006511]ligase activity [GO:0016874]; RNA binding [GO:0003723]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-ubiquitin ligase activity [GO:0034450]; zinc ion binding [GO:0008270]]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]%FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination < and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000250, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:21726808, ECO:0000269|PubMed:22884692}.P83436COG7,Conserved oligomeric Golgi complex subunit 7SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11980916}; Peripheral membrane protein {ECO:0000269|PubMed:11980916}.intracellular protein transport [GO:0006886]; protein glycosylation [GO:0006486]; protein localization to Golgi apparatus [GO:0034067]; protein localization to organelle [GO:0033365]; protein stabilization [GO:0050821]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]Q86VQ0LCA5 LebercilinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17546029}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17546029}. Note=In non- ciliated cells, localizes to the centrosome and its associated microtubule array.pintraciliary transport [GO:0042073]; photoreceptor cell maintenance [GO:0045494]; protein transport [GO:0015031]Jaxoneme [GO:0005930]; ciliary basal body [GO:0036064]; cilium [GO:0005929]HFUNCTION: Might be involved in minus end-directed microtubule transport.P57764GSDMD Gasdermin-D8cellular response to extracellular stimulus [GO:0031668]Q9H8P0POREDPolyprenol reductaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20637498}; Multi-pass membrane protein {ECO:0000305|PubMed:20637498}.androgen biosynthetic process [GO:0006702]; cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichol metabolic process [GO:0019348]; dolichyl diphosphate biosynthetic process [GO:0006489]; polyprenol catabolic process [GO:0016095]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]3-oxo-5-alpha-steroid 4-dehydrogenase activity [GO:0003865]; cholestenone 5-alpha-reductase activity [GO:0047751]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]2FUNCTION: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT). {ECO:0000269|PubMed:17986282, ECO:0000269|PubMed:20637498}.Q86SK9SCD5Stearoyl-CoA desaturase 5SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:15907797}.Ometal ion binding [GO:0046872]; stearoyl-CoA 9-desaturase activity [GO:0004768]FUNCTION: Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:15610069). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797}.Q5R372RBG1L$Rab GTPase-activating protein 1-likedpositive regulation of GTPase activity [GO:0043547]; regulation of protein localization [GO:0032880]Oearly endosome [GO:0005769]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]P48739PIPNB2Phosphatidylinositol transfer protein beta isoformMSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. glycerophospholipid biosynthetic process [GO:0046474]; in utero embryonic development [GO:0001701]; lipid metabolic process [GO:0006629]; phospholipid metabolic process [GO:0006644]; phospholipid transport [GO:0015914]; small molecule metabolic process [GO:0044281]lendoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]Q14195DPYL3%Dihydropyrimidinase-related protein 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone. {ECO:0000250}.actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; axon guidance [GO:0007411]; cellular response to cytokine stimulus [GO:0071345]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron projection development [GO:0010977]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of neuron projection development [GO:0010976]; protein homooligomerization [GO:0051260]; response to axon injury [GO:0048678]chondroitin sulfate binding [GO:0035374]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; SH3 domain binding [GO:0017124]cell body [GO:0044297]; cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]; filamentous actin [GO:0031941]; growth cone [GO:0030426]; lamellipodium [GO:0030027]FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity). {ECO:0000250}.P56199ITA1Integrin alpha-1activation of MAPK activity [GO:0000187]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell-matrix adhesion [GO:0007160]; cellular extravasation [GO:0045123]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; muscle contraction [GO:0006936]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neutrophil chemotaxis [GO:0030593]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; vasodilation [GO:0042311]collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; metal ion binding [GO:0046872]; protein phosphatase binding [GO:0019903]acrosomal vesicle [GO:0001669]; basal part of cell [GO:0045178]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integrin alpha1-beta1 complex [GO:0034665]; integrin complex [GO:0008305]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}.O43598DNPH1-2'-deoxynucleoside 5'-phosphate N-hydrolase 1SUBCELLULAR LOCATION: Cyt< oplasm {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:18726892}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03036}.cell proliferation [GO:0008283]; deoxyribonucleoside monophosphate catabolic process [GO:0009159]; epithelial cell differentiation [GO:0030855]; nucleoside metabolic process [GO:0009116]; nucleotide metabolic process [GO:0009117]; positive regulation of cell growth [GO:0030307]deoxyribonucleoside 5'-monophosphate N-glycosidase activity [GO:0070694]; nucleoside deoxyribosyltransferase activity [GO:0050144]sFUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases. {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359}.O60563CCNT1 Cyclin-T1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12944466}.cell cycle [GO:0007049]; cell division [GO:0051301]; gene expression [GO:0010467]; negative regulation of mRNA polyadenylation [GO:1900364]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; transcription, DNA-templated [GO:0006351]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; snRNA binding [GO:0017069]; transcription regulatory region DNA binding [GO:0044212]onucleoplasm [GO:0005654]; nucleus [GO:0005634]; positive transcription elongation factor complex b [GO:0008024]FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. {ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377}.Q2KJY2KI26BKinesin-like protein KIF26BUSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305}.establishment of cell polarity [GO:0030010]; positive regulation of cell-cell adhesion [GO:0022409]; ureteric bud invasion [GO:0072092] FUNCTION: Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.O00571DDX3X ATP-dependent RNA helicase DDX3XSUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Mitochondrion outer membrane. Note=Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplasm in a XPO1 and may be also in a NFX1-dependent manner. Associated with polyadenylated mRNAs in the cytoplasm and the nucleus. Predominantly located in nucleus during G(0) phase and in the cytoplasm during G1/S phase.cellular response to arsenic-containing substance [GO:0071243]; cellular response to osmotic stress [GO:0071470]; chromosome segregation [GO:0007059]; DNA duplex unwinding [GO:0032508]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; mature ribosome assembly [GO:0042256]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of protein complex assembly [GO:0031333]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell growth [GO:0030307]; positive regulation of chemokine (C-C motif) ligand 5 production [GO:0071651]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of gene expression [GO:0010628]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of translation [GO:0045727]; positive regulation of translational initiation [GO:0045948]; positive regulation of viral genome replication [GO:0045070]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; stress granule assembly [GO:0034063]; transcription, DNA-templated [GO:0006351]; translational initiation [GO:0006413]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; ATP-dependent RNA helicase activity [GO:0004004]; CTPase activity [GO:0043273]; DNA binding [GO:0003677]; eukaryotic initiation factor 4E binding [GO:0008190]; GTPase activity [GO:0003924]; mRNA 5'-UTR binding [GO:0048027]; nucleoside-triphosphatase activity [GO:0017111]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; RNA stem-loop binding [GO:0035613]; transcription factor binding [GO:0008134]; translation initiation factor binding [GO:0031369]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; extracellular exosome [GO:0070062]; mitochondrial outer membrane [GO:0005741]; nuclear speck [GO:0016607]; nucleus [GO:0005634]#FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to co< ver translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in hepatitis C virus (HCV) replication; the function may involve the association with HCV core protein. HCV core protein inhibits the IPS1-dependent function in viral RNA sensing and may switch the function from a INFB inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs. {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16301996, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20375222, ECO:0000269|PubMed:20657822, ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23478265}.Q9NZI8IF2B13Insulin-like growth factor 2 mRNA-binding protein 1BSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cell projection, lamellipodium. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone. Cell projection, filopodium {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by the NMDA receptor agonist (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies. {ECO:0000250}.CRD-mediated mRNA stabilization [GO:0070934]; gene expression [GO:0010467]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; neuronal stem cell maintenance [GO:0097150]; pallium cell proliferation in forebrain [GO:0022013]; regulation of cytokine biosynthetic process [GO:0042035]; regulation of mRNA stability involved in response to stress [GO:0010610]mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; translation regulator activity [GO:0045182]saxon [GO:0030424]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:0030529]FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and poss< ibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250, ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:8132663, ECO:0000269|PubMed:9891060}.Q9UBS8RNF14!E3 ubiquitin-protein ligase RNF14cSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9853615}. Nucleus {ECO:0000269|PubMed:9853615}.androgen receptor signaling pathway [GO:0030521]; positive regulation of transcription, DNA-templated [GO:0045893]; protein ubiquitination [GO:0016567]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]androgen receptor binding [GO:0050681]; ligase activity [GO:0016874]; transcription coactivator activity [GO:0003713]; ubiquitin-like protein transferase activity [GO:0019787]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]QFUNCTION: Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription. {ECO:0000269|PubMed:19345326}.Q9C0H2TTYH3Protein tweety homolog 3}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15010458}; Multi-pass membrane protein {ECO:0000269|PubMed:15010458}.chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]nchloride channel activity [GO:0005254]; intracellular calcium activated chloride channel activity [GO:0005229]gchloride channel complex [GO:0034707]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. {ECO:0000269|PubMed:15010458}.Q9P299COPZ2Coatomer subunit zeta-2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows a significant preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi network. {ECO:0000250}.Uintracellular protein transport [GO:0006886]; vesicle-mediated transport [GO:0016192]cis-Golgi network [GO:0005801]; COPI vesicle coat [GO:0030126]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]|FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). {ECO:0000250}.Q5VWQ8DAB2P&Disabled homolog 2-interacting proteingSUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Membrane. Cell projection, dendrite {ECO:0000250}. Note=Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum (By similarity). Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization. {ECO:0000250}.activation of JUN kinase activity [GO:0007257]; activation of MAPKKK activity [GO:0000185]; activation of signaling protein activity involved in unfolded protein response [GO:0006987]; angiogenesis [GO:0001525]; cell cycle [GO:0007049]; cell motility involved in cerebral cortex radial glia guided migration [GO:0021814]; cellular protein catabolic process [GO:0044257]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endothelial cell apoptotic process [GO:0072577]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; I-kappaB phosphorylation [GO:0007252]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; layer formation in cerebral cortex [GO:0021819]; negative regulation of angiogenesis [GO:0016525]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of catenin import into nucleus [GO:0035414]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cyclin catabolic process [GO:2000599]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulat< ion of G0 to G1 transition [GO:0070317]; negative regulation of GTPase activity [GO:0034260]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of phosphatidylinositol 3-kinase activity [GO:0043553]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; negative regulation of vascular endothelial growth factor signaling pathway [GO:1900747]; neuron projection morphogenesis [GO:0048812]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of dendrite development [GO:1900006]; positive regulation of GTPase activity [GO:0043547]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of synapse maturation [GO:0090129]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; reelin-mediated signaling pathway [GO:0038026]; regulation of growth [GO:0040008]; regulation of GTPase activity [GO:0043087]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; regulation of p38MAPK cascade [GO:1900744]; regulation of protein complex assembly [GO:0043254]; regulation of protein heterodimerization activity [GO:0043497]; transformed cell apoptotic process [GO:0006927]; tube formation [GO:0035148]; vascular endothelial growth factor receptor-2 signaling pathway [GO:0036324]W14-3-3 protein binding [GO:0071889]; death receptor binding [GO:0005123]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; mitogen-activated protein kinase kinase binding [GO:0031434]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; phosphatidylinositol 3-kinase binding [GO:0043548]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; protein complex binding [GO:0032403]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein phosphatase 2A binding [GO:0051721]; SH3 domain binding [GO:0017124]; signaling adaptor activity [GO:0035591]; vascular endothelial growth factor receptor 2 binding [GO:0043184]AIP1-IRE1 complex [GO:1990597]; axon [GO:0030424]; cerebellar mossy fiber [GO:0044300]; climbing fiber [GO:0044301]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; parallel fiber [GO:1990032]; plasma membrane [GO:0005886]R FUNCTION: Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18292600, ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:21700930, ECO:0000269|PubMed:22696229}.Q5JS54PSMG4Proteasome assembly chaperone 4JFUNCTION: Chaperone protein which promotes assembly of the 20S proteasome.Q0VDG4SCRN3 Secernin-3P27708PYR1 CAD proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15890648}. Nucleus {ECO:0000269|PubMed:15890648}. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth.de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; arginine biosynthetic process [GO:0006526]; cellular response to drug [GO:0035690]; cellular response to epidermal growth factor stimulus [GO:0071364]; drug metabolic process [GO:0017144]; female pregnancy [GO:0007565]; glutamine metabolic process [GO:0006541]; heart development [GO:0007507]; lactation [GO:0007< 595]; liver development [GO:0001889]; nucleobase-containing small molecule metabolic process [GO:0055086]; organ regeneration [GO:0031100]; peptidyl-threonine phosphorylation [GO:0018107]; protein autophosphorylation [GO:0046777]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; response to amine [GO:0014075]; response to caffeine [GO:0031000]; response to cortisol [GO:0051414]; response to testosterone [GO:0033574]; small molecule metabolic process [GO:0044281]; urea cycle [GO:0000050]; UTP biosynthetic process [GO:0006228]aspartate binding [GO:0070335]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; zinc ion binding [GO:0008270]Mcell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; terminal bouton [GO:0043195]FUNCTION: This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase). {ECO:0000269|PubMed:24332717}.P22694KAPCB4cAMP-dependent protein kinase catalytic subunit betaPRKACA/B/C/PRKXSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Nucleus {ECO:0000250}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250}.activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; blood coagulation [GO:0007596]; carbohydrate metabolic process [GO:0005975]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:1901621]; neural tube closure [GO:0001843]; neurotrophin TRK receptor signaling pathway [GO:0048011]; protein phosphorylation [GO:0006468]; regulation of insulin secretion [GO:0050796]; regulation of protein processing [GO:0070613]; renal water homeostasis [GO:0003091]; response to clozapine [GO:0097338]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; triglyceride catabolic process [GO:0019433]; water transport [GO:0006833]ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; ubiquitin protein ligase binding [GO:0031625]cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. {ECO:0000269|PubMed:12420224, ECO:0000269|PubMed:21423175}.O94868FCSD2$FCH and double SH3 domains protein 2Q9H7M9GI24Platelet receptor Gi24SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20666777}; Single-pass type I membrane protein {ECO:0000269|PubMed:20666777}.WBMP signaling pathway [GO:0030509]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of T cell cytokine production [GO:0002725]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of stem cell differentiation [GO:2000738]; stem cell differentiation [GO:0048863]VFUNCTION: May stimulate MMP14-mediated MMP2 activation. {ECO:0000269|PubMed:20666777}.Q32MZ4LRRF14Leucine-rich repeat flightless-interacting protein 1innate immune response [GO:0045087]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of type I interferon production [GO:0032481]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]rDNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; protein homodimerization activity [GO:0042803]{cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]VFUNCTION: Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding. {ECO:0000269|PubMed:10364563, ECO:0000269|PubMed:14522076, ECO:0000269|PubMed:16199883, ECO:0000269|PubMed:19265123, ECO:0000269|PubMed:9705290}.P57088TMM33Transmembrane protein 33SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.cellular protein localization [GO:0034613]; endoplasmic reticulum tubular network organization [GO:0071786]; nuclear pore complex assembly [GO:0051292]zendoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; nuclear pore [GO:0005643]P58557YBEYPutative ribonuclease<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22042635}.Jmetal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]P42356PI4KA#Phosphatidylinositol 4-kinase alphaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Associates with the membranes of Golgi vesicles and vacuoles. {ECO:0000250}.phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]O1-phosphatidylinositol 4-kinase activity [GO:0004430]; ATP binding [GO:0005524]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi-associated vesicle membrane [GO:0030660]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.O43294TGFI1>Transforming growth factor beta-1-induced transcript 1 proteinSUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton; colocalizes with stress fibers.Sandrogen receptor signaling pat< hway [GO:0030521]; cell adhesion [GO:0007155]; cell fate commitment [GO:0045165]; epithelial cell differentiation [GO:0030855]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of cell proliferation [GO:0008285]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; response to heat [GO:0009408]; transcription from RNA polymerase II promoter [GO:0006366]; ubiquitin-dependent SMAD protein catabolic process [GO:0030579]; Wnt signaling pathway [GO:0016055]androgen receptor binding [GO:0050681]; I-SMAD binding [GO:0070411]; Roundabout binding [GO:0048495]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; nuclear matrix [GO:0016363]iFUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:12445807, ECO:0000269|PubMed:12700349, ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15561701, ECO:0000269|PubMed:16141357, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9032249}.O14639ABLM1Actin-binding LIM protein 1Factin family cytoskeletal protein(PC00041);structural protein(PC00211)SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with the cytoskeleton. {ECO:0000250}.axon guidance [GO:0007411]; cilium assembly [GO:0042384]; cytoskeleton organization [GO:0007010]; lamellipodium assembly [GO:0030032]; organ morphogenesis [GO:0009887]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; visual perception [GO:0007601]9actin binding [GO:0003779]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; neuronal postsynaptic density [GO:0097481]; stress fiber [GO:0001725]FUNCTION: May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance. {ECO:0000250, ECO:0000269|PubMed:9245787}.Q68EM7RHG17 Rho GTPase-activating protein 17SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm. Cell junction, tight junction. Note=Associates with membranes and concentrates at sites of cell-cell contact.Zbicellular tight junction [GO:0005923]; cytosol [GO:0005829]; plasma membrane [GO:0005886]=FUNCTION: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1. {ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}.O95136S1PR2"Sphingosine 1-phosphate receptor 2actin cytoskeleton reorganization [GO:0031532]; activation of MAPK activity [GO:0000187]; filopodium assembly [GO:0046847]; G-protein coupled receptor signaling pathway [GO:0007186]; negative regulation of excitatory postsynaptic membrane potential [GO:0090394]; positive regulation of cell proliferation [GO:0008284]; positive regulation of establishment of endothelial barrier [GO:1903142]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; sphingosine-1-phosphate signaling pathway [GO:0003376]G-protein coupled receptor activity [GO:0004930]; G-protein coupled receptor binding [GO:0001664]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; sphingosine-1-phosphate receptor activity [GO:0038036]<FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis.Q6EEV6SUMO4"Small ubiquitin-related modifier 4 protein sumoylation [GO:0016925]FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may modulate protein subcellular localization, stability or activity. Upon oxidative stress, conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. May also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. {ECO:0000269|PubMed:15123604, ECO:0000269|PubMed:15247916, ECO:0000269|PubMed:16236267}.P20340RAB6ARas-related protein Rab-6AlSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:23091056}. Golgi apparatus membrane; Lipid-anchor.antigen processing and presentation [GO:0019882]; early endosome to Golgi transport [GO:0034498]; minus-end-directed organelle transport along microtubule [GO:0072385]; peptidyl-cysteine methylation [GO:0018125]; protein localization to Golgi apparatus [GO:0034067]; protein targeting to Golgi [GO:0000042]; Rab protein signal transduction [GO:0032482]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; viral process [GO:0016032]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin V binding [GO:0031489]; protein domain specific binding [GO:0019904] cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endosome to plasma membrane transport vesicle [GO:0070381]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]FUNCTION: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity.P28290SSFA2Sperm-specific antigen 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14673706}. Note=Located near the plasma membrane. Associated with actin filaments. May also exist as a membrane-bound form with extracellular regions.dcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]P05121PAI1!Plasminogen activator inhibitor 1angiogenesis [GO:0001525]; blood coagulation [GO:0007596]; cellular response to lipopolysaccharide [GO:0071222]; chronological cell aging [GO:0001300]; circadian rhythm [GO:0007623]; defense response to Gram-negative bacterium [GO:0050829]; extracellular matrix organization [GO:0030198]; fibrinolysis [GO:0042730]; gene expression [GO:001< 0467]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of cell migration [GO:0030336]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of smooth muscle cell-matrix adhesion [GO:2000098]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of vascular wound healing [GO:0061044]; negative regulation of wound healing [GO:0061045]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood coagulation [GO:0030194]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of leukotriene production involved in inflammatory response [GO:0035491]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of receptor activity [GO:0010469]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]wprotease binding [GO:0002020]; receptor binding [GO:0005102]; serine-type endopeptidase inhibitor activity [GO:0004867]extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]FUNCTION: Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis. {ECO:0000269|PubMed:15853774}.Q5T5Y3CAMP12Calmodulin-regulated spectrin-associated protein 1oSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19508979}. Note=Associates with microtubules.cytoskeleton organization [GO:0007010]; neuron projection development [GO:0031175]; regulation of cell morphogenesis [GO:0022604]`calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; spectrin binding [GO:0030507]FUNCTION: Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth. {ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24117850}.Q9H9B4SFXN1Sideroflexin-1lerythrocyte differentiation [GO:0030218]; iron ion homeostasis [GO:0055072]; iron ion transport [GO:0006826]3ion transmembrane transporter activity [GO:0015075]zFUNCTION: Might be involved in the transport of a component required for iron utilization into or out of the mitochondria.Q8IV38ANKY23Ankyrin repeat and MYND domain-containing protein 2<SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.cilium [GO:0005929]_FUNCTION: May be involved in the trafficking of signaling proteins to the cilia. {ECO:0000250}.Q9Y266NUDCNuclear migration protein nudCWSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Note=In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells. A small proportion is nuclear, in a punctate pattern.cell division [GO:0051301]; cell proliferation [GO:0008283]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; multicellular organismal development [GO:0007275]; small GTPase mediated signal transduction [GO:0007264]`cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]'FUNCTION: Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation. {ECO:0000250, ECO:0000269|PubMed:12679384, ECO:0000269|PubMed:12852857}.O75419CDC45(Cell division control protein 45 homologDNA duplex unwinding [GO:0032508]; DNA replication [GO:0006260]; DNA replication checkpoint [GO:0000076]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair via break-induced replication [GO:0000727]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; mitotic DNA replication preinitiation complex assembly [GO:1902977]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; pre-replicative complex assembly involved in nuclear cell cycle DNA replication [GO:0006267]; regulation of chromatin silencing at telomere [GO:0031938]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]3'-5' DNA helicase activity [GO:0043138]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; single-stranded DNA binding [GO:0003697]centrosome [GO:0005813]; cytoplasm [GO:0005737]; DNA replication preinitiation complex [GO:0031261]; nuclear pre-replicative complex [GO:0005656]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]AFUNCTION: Required for initiation of chromosomal DNA replication.Q5JTB6PLAC9Placenta-specific protein 9P69905HBAHemoglobin subunit alphabicarbonate transport [GO:0015701]; hydrogen peroxide catabolic process [GO:0042744]; oxidation-reduction process [GO:0055114]; oxygen transport [GO:0015671]; positive regulation of cell death [GO:0010942]; protein heterooligomerization [GO:0051291]; receptor-mediated endocytosis [GO:0006898]; response to hydrogen peroxide [GO:0042542]; small molecule metabolic process [GO:0044281]heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxygen binding [GO:0019825]; oxygen transporter activity [GO:0005344]8blood microparticle [GO:0072562]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]; membrane [GO:0016020]WFUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.P51149RAB7ARas-related protein Rab-7aJSUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:21255211}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:20028791}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:20028791}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:20028791}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Note=Colocalizes with OSBPL1A at the late endosome (PubMed:16176980). Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts. Recruited to phagosomes containing S.aureus or Mycobacterium (PubMed:21255211). Lipid droplet localization is increased upon ADRB2 stimulation (By similarity). {ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:16176980< , ECO:0000269|PubMed:21255211}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; bone resorption [GO:0045453]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; epidermal growth factor catabolic process [GO:0007174]; phagosome acidification [GO:0090383]; phagosome-lysosome fusion [GO:0090385]; phagosome maturation [GO:0090382]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of viral process [GO:0048524]; protein targeting to lysosome [GO:0006622]; protein to membrane docking [GO:0022615]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of autophagosome assembly [GO:2000785]; retrograde transport, endosome to Golgi [GO:0042147]; viral release from host cell [GO:0019076]alveolar lamellar body [GO:0097208]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome [GO:0042470]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; pre-autophagosomal structure membrane [GO:0034045]; terminal bouton [GO:0043195]; vacuolar membrane [GO:0005774]iFUNCTION: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:11179213, PubMed:12944476, PubMed:14617358, PubMed:20028791, PubMed:21255211). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). {ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12944476, ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20028791, ECO:0000269|PubMed:21255211}.P20645MPRD-Cation-dependent mannose-6-phosphate receptorMSUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein.yendosome to lysosome transport [GO:0008333]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165]mannose binding [GO:0005537]; mannose transmembrane transporter activity [GO:0015578]; transmembrane signaling receptor activity [GO:0004888]endosome [GO:0005768]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.Q8TE77SSH3'Protein phosphatase Slingshot homolog 3SSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}.protein dephosphorylation [GO:0006470]; regulation of actin polymerization or depolymerization [GO:0008064]; regulation of axonogenesis [GO:0050770]; regulation of lamellipodium assembly [GO:0010591]actin binding [GO:0003779]; DNA binding [GO:0003677]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]Gcytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634] FUNCTION: Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). {ECO:0000250}.Q96QD8S38A2/Sodium-coupled neutral amino acid transporter 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430}; Multi-pass membrane protein {ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes (By similarity). Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal. {ECO:0000250}.&amino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; glutamate secretion [GO:0014047]; ion transport [GO:0006811]; neurotransmitter secretion [GO:0007269]; sodium ion transport [GO:0006814]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085][amino acid transmembrane transporter activity [GO:0015171]; symporter activity [GO:0015293]FUNCTION: Functions as a sodium-dependent amino acid transporter. Mediates the saturable, pH-sensitive and electrogenic cotransport of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier and in the supply of maternal nutrients to the fetus through the placenta. {ECO:0000269|PubMed:10930503, ECO:0000269|PubMed:15922329}.P15170ERF3AAEukaryotic peptide chain release factor GTP-binding subunit ERF3AG1/S transition of mitotic cell cycle [GO:0000082]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; protein methylation [GO:0006479]; translational termination [GO:0006415]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; translation release factor activity [GO:0003747]cFUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.O14646CHD1+Chromodomain-helicase-DNA-binding protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis. {ECO:0000250}.chromatin remodeling [GO:0006338]; DNA duplex unwinding [GO:0032508]; positive regulation by host of viral transcription [GO:0043923]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; DNA binding [GO:0003677]; methylated histone binding [GO:0035064]FUNCTION: ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for effic< ient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells. {ECO:0000250, ECO:0000269|PubMed:18042460}.Q9NY12GAR1)H/ACA ribonucleoprotein complex subunit 1sSUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, Cajal body. Note=Also localized to Cajal bodies (coiled bodies).cation transmembrane transport [GO:0098655]; cation transport [GO:0006812]; pseudouridine synthesis [GO:0001522]; rRNA processing [GO:0006364]Fcation channel activity [GO:0005261]; poly(A) RNA binding [GO:0044822]lbox H/ACA snoRNP complex [GO:0031429]; Cajal body [GO:0015030]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:10757788, ECO:0000269|PubMed:15044956}.Q96JH7VCIP1 Deubiquitinating protein VCIP135SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus, Golgi stack {ECO:0000250}. Note=Associated with Golgi stacks and endoplasmic reticulum. {ECO:0000250}.endoplasmic reticulum membrane fusion [GO:0016320]; Golgi reassembly [GO:0090168]; mitotic nuclear division [GO:0007067]; protein K11-linked deubiquitination [GO:0035871]; protein K48-linked deubiquitination [GO:0071108]; protein ubiquitination [GO:0016567]Tcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi stack [GO:0005795]FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity). Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. {ECO:0000250, ECO:0000269|PubMed:23827681}.Q9UIS9MBD1#Methyl-CpG-binding domain protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Nucleus speckle. Chromosome. Note=Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix (By similarity). Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes, with pericentromeric regions on chromosome 1 and with telomeric regions from several chromosomes. {ECO:0000250}.aging [GO:0007568]; heart development [GO:0007507]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of transcription, DNA-templated [GO:0045892]; neuron differentiation [GO:0030182]; regulation of DNA methylation [GO:0044030]; response to cocaine [GO:0042220]; response to estradiol [GO:0032355]; response to fluoxetine [GO:0014076]; response to nutrient levels [GO:0031667]; transcription from RNA polymerase II promoter [GO:0006366]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; methyl-CpG binding [GO:0008327]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleus [GO:0005634]FUNCTION: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters. {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:12697822, ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760, ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:9207790, ECO:0000269|PubMed:9774669}.P30101PDIA3Protein disulfide-isomerase A3SUBCELLULAR LOCATION: Endoplasmic reticulum. Endoplasmic reticulum lumen {ECO:0000250}. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.{antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cell redox homeostasis [GO:0045454]; cellular protein metabolic process [GO:0044267]; oxidation-reduction process [GO:0055114]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; protein import into nucleus [GO:0006606]; protein N-linked glycosylation via asparagine [GO:0018279]; protein retention in ER lumen [GO:0006621]; proteolysis [GO:0006508]; response to endoplasmic reticulum stress [GO:0034976]; signal transduction [GO:0007165]cysteine-type endopeptidase activity [GO:0004197]; disulfide oxidoreductase activity [GO:0015036]; phospholipase C activity [GO:0004629]; poly(A) RNA binding [GO:0044822]; protein disulfide isomerase activity [GO:0003756]cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; melanosome [GO:0042470]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; smooth endoplasmic reticulum [GO:0005790]Q02241KIF23Kinesin-like protein KIF23SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. Midbody. Note=Localizes to the interzone of mitotic spindles. Detected at the midbody during later stages of mitotic cytokinesis.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cytokinesis [GO:0000910]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle elongation [GO:0000022]; mitotic spindle midzone assembly [GO:0051256]; positive regulation of cytokinesis [GO:0032467]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]Ecentralspindlin complex [GO:0097149]; centrosome [GO:0005813]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; intercellular bridge [GO:0045171]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spind< le. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. {ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:22522702}.Q9NUG6PDRG1&p53 and DNA damage-regulated protein 16cytoplasm [GO:0005737]; prefoldin complex [GO:0016272]OFUNCTION: May play a role in chaperone-mediated protein folding. {ECO:0000305}.Q9Y5X3SNX5Sorting nexin-5ySUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:11485546}. Early endosome {ECO:0000269|PubMed:17148574, ECO:0000269|PubMed:24610942}. Early endosome membrane {ECO:0000269|PubMed:15561769}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000269|PubMed:15561769}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:18854019}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (PubMed:15561769). Detected on macropinosomes (PubMed:16968745, PubMed:21048941). Targeted to membrane ruffles in response to EGFR stimulation. {ECO:0000269|PubMed:15561769, ECO:0000269|PubMed:16968745, ECO:0000269|PubMed:21048941}.intracellular protein transport [GO:0006886]; pinocytosis [GO:0006907]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle organization [GO:0016050]Hdynactin binding [GO:0034452]; phosphatidylinositol binding [GO:0035091]wcytoplasmic vesicle membrane [GO:0030659]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of endosome membrane [GO:0031313]; macropinocytic cup [GO:0070685]; phagocytic cup [GO:0001891]; retromer complex [GO:0030904]; ruffle [GO:0001726]; tubular endosome [GO:0097422]FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) (PubMed:15561769). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:17148574, PubMed:18596235). May function as link between endosomal transport vesicles and dynactin (Probable). Plays a role in the internalization of EGFR after EGF stimulation (Probable). Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C isoform 3 and is retromer-independent (PubMed:23602387). Together with PIP5K1C isoform 3 facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation (Probable). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). Plays a role in macropinocytosis (PubMed:18854019, PubMed:21048941). {ECO:0000269|PubMed:18854019, ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:24610942, ECO:0000303|PubMed:15561769, ECO:0000303|PubMed:19619496, ECO:0000303|PubMed:23085988}.P16035TIMP2Metalloproteinase inhibitor 2caging [GO:0007568]; cellular response to organic substance [GO:0071310]; central nervous system development [GO:0007417]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of cell proliferation [GO:0008285]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of metalloenzyme activity [GO:0048553]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of adenylate cyclase activity [GO:0045762]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuron differentiation [GO:0045666]; regulation of Rap protein signal transduction [GO:0032487]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to hormone [GO:0009725]enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872]; metalloendopeptidase inhibitor activity [GO:0008191]; protease binding [GO:0002020]basement membrane [GO:0005604]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; proteinaceous extracellular matrix [GO:0005578]UFUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. {ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:2554304, ECO:0000269|PubMed:2793861}.Q9ULZ3ASC9Apoptosis-associated speck-like protein containing a CARDSUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Mitochondrion. Nucleus. Note=Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection. Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis (By similarity). {ECO:0000250}. activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of innate immune response [GO:0002218]; apoptotic process [GO:0006915]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; defense response to Gram-negative bacterium [GO:0050829]; defense response to virus [GO:0051607]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; interleukin-1 beta production [GO:0032611]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; macropinocytosis [GO:0044351]; myeloid dendritic cell activation [GO:0001773]; myeloid dendritic cell activation involved in immune response [GO:0002277]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of antigen processing and presentation of peptide antigen via MHC class II [GO:0002588]; positive regulation of apoptotic process [GO:0043065]; positive regulation of chemokine secretion [GO:0090197]; positive regulation of cysteine-type endopeptidase activity [GO:2001056]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of interferon-< gamma production [GO:0032729]; positive regulation of interleukin-10 secretion [GO:2001181]; positive regulation of interleukin-1 beta secretion [GO:0050718]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-6 secretion [GO:2000778]; positive regulation of interleukin-8 secretion [GO:2000484]; positive regulation of JNK cascade [GO:0046330]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phagocytosis [GO:0050766]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell migration [GO:2000406]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of autophagy [GO:0010506]; regulation of GTPase activity [GO:0043087]; regulation of inflammatory response [GO:0050727]; regulation of intrinsic apoptotic signaling pathway [GO:2001242]; regulation of protein stability [GO:0031647]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; signal transduction [GO:0007165]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; tumor necrosis factor-mediated signaling pathway [GO:0033209]BMP receptor binding [GO:0070700]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; interleukin-6 receptor binding [GO:0005138]; myosin I binding [GO:0017024]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; Pyrin domain binding [GO:0032090]; tropomyosin binding [GO:0005523]\AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; IkappaB kinase complex [GO:0008385]; mitochondrion [GO:0005739]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]; nucleolus [GO:0005730]; nucleus [GO:0005634] FUNCTION: Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. {ECO:0000269|PubMed:11103777, ECO:0000269|PubMed:12486103, ECO:0000269|PubMed:12646168, ECO:0000269|PubMed:14499617, ECO:0000269|PubMed:14730312, ECO:0000269|PubMed:15030775, ECO:0000269|PubMed:16585594, ECO:0000269|PubMed:16964285, ECO:0000269|PubMed:16982856, ECO:0000269|PubMed:17349957, ECO:0000269|PubMed:17599095, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19234215, ECO:0000269|PubMed:19494289, ECO:0000269|PubMed:21487011, ECO:0000269|PubMed:22732093}.Q86TI2DPP9Dipeptidyl peptidase 9SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15245913}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:24562348}.yaminopeptidase activity [GO:0004177]; identical protein binding [GO:0042802]; serine-type peptidase activity [GO:0008236]~FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.Q16836HCDH3Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialcellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; negative regulation of insulin secretion [GO:0046676]; response to activity [GO:0014823]; response to drug [GO:0042493]; response to insulin [GO:0032868]; small molecule metabolic process [GO:0044281]P3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; NAD+ binding [GO:0070403]cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.Q8WY22BRI3BBRI3-binding proteinSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305|PubMed:17943721}; Multi-pass membrane protein {ECO:0000305|PubMed:17943721}.lFUNCTION: Involved in tumorigenesis and may function by stabilizing p53/TP53. {ECO:0000269|PubMed:17943721}.O00264PGRC15Membrane-associated progesterone receptor component 1SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.axon guidance [GO:0007411]7heme binding [GO:0020037]; steroid binding [GO:0005496]endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleolus [GO:0005730]3FUNCTION: Receptor for progesterone. {ECO:0000250}.Q9P0I2EMC3%ER membrane protein complex subunit 35protein folding in endoplasmic reticulum [GO:0034975]Q96BK5PINX1-PIN2/TERF1-interacting telomerase inhibitor 1(SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome, telomere. Chromosome, centromere, kinetochore. Note=Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore is mediated by its central region and depends on NDC80 and CENPE.mitotic metaphase plate congression [GO:0007080]; negative regulation of cell proliferation [GO:0008285]; negative regulation of telomerase activity [GO:0051974]; regulation of t< elomerase activity [GO:0051972]; telomere maintenance via telomerase [GO:0007004]Ntelomerase inhibitor activity [GO:0010521]; telomeric RNA binding [GO:0070034]\chromosome, telomeric region [GO:0000781]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; kinetochore [GO:0000776]; mitochondrion [GO:0005739]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor. {ECO:0000269|PubMed:15381700, ECO:0000269|PubMed:17198684, ECO:0000269|PubMed:19117989, ECO:0000269|PubMed:19265708, ECO:0000269|PubMed:19393617, ECO:0000269|PubMed:19553660}.P35232PHB Prohibitin`cellular response to interleukin-6 [GO:0071354]; DNA biosynthetic process [GO:0071897]; histone deacetylation [GO:0016575]; mitochondrion organization [GO:0007005]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of glucocorticoid receptor signaling pathway [GO:2000323]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of complement activation [GO:0045917]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G-protein coupled receptor protein signaling pathway [GO:0045745]; positive regulation of transcription, DNA-templated [GO:0045893]; progesterone receptor signaling pathway [GO:0050847]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription from RNA polymerase II promoter [GO:0006366]complement component C3a binding [GO:0001850]; complement component C3b binding [GO:0001851]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; proteinase activated receptor binding [GO:0031871]; protein C-terminus binding [GO:0008022]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; transcription regulatory region DNA binding [GO:0044212]ncell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging. {ECO:0000269|PubMed:11302691}.O00139KIF2AKinesin-like protein KIF2ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, spindle. Note=Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cell division [GO:0051301]; microtubule-based movement [GO:0007018]; microtubule depolymerization [GO:0007019]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; nervous system development [GO:0007399]; small GTPase mediated signal transduction [GO:0007264]|ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule motor activity [GO:0003777]; motor activity [GO:0003774]centrosome [GO:0005813]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; sperm principal piece [GO:0097228]; spindle pole [GO:0000922]FUNCTION: Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity. {ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:17538014, ECO:0000269|PubMed:18411309}.Q9NQC7CYLD*Ubiquitin carboxyl-terminal hydrolase CYLDribosomal protein(PC00202)SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25134987}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25134987}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80TQ2}. Note=Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase. During metaphase, it remains localized to the centrosome but is also present along the spindle (PubMed:25134987). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:25134987}.hcell cycle [GO:0007049]; innate immune response [GO:0045087]; necroptotic process [GO:0070266]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of NF-kappaB import into nucleus [GO:0042347]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of T cell differentiation [GO:0045581]; negative regulation of type I interferon production [GO:0032480]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; protein K63-linked deubiquitination [GO:0070536]; regulation of cilium assembly [GO:1902017]; regulation of intrinsic apoptotic signaling pathway [GO:2001242]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of mitotic cell cycle [GO:0007346]; ripoptosome assembly involved in necroptotic process [GO:1901026]; ubiquitin-dependent protein catabolic process [GO:0006511]; Wnt signaling pathway [GO:0016055]Lys63-specific deubiquitinase activity [GO:0061578]; proline-rich region binding [GO:0070064]; protein kinase binding [GO:0019901]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270])centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]FUNCTION: Protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Has endodeubiquitinase activity. Plays an important role in the regulation of pathways leading to NF-kappa-B activation (PubMed:12917689, PubMed:12917691). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:12917690). Negative regulator of Wnt signaling (PubMed:20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regula< tion of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:17495026, PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (PubMed:18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). {ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:12917691, ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18222923, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:20227366}.Q8N8E3CE112Centrosomal protein of 112 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes around spindle poles in some cells. {ECO:0000269|PubMed:21399614}.-receptor localization to synapse [GO:0097120]ncentrosome [GO:0005813]; cytoplasm [GO:0005737]; inhibitory synapse [GO:0060077]; plasma membrane [GO:0005886]Q8WXC3PYDC1!Pyrin domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12656673}. Note=Recruited to specks formed by PYCARD within the cytoplasm. {ECO:0000269|PubMed:17178784}.innate immune response [GO:0045087]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; positive regulation of interleukin-1 beta secretion [GO:0050718]; tumor necrosis factor-mediated signaling pathway [GO:0033209]Ocytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; nucleus [GO:0005634]FUNCTION: Associates with PYCARD/ASC and modulates its ability to collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-caspase-1 activation. Suppresses kinase activity of NF-kappa-B inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible genes and inhibits NF-kappa-B activation by cytokines and LPS. {ECO:0000269|PubMed:12656673, ECO:0000269|PubMed:24871464}.Q8TDZ2MICA1+Protein-methionine sulfoxide oxidase MICAL19SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.dactin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of protein phosphorylation [GO:0001933]; oxidation-reduction process [GO:0055114]; signal transduction [GO:0007165]; sulfur oxidation [GO:0019417]'actin binding [GO:0003779]; FAD binding [GO:0071949]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270]:cytoplasm [GO:0005737]; intermediate filament [GO:0005882]fFUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. {ECO:0000269|PubMed:18305261, ECO:0000269|PubMed:21864500, ECO:0000305}.Q8NCL4GALT6/Polypeptide N-acetylgalactosaminyltransferase 6Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]6FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides.Q5NDL2EOGT<EGF domain-specific O-linked N-acetylglucosamine transferase+protein O-linked glycosylation [GO:0006493]=protein N-acetylglucosaminyltransferase activity [GO:0016262]{FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. {ECO:0000269|PubMed:23671640}.Q14061COX17%Cytochrome c oxidase copper chaperonebrain development [GO:0007420]; copper ion transport [GO:0006825]; generation of precursor metabolites and energy [GO:0006091]; heart development [GO:0007507]Gcopper chaperone activity [GO:0016531]; copper ion binding [GO:0005507]bcytoplasm [GO:0005737]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]FUNCTION: Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX (By similarity). {ECO:0000250}.Q68E01INT3Integrator complex subunit 3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following DNA damage.cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; mitotic cell cycle checkpoint [GO:0007093]; response to ionizing radiation [GO:0010212]; snRNA processing [GO:0016180]Pintegrator complex [GO:0032039]; nucleus [GO:0005634]; SOSS complex [GO:0070876]FUNCTION: Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.; FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites.Q15149PLECPlectinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12482924}. Cell junction, hemidesmosome {ECO:0000269|PubMed:12482924}.apoptotic process [GO:0006915]; cell junction assembly [GO:0034329]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581]; programmed cell death [GO:0012501]mankyrin binding [GO:0030506]; poly(A) RNA binding [GO:0044822]; structural constituent of muscle [GO:0008307]=brush border [GO:0005903]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; hemidesmosome [GO:0030056]; intermediate filament cytoskeleton [GO:0045111]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]FUNCTION: Interlinks intermediate filaments with microtubules< and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity. {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:21109228}.Q9UIM3FKBPLFK506-binding protein-likechaperone-mediated protein folding [GO:0061077]; protein peptidyl-prolyl isomerization [GO:0000413]; response to radiation [GO:0009314]Ccytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]FUNCTION: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21. {ECO:0000269|PubMed:15664193}.Q8WYH8ING5Inhibitor of growth protein 5<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358}.chromatin organization [GO:0006325]; DNA replication [GO:0006260]; histone H3 acetylation [GO:0043966]; negative regulation of cell proliferation [GO:0008285]; negative regulation of growth [GO:0045926]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of transcription, DNA-templated [GO:0045893]; protein acetylation [GO:0006473]; transcription, DNA-templated [GO:0006351]fchromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; zinc ion binding [GO:0008270]gMOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator. {ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:16387653}.Q567U6CCD93(Coiled-coil domain-containing protein 93CSUBCELLULAR LOCATION: Early endosome {ECO:0000305|PubMed:25355947}.dFUNCTION: Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with FAM21C (PubMed:25355947). {ECO:0000269|PubMed:25355947}.Q9NSA3CNBP1"Beta-catenin-interacting protein 1Zanterior/posterior pattern specification [GO:0009952]; branching involved in ureteric bud morphogenesis [GO:0001658]; negative regulation of DNA binding [GO:0043392]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of protein binding [GO:0032091]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription initiation from RNA polymerase II promoter [GO:0060633]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of vascular permeability involved in acute inflammatory response [GO:0002528]; Wnt signaling pathway [GO:0016055]Oarmadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]beta-catenin destruction complex [GO:0030877]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway. {ECO:0000269|PubMed:12408824}.P10515ODP2hDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialhacetyl-CoA biosynthetic process from pyruvate [GO:0006086]; cellular metabolic process [GO:0044237]; glucose metabolic process [GO:0006006]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; sleep [GO:0030431]; small molecule metabolic process [GO:0044281]; tricarboxylic acid cycle [GO:0006099]Cdihydrolipoyllysine-residue acetyltransferase activity [GO:0004742]mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; pyruvate dehydrogenase complex [GO:0045254]FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.P53609PGTB1.Geranylgeranyl transferase type-1 subunit betanegative regulation of nitric-oxide synthase biosynthetic process [GO:0051771]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; protein geranylgeranylation [GO:0018344]; response to cytokine [GO:0034097]CAAX-protein geranylgeranyltransferase activity [GO:0004662]; drug binding [GO:0008144]; isoprenoid binding [GO:0019840]; peptide binding [GO:0042277]; protein geranylgeranyltransferase activity [GO:0004661]; zinc ion binding [GO:0008270];CAAX-protein geranylgeranyltransferase complex [GO:0005953]2FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B. {ECO:0000269|PubMed:8106351}.Q9BU89DOHHDeoxyhypusine hydroxylasecellular protein metabolic process [GO:0044267]; peptidyl-lysine modification to peptidyl-hypusine [GO:0008612]; post-translational protein modification [GO:0043687]Qdeoxyhypusine monooxygenase activity [GO:0019135]; metal ion binding [GO:0046872]FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor. {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:16371467, ECO:0000269|PubMed:19706422}.Q96SL4GPX7Glutathione peroxidase 7ncatalase activity [GO:0004096]; glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]oendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]FUNCTION: It protects esophageal epithelia from hydrogen peroxide-induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks. {ECO:0000269|PubMed:22157330}.Q9BUT9F195AProtein FAM195AQ6P587FAHD1!Acylpyruvase FAHD1, mitochondrialtSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21878618}. Cytoplasm, cytosol {ECO:0000269|PubMed:21878618}.acetylpyruvate hydrolase activity [GO:0018773]; acylpyruvate hydrolase activity [GO:0047621]; fumarylpyruvate hydrolase activity [GO:0034545]; metal ion binding [GO:0046872]; oxaloacetate decarboxylase activity [GO:0008948]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]1FUNCTION: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (PubMed:15551868, PubMed:21878618). Also has oxaloacetate decarboxylase activity (PubMed:25575590). {ECO:0000269|PubMed:15551868, ECO:0000269|PubMed:21878618, ECO:0000269|PubMed:25575590}.P33908MA1A11Mannosyl-oligosaccharide 1,2-alpha-mannosidase IAcalcium ion binding [GO:0005509]; mannosidase activity [GO:0015923]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021];< membrane [GO:0016020]Q8IXT5RB12BRNA-binding protein 12BP52888THOP1Thimet oligopeptidaseFUNCTION: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.Q92541RTF1.RNA polymerase-associated protein RTF1 homolog9SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.blastocyst growth [GO:0001832]; DNA-templated transcription, initiation [GO:0006352]; endodermal cell fate commitment [GO:0001711]; histone H3-K4 trimethylation [GO:0080182]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; stem cell maintenance [GO:0019827]; transcription elongation from RNA polymerase II promoter [GO:0006368]; Wnt signaling pathway [GO:0016055]Jpoly(A) RNA binding [GO:0044822]; single-stranded DNA binding [GO:0003697]7Cdc73/Paf1 complex [GO:0016593]; nucleolus [GO:0005730]FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Binds single-stranded DNA. Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex (By similarity). {ECO:0000250}.Q8TCY9URGCP"Up-regulator of cell proliferationSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}. Nucleus {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}. Note=In epithelial cells localized predominantly in the cytoplasm and occasionally in nuclei.RFUNCTION: May be involved in cell cycle progression through the regulation of cyclin D1 expression. May participate in the development of hepatocellular carcinoma (HCC) by promoting hepatocellular growth and survival. May play an important role in development of gastric cancer. {ECO:0000269|PubMed:12082552, ECO:0000269|PubMed:17217616}.Q96RR4KKCC24Calcium/calmodulin-dependent protein kinase kinase 2CAMKKSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:21957496}. Cell projection {ECO:0000269|PubMed:21957496}. Note=Predominantly nuclear in unstimulated cells (By similarity). Found in the cytoplasm and neurites after forskolin induction. {ECO:0000250}.8calcium-mediated signaling [GO:0019722]; MAPK cascade [GO:0000165]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of transcription, DNA-templated [GO:0045893]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of protein kinase activity [GO:0045859]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein tyrosine kinase activity [GO:0004713]fcell projection [GO:0042995]; cytoplasm [GO:0005737]; intracellular [GO:0005622]; nucleus [GO:0005634]{FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching. {ECO:0000250, ECO:0000269|PubMed:11395482, ECO:0000269|PubMed:12935886, ECO:0000269|PubMed:21957496, ECO:0000269|PubMed:9662074}.P30281CCND3G1/S-specific cyclin-D36SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15358120}. Cytoplasm {ECO:0000269|PubMed:15358120}. Membrane {ECO:0000269|PubMed:15358120}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. {ECO:0000250}.cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of protein phosphorylation [GO:0001934]; signal transduction [GO:0007165]; T cell proliferation [GO:0042098]kcyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]cFUNCTION: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:15358120}.Q7Z6I8CE024UPF0461 protein C5orf24Q9NYY8FAKD2'FAST kinase domain-containing protein 2P33764S10A3Protein S100-A3>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18083705}.FUNCTION: Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation. {ECO:0000269|PubMed:18083705}.P07199CENPBMajor centromere autoantigen BSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583, ECO:0000269|PubMed:18072184}. Chromosome, centromere {ECO:0000269|PubMed:18072184}.7regulation of transcription, DNA-templated [GO:0006355]centromeric DNA binding [GO:0019237]; chromatin binding [GO:0003682]; satellite DNA binding [GO:0003696]; sequence-specific DNA binding [GO:0043565]Zchromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; nucleus [GO:0005634]BFUNCTION: Interacts wi< th centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.P30519HMOX2Heme oxygenase 27SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum.!cellular iron ion homeostasis [GO:0006879]; heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; porphyrin-containing compound metabolic process [GO:0006778]; response to hypoxia [GO:0001666]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]Rheme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]`endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.P10644KAP0=cAMP-dependent protein kinase type I-alpha regulatory subunitPKA-rBSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23115245}.activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; blood coagulation [GO:0007596]; cardiac muscle cell proliferation [GO:0060038]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; female meiotic division [GO:0007143]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; mesoderm formation [GO:0001707]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; negative regulation of meiotic nuclear division [GO:0045835]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of insulin secretion [GO:0050796]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; renal water homeostasis [GO:0003091]; sarcomere organization [GO:0045214]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; water transport [GO:0006833]cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236]; ubiquitin protein ligase binding [GO:0031625]+AMP-activated protein kinase complex [GO:0031588]; cAMP-dependent protein kinase complex [GO:0005952]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; plasma membrane raft [GO:0044853]; protein complex [GO:0043234]FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:20215566}.Q13867BLMHBleomycin hydrolaseantigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]; response to drug [GO:0042493]; response to toxic substance [GO:0009636]aminopeptidase activity [GO:0004177]; carboxypeptidase activity [GO:0004180]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]#FUNCTION: The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. {ECO:0000250}.P53602MVD1!Diphosphomevalonate decarboxylase/cellular protein metabolic process [GO:0044267]; cholesterol biosynthetic process [GO:0006695]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichyl diphosphate biosynthetic process [GO:0006489]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; isoprenoid biosynthetic process [GO:0008299]; positive regulation of cell proliferation [GO:0008284]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; diphosphomevalonate decarboxylase activity [GO:0004163]; Hsp70 protein binding [GO:0030544]; protein homodimerization activity [GO:0042803]MFUNCTION: Performs the first committed step in the biosynthesis of isoprenes.Q9UBF8PI4KB"Phosphatidylinositol 4-kinase betaSUBCELLULAR LOCATION: Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus. Cytoplasm, perinuclear region. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex.Iphosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum membrane [GO:0030867]QFUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity). {ECO:0000250}.P53701CCHLCytochrome c-type heme lyaseASUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}.Jorgan morphogenesis [GO:0009887]; oxidation-reduction process [GO:0055114]Oholocytochrome-c synthase activity [GO:0004408]; metal ion binding [GO:0046872][FUNCTION: Links covalently the heme group to the apoprotein of cytochrome c. {ECO:0000250}.Q08AM6VAC14Protein VAC14 homologSUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:15542851, ECO:0000269|PubMed:17556371}. Microsome membrane {ECO:0000250}. Note=Mainly associated with membranes of the late endocytic pathway.phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; regulation of lipid kinase activity [GO:0043550]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; viral process [GO:0016032]early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; PAS complex [GO:0070772]FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts as a positive activator of PIKfyve kinase activity. Also required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:15542851, ECO:0000269|PubMed:17556371}.O43414ERI3ERI1 exoribonuclease 3DNA catabolic process, exonucleolytic [GO:0000738]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tri< cistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]m3'-5'-exoribonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]Q08170SRSF4&Serine/arginine-rich splicing factor 4DSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14578391}.gene expression [GO:0010467]; hematopoietic progenitor cell differentiation [GO:0002244]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Jnuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:15009664}.Q13564ULA1-NEDD8-activating enzyme E1 regulatory subunitE1lSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14557245}. Note=Colocalizes with APP in lipid rafts.mitotic DNA replication checkpoint [GO:0033314]; neuron apoptotic process [GO:0051402]; protein neddylation [GO:0045116]; regulation of apoptotic process [GO:0042981]; regulation of neuron apoptotic process [GO:0043523]; signal transduction [GO:0007165]NEDD8 activating enzyme activity [GO:0019781]; protein heterodimerization activity [GO:0046982]; ubiquitin protein ligase binding [GO:0031625]`cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]8FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:10722740, ECO:0000269|PubMed:12740388}.P16157ANK1 Ankyrin-1KSUBCELLULAR LOCATION: Isoform Er1: Cytoplasm, cytoskeleton. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.; SUBCELLULAR LOCATION: Isoform Mu17: Membrane. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells.; SUBCELLULAR LOCATION: Isoform Mu18: Sarcoplasmic reticulum {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform Mu19: Sarcoplasmic reticulum {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform Mu20: Sarcoplasmic reticulum {ECO:0000305}.daxon guidance [GO:0007411]; cytoskeleton organization [GO:0007010]; ER to Golgi vesicle-mediated transport [GO:0006888]; exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; positive regulation of organelle organization [GO:0010638]; protein targeting to plasma membrane [GO:0072661]; signal transduction [GO:0007165]ATPase binding [GO:0051117]; cytoskeletal adaptor activity [GO:0008093]; enzyme binding [GO:0019899]; spectrin binding [GO:0030507]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]_axolemma [GO:0030673]; basolateral plasma membrane [GO:0016323]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; M band [GO:0031430]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; spectrin-associated cytoskeleton [GO:0014731]; Z disc [GO:0030018]zFUNCTION: Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. {ECO:0000269|PubMed:12456646}.; FUNCTION: Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. {ECO:0000269|PubMed:12456646}.Q8NC96NECP1-Adaptin ear-binding coat-associated protein 1Yclathrin vesicle coat [GO:0030125]; coated pit [GO:0005905]; plasma membrane [GO:0005886]Q8NHH9ATLA2 Atlastin-2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18270207}; Multi-pass membrane protein {ECO:0000269|PubMed:18270207}.Q00839HNRPU)Heterogeneous nuclear ribonucleoprotein USUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}. Cytoplasm {ECO:0000269|PubMed:19029303}. Cell surface {ECO:0000269|PubMed:7993898}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. {ECO:0000269|PubMed:17289661}.circadian regulation of gene expression [GO:0032922]; CRD-mediated mRNA stabilization [GO:0070934]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; core promoter binding [GO:0001047]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]catalytic step 2 spliceosome [GO:0071013]; cell surface [GO:0009986]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasmic ribonucleoprotein granule [GO:0036464]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single-stranded DNA and RNA. Plays a role in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:19029303}.Q5H8A4PIGG(GPI ethanolamine phosphate transferase 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15632136}; Multi-pass membrane protein {ECO:0000269|PubMed:15632136}.cellular protein metabolic process [GO:0044267]; C-terminal protein lipidation [GO:0006501]; GPI anchor biosynthetic process [GO:0006506]; post-translational protein modification [GO:0043687]; preassembly of GPI anchor in ER membrane [GO:0016254]CP2 mannose-ethanolamine phosphotransferase activity [GO:0051267]; phosphotransferase activity, for other substituted phosphate groups [GO:0016780]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose. {ECO:0000269|PubMed:15632136}.O75431MTX2 Metaxin-2~SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:10381257}. Mitochondrion {ECO:0000269|PubMed:25997101}.cellular protein metabolic process [GO:0044267]; mitochondrial transport [GO:0006839]; protein targeting to mitochondrion [GO:0006626]Emitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]bFUNCTION: Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:10381257}.Q9BZQ8NIBAN Protein Niban>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16949643}.negative regulation of protein phosphorylation [GO:0001933]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of translation [GO:0045727]; response to endoplasmic reticulum stress [GO:0034976]ocytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Regulates phosphorylation of a number o< f proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response (By similarity). {ECO:0000250}.Q9Y5T5UBP16(Ubiquitin carboxyl-terminal hydrolase 16<SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17914355}.Vcell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to DNA damage stimulus [GO:0006974]; histone deubiquitination [GO:0016578]; histone H2A K63-linked deubiquitination [GO:0070537]; mitotic nuclear division [GO:0007067]; monoubiquitinated histone H2A deubiquitination [GO:0035522]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of translational elongation [GO:0045901]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein homotetramerization [GO:0051289]; regulation of cell cycle [GO:0051726]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]cysteine-type endopeptidase activity [GO:0004197]; histone binding [GO:0042393]; transcription coactivator activity [GO:0003713]; ubiquitin binding [GO:0043130]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:10077596, ECO:0000269|PubMed:17914355}.P0CW19LIMS3?LIM and senescent cell antigen-like-containing domain protein 3O14686KMT2D%Histone-lysine N-methyltransferase 2D7chromatin organization [GO:0006325]; chromatin silencing [GO:0006342]; histone H3-K4 methylation [GO:0051568]; in utero embryonic development [GO:0001701]; oocyte growth [GO:0001555]; oogenesis [GO:0048477]; positive regulation of cell proliferation [GO:0008284]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; response to estrogen [GO:0043627]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; histone methyltransferase activity (H3-K4 specific) [GO:0042800]; transcription regulatory region DNA binding [GO:0044212]; zinc ion binding [GO:0008270]^histone methyltransferase complex [GO:0035097]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]^FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription. {ECO:0000269|PubMed:16603732, ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17851529}.Q13485SMAD4)Mothers against decapentaplegic homolog 4 R Smads(6)SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation in response to TGF-beta. atrioventricular canal development [GO:0036302]; atrioventricular valve formation [GO:0003190]; axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; brainstem development [GO:0003360]; branching involved in ureteric bud morphogenesis [GO:0001658]; cardiac septum development [GO:0003279]; cell proliferation [GO:0008283]; cellular iron ion homeostasis [GO:0006879]; cellular response to BMP stimulus [GO:0071773]; developmental growth [GO:0048589]; embryonic digit morphogenesis [GO:0042733]; endocardial cell differentiation [GO:0060956]; endoderm development [GO:0007492]; endothelial cell activation [GO:0042118]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; formation of anatomical boundary [GO:0048859]; gastrulation with mouth forming second [GO:0001702]; gene expression [GO:0010467]; intracellular signal transduction [GO:0035556]; in utero embryonic development [GO:0001701]; mesoderm development [GO:0007498]; metanephric mesenchyme morphogenesis [GO:0072133]; negative regulation of cell death [GO:0060548]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nephrogenic mesenchyme morphogenesis [GO:0072134]; neural crest cell differentiation [GO:0014033]; neuron fate commitment [GO:0048663]; palate development [GO:0060021]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of cell proliferation involved in heart valve morphogenesis [GO:0003251]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of SMAD protein import into nucleus [GO:0060391]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus [GO:1901522]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of binding [GO:0051098]; regulation of hair follicle development [GO:0051797]; regulation of transforming growth factor beta2 production [GO:0032909]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to hypoxia [GO:0001666]; response to transforming growth factor beta [GO:0071559]; sebaceous gland development [GO:0048733]; SMAD protein complex assembly [GO:0007183]; SMAD protein signal transduction [GO:0060395]; somatic stem cell maintenance [GO:0035019]; somite rostral/caudal axis specification [GO:0032525]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]chromatin binding [GO:0003682]; core promoter proximal region sequence-specific DNA binding [GO:0000987]; identical protein binding [GO:0042802]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II transcription factor binding transcription factor activity [GO:0001076]; R-SMAD binding [GO:0070412]; transcription regulatory region DNA binding [GO:0044212]; transforming growth factor beta receptor, common-partner cytoplasmic mediator activity [GO:0030616]activin responsive factor complex [GO:0032444]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMAD protein complex [GO:0071141]; transcription factor complex [GO:0005667]hFUNCTION: In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylate< d SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:9389648}.Q16270IBP7,Insulin-like growth factor-binding protein 7zcell adhesion [GO:0007155]; negative regulation of cell proliferation [GO:0008285]; regulation of cell growth [GO:0001558]FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. {ECO:0000269|PubMed:8117260, ECO:0000269|PubMed:8939990}.Q53FA7QORXQuinone oxidoreductase PIG3 Appotosis#NADP metabolic process [GO:0006739]NADPH:quinone reductase activity [GO:0003960]; NADPH binding [GO:0070402]; protein homodimerization activity [GO:0042803]; quinone binding [GO:0048038]; zinc ion binding [GO:0008270]7FUNCTION: May be involved in the generation of reactive oxygen species (ROS). Has low NADPH-dependent beta-naphthoquinone reductase activity, with a preference for 1,2-beta-naphthoquinone over 1,4-beta-naphthoquinone. Has low NADPH-dependent diamine reductase activity (in vitro). {ECO:0000269|PubMed:19349281}.Q9HC35EMAL40Echinoderm microtubule-associated protein-like 4microtubule-based process [GO:0007017]; mitotic nuclear division [GO:0007067]; negative regulation of microtubule depolymerization [GO:0007026]ecytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule [GO:0005874]; mitotic spindle [GO:0072686]FUNCTION: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. {ECO:0000250}.Q7L2E3DHX30)Putative ATP-dependent RNA helicase DHX30SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.; SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm {ECO:0000305}. Mitochondrion matrix, mitochondrion nucleoid.ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; chromatin binding [GO:0003682]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]FUNCTION: Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA. {ECO:0000250, ECO:0000269|PubMed:16825194}.Q13424SNTA1Alpha-1-syntrophinVSUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. {ECO:0000250}.muscle contraction [GO:0006936]; negative regulation of peptidyl-cysteine S-nitrosylation [GO:1902083]; neuromuscular junction development [GO:0007528]; regulation of heart rate [GO:0002027]; regulation of sodium ion transmembrane transport [GO:1902305]; regulation of vasoconstriction by circulating norepinephrine [GO:0003117]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; ventricular cardiac muscle cell action potential [GO:0086005]ATPase binding [GO:0051117]; ion channel binding [GO:0044325]; nitric-oxide synthase binding [GO:0050998]; structural molecule activity [GO:0005198] cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intracellular [GO:0005622]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211]; protein complex [GO:0043234]; sarcolemma [GO:0042383]; syntrophin complex [GO:0016013]FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250}.O43684BUB3Mitotic checkpoint protein BUB3SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition. {ECO:0000250}.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small GTPase mediated signal transduction [GO:0007264]; spindle assembly checkpoint [GO:0071173]wcondensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]FUNCTION: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:18199686}.Q9UBQ6EXTL2Exostosin-like 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Processed exostosin-like 2: Secreted. Note=A soluble form is found in the serum.glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; N-acetylglucosamine metabolic process [GO:0006044]; UDP-N-acetylgalactosamine metabolic process [GO:0019276]alpha-1,4-N-acetylgalactosaminyltransferase activity [GO:0035248]; glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0001888]; metal ion binding [GO:0046872]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. {ECO:0000269|PubMed:10318803}.P98173FAM3A Protein FAM3AGFUNCTION: May act as a defensin against invading fungal microorganisms.Q86VN1VPS36.Vacuolar protein-sorting-associated protein 36!SUBCELLULAR LOCATION: Cytoplasm. Endosome. Late endosome {ECO:0000250|UniProtKB:Q91XD6}. Membrane. Nucleus {ECO:0000305}. Note=Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membran< e to participate in vesicle formation. {ECO:0000250|UniProtKB:Q91XD6}.9endosomal transport [GO:0016197]; membrane organization [GO:0061024]; protein targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]~phosphatidylinositol-3-phosphate binding [GO:0032266]; protein C-terminus binding [GO:0008022]; ubiquitin binding [GO:0043130]cytosol [GO:0005829]; endosome [GO:0005768]; ESCRT II complex [GO:0000814]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; lysosome [GO:0005764]; nucleus [GO:0005634]FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.P20338RAB4ARas-related protein Rab-4ASUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm. Note=Generally associated with membranes. Cytoplasmic when phosphorylated by CDK1.antigen processing and presentation [GO:0019882]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]ATPase activator activity [GO:0001671]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; protein transporter activity [GO:0008565]cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; insulin-responsive compartment [GO:0032593]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; vesicle [GO:0031982]Q9H0S4DDX47)Probable ATP-dependent RNA helicase DDX47SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16963496}. Note=Localizes in the nucleolar-organizing region during ribosome biogenesis.extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; mRNA processing [GO:0006397]; RNA secondary structure unwinding [GO:0010501]; RNA splicing [GO:0008380]; rRNA processing [GO:0006364]FUNCTION: Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors. {ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}.Q9H2D6TARA TRIO and F-actin-binding protein SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9853615}. Note=Localized to F-actin in a periodic pattern.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:22820163}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22820163}. Midbody {ECO:0000269|PubMed:22820163}. Note=Centrosomal localization occurs upon phosphorylation by PLK1 at Thr-457 and lasts from prophase to anaphase. At telophase, relocalizes to midbody.actin modification [GO:0030047]; barbed-end actin filament capping [GO:0051016]; cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]actin filament binding [GO:0051015]; GTP-Rho binding [GO:0017049]; myosin II binding [GO:0045159]; ubiquitin protein ligase binding [GO:0031625]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; nucleus [GO:0005634]FUNCTION: May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover. {ECO:0000269|PubMed:18194665}.Q99873ANM1&Protein arginine N-methyltransferase 1$SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19136629}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). {ECO:0000250}.cell surface receptor signaling pathway [GO:0007166]; chromatin organization [GO:0006325]; histone H4-R3 methylation [GO:0043985]; histone methylation [GO:0016571]; negative regulation of megakaryocyte differentiation [GO:0045653]; neuron projection development [GO:0031175]; peptidyl-arginine methylation [GO:0018216]; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [GO:0019919]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of hemoglobin biosynthetic process [GO:0046985]; positive regulation of p38MAPK cascade [GO:1900745]; protein methylation [GO:0006479]; regulation of transcription, DNA-templated [GO:0006355]histone methyltransferase activity [GO:0042054]; histone methyltransferase activity (H4-R3 specific) [GO:0044020]; identical protein binding [GO:0042802]; methyltransferase activity [GO:0008168]; mitogen-activated protein kinase p38 binding [GO:0048273]; N-methyltransferase activity [GO:0008170]; poly(A) RNA binding [GO:0044822]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:19124016, ECO:0000269|PubMed:19136629, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:20442406}.Q9HC07TM165Transmembrane protein 165SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane. Lysosome membrane. Early endosome membrane. Late endosome membrane.cellular calcium ion homeostasis [GO:0006874]; Golgi calcium ion transport [GO:0032472]; protein N-linked glycosylation [GO:0006487]; regulation of lysosomal lumen pH [GO:0035751]7early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; trans-Golgi network membrane [GO:0032588]FUNCTION: May function as a calcium/proton transporter involved in calcium and in lysosomal pH homeostasis. Therefore, it may play an indirect role in protein glycosylation. {ECO:0000269|PubMed:22683087, ECO:0000269|PubMed:23569283}.P32019I5P22Type II inositol 1,4,5-trisphosphate 5-phosphata< seSUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum-Golgi intermediate compartment. Early endosome membrane. Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}. Golgi apparatus.inositol phosphate metabolic process [GO:0043647]; in utero embryonic development [GO:0001701]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of protein processing [GO:0070613]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; sperm motility [GO:0030317]inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; metal ion binding [GO:0046872]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]?cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. {ECO:0000269|PubMed:7721860}.Q6PKG0LARP1La-related protein 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:24532714}.cell proliferation [GO:0008283]; positive regulation of macroautophagy [GO:0016239]; positive regulation of translation [GO:0045727]; TOR signaling [GO:0031929]; translational initiation [GO:0006413]eukaryotic initiation factor 4E binding [GO:0008190]; mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; poly(A) RNA binding [GO:0044822]; RNA cap binding [GO:0000339]; translation activator activity [GO:0008494]; translation initiation factor binding [GO:0031369]FUNCTION: RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5'cap in an MTOR-dependent manner and associates with mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5'TOP, thereby regulating cell growth and proliferation. {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370, ECO:0000269|PubMed:24532714}.Q969S3ZN622Zinc finger protein 622eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11802789}. Nucleus {ECO:0000269|PubMed:11802789}.!intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JNK cascade [GO:0046330]; positive regulation of kinase activity [GO:0033674]; positive regulation of MAPK cascade [GO:0043410]Lcytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]xFUNCTION: May behave as an activator of the bound transcription factor, MYBL2, and be involved in embryonic development.Q13535ATR#Serine/threonine-protein kinase ATRSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11721054, ECO:0000269|PubMed:11865061, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:14871897, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:18283122, ECO:0000269|PubMed:8843195}. Nucleus, PML body {ECO:0000250}. Chromosome {ECO:0000250}. Note=Depending on the cell type, it can also be found in PML nuclear bodies. Recruited to chromatin during S-phase. Redistributes to discrete nuclear foci upon DNA damage, hypoxia or replication fork stalling.:cell cycle [GO:0007049]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to gamma radiation [GO:0071480]; cellular response to heat [GO:0034605]; cellular response to UV [GO:0034644]; DNA damage checkpoint [GO:0000077]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; multicellular organismal development [GO:0007275]; negative regulation of DNA replication [GO:0008156]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; protein autophosphorylation [GO:0046777]; regulation of cellular response to heat [GO:1900034]; regulation of protein binding [GO:0043393]; replicative senescence [GO:0090399]; response to drug [GO:0042493] ATP binding [GO:0005524]; DNA binding [GO:0003677]; MutLalpha complex binding [GO:0032405]; MutSalpha complex binding [GO:0032407]; protein dimerization activity [GO:0046983]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]|chromosome [GO:0005694]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; PML body [GO:0016605]; XY body [GO:0001741]OFUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication. {ECO:0000269|PubMed:10597277, ECO:0000269|PubMed:10608806, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11418864, ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:11721054, ECO:0000269|PubMed:11865061, ECO:0000269|PubMed:12526805, ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14729973, ECO:0000269|PubMed:14742437, ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15314022, ECO:0000269|PubMed:15496423, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:9427750, ECO:0000269|PubMed:9636169, ECO:0000269|PubMed:9925639}.Q96JJ7TMX3 Protein disulfide-isomerase TMX3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15623505}; Single-pass membrane protein {ECO:0000269|PubMed:15623505}.scell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]FUNCTION: Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. {ECO:0000269|PubMed:15623505}.Q13435SF3B2Splicing factor 3B subunit 2gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; viral process [GO:0016032]catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]Q969S9RRF2M*Ribosome-releasing factor 2, mitochondrialFSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}.mitochondrial translation [GO:0032543]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; ribosome disassembly [GO:0032790]FUNCTION: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. {ECO:0000255|HAMAP-Rule:MF_03059, ECO:0000269|PubMed:19716793}.Q5VY43PEAR1+Platelet endothelial aggregation receptor 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-< pass membrane protein {ECO:0000305}. Note=Detected on the cell surface in resting platelets. {ECO:0000269|PubMed:15851471}.*recognition of apoptotic cell [GO:0043654]Hintegral component of membrane [GO:0016021]; phagocytic cup [GO:0001891]}FUNCTION: When overexpressed, reduces the number of both early and late non-adherent myeloid progenitor cells. {ECO:0000250}.P08047SP1Transcription factor Sp1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.6definitive hemopoiesis [GO:0060216]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; embryonic skeletal system development [GO:0048706]; enucleate erythrocyte differentiation [GO:0043353]; gene expression [GO:0010467]; liver development [GO:0001889]; lung development [GO:0030324]; megakaryocyte differentiation [GO:0030219]; ossification [GO:0001503]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; rhythmic process [GO:0048511]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; trophectodermal cell differentiation [GO:0001829]; viral process [GO:0016032]bHLH transcription factor binding [GO:0043425]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; enhancer binding [GO:0035326]; histone deacetylase binding [GO:0042826]; HMG box domain binding [GO:0071837]; metal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II repressing transcription factor binding [GO:0001103]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1. {ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466, ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531, ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743, ECO:0000269|PubMed:21798247}.Q8N1B4VPS526Vacuolar protein sorting-associated protein 52 homologectodermal cell differentiation [GO:0010668]; embryonic ectodermal digestive tract development [GO:0048611]; endocytic recycling [GO:0032456]; protein transport [GO:0015031]EARP complex [GO:1990745]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]Q9BY44EIF2A+Eukaryotic translation initiation factor 2Apositive regulation of signal transduction [GO:0009967]; protein phosphorylation [GO:0006468]; regulation of translation [GO:0006417]; ribosome assembly [GO:0042255]; SREBP signaling pathway [GO:0032933]mribosome binding [GO:0043022]; translation initiation factor activity [GO:0003743]; tRNA binding [GO:0000049]blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; eukaryotic translation initiation factor 2 complex [GO:0005850]; extracellular space [GO:0005615]FUNCTION: Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40 S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40 S subunits in a GTP-dependent manner. May act by impiging the expression of specific proteins. {ECO:0000269|PubMed:12133843}.Q4VC31CCD58(Coiled-coil domain-containing protein 58O95376ARI2!E3 ubiquitin-protein ligase ARIH2developmental cell growth [GO:0048588]; hematopoietic stem cell proliferation [GO:0071425]; multicellular organismal development [GO:0007275]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]ligase activity [GO:0016874]; nucleic acid binding [GO:0003676]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys-63'-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis. {ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006}.P15531NDKANucleoside diphosphate kinase ASUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}. Note=Cell-cycle dependent nuclear localization which can be induced by interaction with Epstein-barr viral proteins or by degradation of the SET complex by GzmA.1cell differentiation [GO:0030154]; CTP biosynthetic process [GO:0006241]; DNA metabolic process [GO:0006259]; endocytosis [GO:0006897]; GTP biosynthetic process [GO:0006183]; negative regulation of cell proliferation [GO:0008285]; nervous system development [GO:0007399]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside triphosphate biosynthetic process [GO:0009142]; positive regulation of DNA binding [GO:0043388]; positive regulation of epithelial cell proliferation [GO:0050679]; purine nucleotide metabolic process [GO:0006163]; pyrimidine nucleotide metabolic process [GO:0006220]; regulation of apoptotic process [GO:0042981]; small molecule metabolic process [GO:0044281]; UTP biosynthetic process [GO:0006228],ATP binding [GO:0005524]; deoxyribonuclease activity [GO:0004536]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; magnesium ion binding< [GO:0000287]; nucleoside diphosphate kinase activity [GO:0004550]; poly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}.P54105ICLNMethylosome subunit pIClnSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:18984161}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18984161}. Note=A small fraction is also associated with the cytoskeleton.cell volume homeostasis [GO:0006884]; chloride transport [GO:0006821]; gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; spliceosomal snRNP assembly [GO:0000387]Rpoly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; plasma membrane [GO:0005886]FUNCTION: Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also indirectly participate in cellular volume control by activation of a swelling-induced chloride conductance pathway. {ECO:0000269|PubMed:10330151, ECO:0000269|PubMed:11713266, ECO:0000269|PubMed:18984161}.Q9UP95S12A4!Solute carrier family 12 member 4dcell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; ion transport [GO:0006811]; potassium ion homeostasis [GO:0055075]; potassium ion import [GO:0010107]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; transport [GO:0006810]potassium:chloride symporter activity [GO:0015379]; potassium ion symporter activity [GO:0022820]; protein kinase binding [GO:0019901]integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]9FUNCTION: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). Isoform 4 has no transport activity. {ECO:0000250}.Q9H6E5STPAP5Speckle targeted PIP5K1A-regulated poly(A) polymerase:SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus speckle.}mRNA polyadenylation [GO:0006378]; pre-mRNA cleavage required for polyadenylation [GO:0098789]; snRNA processing [GO:0016180]ATP binding [GO:0005524]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; polynucleotide adenylyltransferase activity [GO:0004652]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265]ointercellular bridge [GO:0045171]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation. {ECO:0000269|PubMed:16790842, ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:21102410}.P32189GLPKGlycerol kinaseSUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note=In sperm and fetal tissues, the majority of the enzyme is bound to mitochondria, but in adult tissues, such as liver found in the cytoplasm.cellular lipid metabolic process [GO:0044255]; glucose homeostasis [GO:0042593]; glycerol-3-phosphate biosynthetic process [GO:0046167]; glycerol catabolic process [GO:0019563]; glycerol metabolic process [GO:0006071]; phosphorylation [GO:0016310]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; triglyceride metabolic process [GO:0006641]?ATP binding [GO:0005524]; glycerol kinase activity [GO:0004370]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]IFUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism.P37059DHB2!Estradiol 17-beta-dehydrogenase 2in utero embryonic development [GO:0001701]; placenta development [GO:0001890]; response to retinoic acid [GO:0032526]; steroid biosynthetic process [GO:0006694]17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity [GO:0047006]; estradiol 17-beta-dehydrogenase activity [GO:0004303]; testosterone dehydrogenase (NAD+) activity [GO:0047035]FUNCTION: Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH.P98161PKD1 Polycystin-1SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20980620}; Multi-pass membrane protein {ECO:0000269|PubMed:20980620}. Cell projection, cilium {ECO:0000250|UniProtKB:O08852}. Note=PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autoproteolytic cleavage at the GPS domain (By similarity). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (By similarity). {ECO:0000250|UniProtKB:O08852}.anatomical structure morphogenesis [GO:0009653]; branching morphogenesis of an epithelial tube [GO:0048754]; calcium-independent cell-matrix adhesion [GO:0007161]; calcium ion transmembrane transport [GO:0070588]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell cycle arrest [GO:0007050]; cell-matrix adhesion [GO:0007160]; cytoplasmic seque< stering of transcription factor [GO:0042994]; detection of mechanical stimulus [GO:0050982]; digestive tract development [GO:0048565]; embryonic placenta development [GO:0001892]; establishment of cell polarity [GO:0030010]; genitalia development [GO:0048806]; heart development [GO:0007507]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; in utero embryonic development [GO:0001701]; JAK-STAT cascade [GO:0007259]; kidney development [GO:0001822]; liver development [GO:0001889]; lung epithelium development [GO:0060428]; lymph vessel morphogenesis [GO:0036303]; mesonephric duct development [GO:0072177]; mesonephric tubule development [GO:0072164]; metanephric ascending thin limb development [GO:0072218]; metanephric collecting duct development [GO:0072205]; metanephric distal tubule morphogenesis [GO:0072287]; metanephric proximal tubule development [GO:0072237]; neural tube development [GO:0021915]; nitrogen compound metabolic process [GO:0006807]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; placenta blood vessel development [GO:0060674]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of protein binding [GO:0032092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein export from nucleus [GO:0006611]; regulation of cell adhesion [GO:0030155]; regulation of mitotic spindle organization [GO:0060236]; regulation of proteasomal protein catabolic process [GO:0061136]; response to fluid shear stress [GO:0034405]; single organismal cell-cell adhesion [GO:0016337]; skin development [GO:0043588]; spinal cord development [GO:0021510]calcium channel activity [GO:0005262]; carbohydrate binding [GO:0030246]; ion channel binding [GO:0044325]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]3basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi-associated vesicle membrane [GO:0030660]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lateral plasma membrane [GO:0016328]; motile primary cilium [GO:0031512]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; polycystin complex [GO:0002133]; primary cilium [GO:0072372]FUNCTION: Involved in renal tubulogenesis (PubMed:12482949). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). Acts as a regulator of cilium length, together with PKD2 (By similarity). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling (By similarity). The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (By similarity). May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. {ECO:0000250|UniProtKB:O08852, ECO:0000269|PubMed:12482949}.O00754MA2B1Lysosomal alpha-mannosidasecellular protein modification process [GO:0006464]; mannose metabolic process [GO:0006013]; protein deglycosylation [GO:0006517]Yextracellular exosome [GO:0070062]; lysosome [GO:0005764]; vacuolar membrane [GO:0005774]FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.Q9UBN6TR10D5Tumor necrosis factor receptor superfamily member 10Dwapoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; signal transduction [GO:0007165]6transmembrane signaling receptor activity [GO:0004888]xFUNCTION: Receptor for the cytotoxic ligand TRAIL. Contains a truncated death domain and hence is not capable of inducing apoptosis but protects against TRAIL-mediated apoptosis. Reports are contradictory with regards to its ability to induce the NF-kappa-B pathway. According to PubMed:9382840, it cannot but according to PubMed:9430226, it can induce the NF-kappa-B pathway.A8MW92P20L1$PHD finger protein 20-like protein 1Q9ULF5S39AAZinc transporter ZIP10NFUNCTION: May act as a zinc-influx transporter. {ECO:0000269|PubMed:17359283}.P57077M3KCLMAP3K7 C-terminal-like proteinQ9BUE6ISCA15Iron-sulfur cluster assembly 1 homolog, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15262227, ECO:0000269|PubMed:22323289}.)iron-sulfur cluster assembly [GO:0016226]siron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; structural molecule activity [GO:0005198] FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000269|PubMed:15262227, ECO:0000269|PubMed:22323289}.Q9BX74TM2D1TM2 domain-containing protein 1xSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11278849}; Multi-pass membrane protein {ECO:0000269|PubMed:11278849}.capoptotic signaling pathway [GO:0097190]; G-protein coupled receptor signaling pathway [GO:0007186]Sbeta-amyloid binding [GO:0001540]; G-protein coupled receptor activity [GO:0004930]Lintegral component of plasma membrane [GO:0005887]; nucleoplasm [GO:0005654]FUNCTION: May participate in beta-amyloid-induced apoptosis via its interaction with beta-APP42. {ECO:0000269|PubMed:11278849, ECO:0000269|PubMed:12836168}.Q9NQT8KI13BKinesin-like protein KIF13BSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20194617}. Cell projection, axon {ECO:0000269|PubMed:20194617}. Note=accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites.microtubule-based movement [GO:0007018]; protein targeting [GO:0006605]; regulation of axonogenesis [GO:0050770]; signal transduction [GO:0007165]; T cell activation [GO:0042110]14-3-3 protein binding [GO:0071889]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule motor activity [GO:0003777]; protein kinase binding [GO:0019901]aaxon [GO:0030424]; cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874]FUNCTION: Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes. {ECO:0000269|PubMed:20194617}.Q13342SP140Nuclear body protein SP140SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Nucleus, PML body {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Cytoplasm {ECO:0000269|PubMed:8695863}. Note=Localized to nuclear structures termed LANDS, for LYSp100-associated nuclear domains. LANDS are globular, electron-dense structures most often found in the nucleoplasm, but also found at the nuclear membrane and in the cytoplasm, suggesting that these structures may traffic between the cytoplasm and the nucleus (PubMed:8695863). Also colocalizes with PML in a subset of PML nuclear bodies (PubMed:8910577). {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}.ychromatin remodeling [GO:0006338]; defense response [GO:0006952]; regulation of transcription, DNA-templated [GO:0006355]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]|cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Component of the nuclear body, also known as nuclear domain 10, PML oncogenic domain, and KR body (PubMed:8910577). May be involved in the pathogenesis of acute promyelocytic leukemia and viral i< nfection (PubMed:8910577). May play a role in chromatin-mediated regulation of gene expression although it does not bind to histone H3 tails (PubMed:24267382). {ECO:0000269|PubMed:24267382, ECO:0000269|PubMed:8910577, ECO:0000303|PubMed:8910577}.P01111RASN GTPase NRasESUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15705808}; Lipid-anchor {ECO:0000269|PubMed:15705808}; Cytoplasmic side {ECO:0000269|PubMed:15705808}. Golgi apparatus membrane {ECO:0000269|PubMed:15705808}; Lipid-anchor {ECO:0000269|PubMed:15705808}. Note=Shuttles between the plasma membrane and the Golgi apparatus.cactivation of MAPKK activity [GO:0000186]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; epidermal growth factor receptor signaling pathway [GO:0007173]; establishment of protein localization to Golgi [GO:0072600]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; leukocyte migration [GO:0050900]; MAPK cascade [GO:0000165]; negative regulation of skeletal muscle tissue development [GO:0048642]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Ras protein signal transduction [GO:0007265]; small GTPase mediated signal transduction [GO:0007264]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]>GTP binding [GO:0005525]; protein complex binding [GO:0032403]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]JFUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.P04899GNAI27Guanine nucleotide-binding protein G(i) subunit alpha-2DSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.activation of MAPKK activity [GO:0000186]; adenosine receptor signaling pathway [GO:0001973]; adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; blood coagulation [GO:0007596]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell proliferation [GO:0008283]; gamma-aminobutyric acid signaling pathway [GO:0007214]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; G-protein coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; negative regulation of adenylate cyclase activity [GO:0007194]; negative regulation of synaptic transmission [GO:0050805]; platelet activation [GO:0030168]; positive regulation of cell proliferation [GO:0008284]; regulation of calcium ion transport [GO:0051924]; response to nutrient [GO:0007584]; signal transduction [GO:0007165]; synaptic transmission [GO:0007268]G-protein beta/gamma-subunit complex binding [GO:0031683]; G-protein coupled receptor binding [GO:0001664]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]=centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; membrane raft [GO:0045121]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division.; FUNCTION: Isoform sGi2: Regulates the cell surface density of dopamine receptors DRD2 by sequestrating them as an intracellular pool.P31942HNRH3*Heterogeneous nuclear ribonucleoprotein H3;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8999868}.epithelial cell differentiation [GO:0030855]; mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]Qnucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.Q2M389WASH7WASH complex subunit 7CSUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23676666}.dendosomal transport [GO:0016197]; endosome organization [GO:0007032]; protein transport [GO:0015031]gearly endosome [GO:0005769]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; WASH complex [GO:0071203]FUNCTION: Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes sems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in the regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093). {ECO:0000250|UniProtKB:Q3UMB9, ECO:0000303|PubMed:21498477, ECO:0000305|PubMed:19922875, ECO:0000305|PubMed:20498093}.P05166PCCB3Propionyl-CoA carboxylase beta chain, mitochondrial@biotin metabolic process [GO:0006768]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; short-chain fatty acid catabolic process [GO:0019626]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]IATP binding [GO:0005524]; propionyl-CoA carboxylase activity [GO:0004658]Q96IJ6GMPPA+Mannose-1-phosphate guanyltransferase alphaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24035193}. Note=Myc-tagged GMPPA shows a diffuse cytoplasmic and nuclear pattern in transfected COS-7 cells.,nucleotidyltransferase activity [GO:0016779]FUNCTION: May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. {ECO:0000269|PubMed:24035193}.O96008TOM403Mitochondrial import receptor subunit TOM40 homologSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15644312}; Multi-pass membrane protein {ECO:0000269|PubMed:15644312}.cellular protein metabolic process [GO:0044267]; ion transport [GO:0006811]; protein targeting to mitochondrion [GO:0006626]; protein transmembrane transport [GO:0071806]Tporin activity [GO:0015288]; protein transmembrane transporter activity [GO:0008320]8cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of mitochondrial outer membrane [GO:0031307]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; pore complex [GO:0046930]nFUNCTION: Channel-forming protein essential for import of protein precursors into mitochondria. {ECO:0000250}.P33527MRP1)Multidrug resistance-associated protein 1 Vitamin digestion and absorptionSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16230346}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16230346}.oarachidonic acid metabolic process [GO:0019369]; cobalamin metabolic process [GO:0009235]; leukotriene metabolic process [GO:0006691]; response to drug [GO:0042493]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; transport [GO:0006810]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATPase activity [GO:0016887]; ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; transporter activity [GO:0005215]basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; integral component< of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. {ECO:0000269|PubMed:10064732, ECO:0000269|PubMed:11114332, ECO:0000269|PubMed:16230346}.Q9H9L4KANL2%KAT8 regulatory NSL complex subunit 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20018852}.chromatin organization [GO:0006325]; histone H4-K16 acetylation [GO:0043984]; histone H4-K5 acetylation [GO:0043981]; histone H4-K8 acetylation [GO:0043982]bhistone acetyltransferase complex [GO:0000123]; NSL complex [GO:0044545]; nucleoplasm [GO:0005654]FUNCTION: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000269|PubMed:20018852}.P80404GABT/4-aminobutyrate aminotransferase, mitochondrialbehavioral response to cocaine [GO:0048148]; copulation [GO:0007620]; gamma-aminobutyric acid biosynthetic process [GO:0009449]; gamma-aminobutyric acid catabolic process [GO:0009450]; locomotory behavior [GO:0007626]; negative regulation of blood pressure [GO:0045776]; neurotransmitter catabolic process [GO:0042135]; neurotransmitter secretion [GO:0007269]; positive regulation of heat generation [GO:0031652]; positive regulation of insulin secretion [GO:0032024]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666]; response to iron ion [GO:0010039]; response to nicotine [GO:0035094]; synaptic transmission [GO:0007268]T(S)-3-amino-2-methylpropionate transaminase activity [GO:0047298]; 4-aminobutyrate transaminase activity [GO:0003867]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; succinate-semialdehyde dehydrogenase binding [GO:0032145]4-aminobutyrate transaminase complex [GO:0032144]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.Q01995TAGL TransgelinSepithelial cell differentiation [GO:0030855]; muscle organ development [GO:0007517]FUNCTION: Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence. {ECO:0000250}.Q7Z739YTHD3&YTH domain-containing family protein 3XN6-methyladenosine-containing RNA binding [GO:1990247]; poly(A) RNA binding [GO:0044822]2FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. {ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625}.P11498PYC#Pyruvate carboxylase, mitochondrialWbiotin metabolic process [GO:0006768]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; lipid metabolic process [GO:0006629]; negative regulation of gene expression [GO:0010629]; positive regulation by host of viral process [GO:0044794]; positive regulation by host of viral release from host cell [GO:0044791]; pyruvate metabolic process [GO:0006090]; small molecule metabolic process [GO:0044281]; viral RNA genome packaging [GO:0019074]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin carboxylase activity [GO:0004075]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; pyruvate carboxylase activity [GO:0004736]uFUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.Q9H4L4SENP3Sentrin-specific protease 3@SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress. {ECO:0000250}."protein desumoylation [GO:0016926]Qendopeptidase activity [GO:0004175]; SUMO-specific protease activity [GO:0016929]_cytoplasm [GO:0005737]; MLL1 complex [GO:0071339]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085, ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224, ECO:0000269|PubMed:22872859}.Q9H7C4SYNCI SyncoilinNSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EPM5}. Note=In skeletal muscle, colocalizes with DES and DTNA, and is localized at the myotendinous and neuromuscular junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate cytoplasmic pattern (By similarity). {ECO:0000250|UniProtKB:Q9EPM5}.0intermediate filament-based process [GO:0045103]cytosol [GO:0005829]; intermediate filament [GO:0005882]; neuromuscular junction [GO:0031594]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]; Z disc [GO:0030018]mFUNCTION: Atypical type III intermediate filament (IF) protein that may play a supportive role in the efficient coupling of mechanical stress between the myofibril and fiber exterior. May facilitate lateral force transmission during skeletal muscle contraction. Does not form homofilaments nor heterofilaments with other IF proteins. {ECO:0000250|UniProtKB:Q9EPM5}.Q14149MORC3)MORC family CW-type zinc finger protein 3/cell aging [GO:0007569]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of fibroblast proliferation [GO:0048147]; peptidyl-serine phosphorylation [GO:0018105]; post-embryonic development [GO:0009791]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]`intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; PML body [GO:0016605]P10809CH60(60 kDa heat shock protein, mitochondrialde novo' protein folding [GO:0006458]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; B cell activation [GO:0042113]; B cell cytokine production [GO:0002368]; B cell proliferation [GO:0042100]; chaperone-mediated protein complex assembly [GO:0051131]; chaperone mediated protein folding requiring cofactor [GO:0051085]; detection of misfolded protein [GO:0002236]; isotype switching to IgG isotypes [GO:0048291]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; ne< gative regulation of apoptotic process [GO:0043066]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of apoptotic process [GO:0043065]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage activation [GO:0043032]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell mediated immune response to tumor cell [GO:0002842]; protein maturation [GO:0051604]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to ATP [GO:0033198]; response to cocaine [GO:0042220]; response to cold [GO:0009409]; response to drug [GO:0042493]; response to estrogen [GO:0043627]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; response to unfolded protein [GO:0006986]; T cell activation [GO:0042110]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; chaperone binding [GO:0051087]; DNA replication origin binding [GO:0003688]; double-stranded RNA binding [GO:0003725]; lipopolysaccharide binding [GO:0001530]; p53 binding [GO:0002039]; poly(A) RNA binding [GO:0044822]; single-stranded DNA binding [GO:0003697]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]cell surface [GO:0009986]; coated pit [GO:0005905]; coated vesicle [GO:0030135]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lipopolysaccharide receptor complex [GO:0046696]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; rough endoplasmic reticulum [GO:0005791]; secretory granule [GO:0030141]; zymogen granule [GO:0042588],FUNCTION: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.P54289CA2D19Voltage-dependent calcium channel subunit alpha-2/delta-1 Receptor/CACNcalcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; regulation of calcium ion transport [GO:0051924]calcium channel regulator activity [GO:0005246]; metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245]extracellular exosome [GO:0070062]; sarcoplasmic reticulum [GO:0016529]; T-tubule [GO:0030315]; voltage-gated calcium channel complex [GO:0005891]FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250}.Q13042CDC16&Cell division cycle protein 16 homologSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:7736578}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:7736578}. Note=Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell division [GO:0051301]; cell proliferation [GO:0008283]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K11-linked ubiquitination [GO:0070979]; regulation of mitotic nuclear division [GO:0007088]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; spindle [GO:0005819]P41091IF2G4Eukaryotic translation initiation factor 2 subunit 3cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; translation [GO:0006412]; translational initiation [GO:0006413]; transmembrane transport [GO:0055085]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]Q8WW59SPRY4 SPRY domain-containing protein 4effectorP11309PIM1%Serine/threonine-protein kinase pim-1eSUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 1: Cell membrane.apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell proliferation [GO:0008283]; hyaluronan metabolic process [GO:0030212]; multicellular organismal development [GO:0007275]; negative regulation of apoptotic process [GO:0043066]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of mitotic cell cycle [GO:0007346]; vitamin D receptor signaling pathway [GO:0070561]ATP binding [GO:0005524]; manganese ion binding [GO:0030145]; protein serine/threonine kinase activity [GO:0004674]; ribosomal small subunit binding [GO:0043024]; transcription factor binding [GO:0008134]FUNCTION: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis. {ECO:0000269|PubMed:10664448, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:1825810, ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19749799}.P46939UTROUtrophinSUBCELLULAR L< OCATION: Cell junction, synapse, postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Neuromuscular junction.muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; positive regulation of cell-matrix adhesion [GO:0001954]; regulation of sodium ion transmembrane transporter activity [GO:2000649]actin binding [GO:0003779]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein complex [GO:0043234]; sarcolemma [GO:0042383]^FUNCTION: May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}.Q9Y4C2F115AProtein FAM115ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25559186}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000269|PubMed:25559186}.negative regulation of cell migration [GO:0030336]; positive regulation of anion channel activity [GO:1901529]; positive regulation of protein targeting to membrane [GO:0090314]; transport [GO:0006810]plasma membrane [GO:0005886]FUNCTION: Positively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration inhibition in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}.P50895BCAMBasal cell adhesion molecule_cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; signal transduction [GO:0007165]laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; protein C-terminus binding [GO:0008022]; transmembrane signaling receptor activity [GO:0004888]external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]fFUNCTION: Laminin alpha-5 receptor. May mediate intracellular signaling. {ECO:0000269|PubMed:9616226}.P52943CRIP2Cysteine-rich protein 2Phemopoiesis [GO:0030097]; positive regulation of cell proliferation [GO:0008284]cell cortex [GO:0005938]Q96F10SAT2Diamine acetyltransferase 2 Amine and polyamine degradation?SUBCELLULAR LOCATION: Cytoplasm. Note=Intracellular organelles.nor-spermidine metabolic process [GO:0046204]; putrescine acetylation [GO:0032920]; putrescine catabolic process [GO:0009447]; spermidine acetylation [GO:0032918]; spermine acetylation [GO:0032919]1diamine N-acetyltransferase activity [GO:0004145]FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine.Q9GZT4SRRSerine racemaseaging [GO:0007568]; brain development [GO:0007420]; D-serine biosynthetic process [GO:0070179]; D-serine metabolic process [GO:0070178]; L-serine metabolic process [GO:0006563]; protein homotetramerization [GO:0051289]; pyruvate biosynthetic process [GO:0042866]; response to drug [GO:0042493]; response to lipopolysaccharide [GO:0032496]; response to morphine [GO:0043278]; serine family amino acid metabolic process [GO:0009069]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; D-serine ammonia-lyase activity [GO:0008721]; glycine binding [GO:0016594]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threonine racemase activity [GO:0018114]wapical part of cell [GO:0045177]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. {ECO:0000269|PubMed:11054547, ECO:0000269|PubMed:20106978}.Q08379GOGA2Golgin subfamily A member 2YSUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.mitotic cell cycle [GO:0000278]; negative regulation of autophagy [GO:0010507]; negative regulation of protein binding [GO:0032091]; positive regulation of protein glycosylation [GO:0060050]Bprotein kinase binding [GO:0019901]; syntaxin binding [GO:0019905]cis-Golgi network [GO:0005801]; ER to Golgi transport vesicle [GO:0030134]; Golgi apparatus [GO:0005794]; Golgi cis cisterna [GO:0000137]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]SFUNCTION: Golgi auto-antigen; probably involved in maintaining cis-Golgi structure.Q9UKM7MA1B1DEndoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10409699}; Single-pass type II membrane protein {ECO:0000269|PubMed:10409699}.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum mannose trimming [GO:1904380]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; glycoprotein ERAD pathway [GO:0097466]; mannose trimming involved in glycoprotein ERAD pathway [GO:1904382]; N-glycan processing [GO:0006491]; oligosaccharide metabolic process [GO:0009311]; post-translational protein modification [GO:0043687]; protein alpha-1,2-demannosylation [GO:0036508]; protein folding [GO:0006457]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; trimming of terminal mannose on B branch [GO:0036509]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2). {ECO:0000269|PubMed:12090241, ECO:0000269|PubMed:18003979}.Q6GMV2SMYD5(SET and MYND domain-containing protein 5Gmetal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]P22830HEMHFerrochelatase, mitochondrialcellular response to dexamethasone stimulus [GO:0071549]; cholesterol metabolic process [GO:0008203]; detection of UV [GO:0009589]; erythrocyte differentiation [GO:0030218]; generation of precursor metabolites and energy [GO:0006091]; heme biosynthetic process [GO:0006783]; iron ion homeostasis [GO:0055072]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX metabolic process [GO:0046501]; regulation of eIF2 alpha phosphorylation by heme [GO:0010999]; regulation of gene expression [GO:0010468]; regulation of hemoglobin biosynthetic process [GO:0046984]; response to arsenic-containing substance [GO:0046685]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to insecticide [GO:0017085]; response to lead ion [GO:0010288]; response to light stimulus [GO:0009416]; response to methylmercury [GO:0051597]; response to platinum ion [GO:0070541]; small molecule metabolic process [GO:0044281]; very-low-density lipoprotein particle assembly [GO:0034379]2 iron, 2 sulfur cluster binding [GO:0051537]; ferrochelatase activity [GO:0004325]; ferrous iron binding [GO:0008198]; heme binding [GO:0020037]; iron-responsive element binding [GO:0030350]AFUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.P50995ANX11 Annexin A11SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus envelope. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindl< e. Note=Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus (By similarity). Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. {ECO:0000250}.tcell cycle [GO:0007049]; cell division [GO:0051301]; phagocytosis [GO:0006909]; response to calcium ion [GO:0051592],calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; MHC class II protein complex binding [GO:0023026]; phosphatidylethanolamine binding [GO:0008429]; poly(A) RNA binding [GO:0044822]; S100 protein binding [GO:0044548]/azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; phagocytic vesicle [GO:0045335]; specific granule [GO:0042581]; spindle [GO:0005819]FUNCTION: Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis. {ECO:0000250, ECO:0000269|PubMed:15197175}.Q8NBX0SCPDL.Saccharopine dehydrogenase-like oxidoreductasezlipid particle [GO:0005811]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; nucleus [GO:0005634]Q96EY7PTCD3CPentatricopeptide repeat domain-containing protein 3, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19427859, ECO:0000269|PubMed:23908630}.mitochondrial translation [GO:0032543]; mitochondrial translational elongation [GO:0070125]; mitochondrial translational initiation [GO:0070124]; mitochondrial translational termination [GO:0070126]; organelle organization [GO:0006996]; regulation of translation [GO:0006417]ipoly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]; rRNA binding [GO:0019843]xFUNCTION: Mitochondrial RNA-binding protein that has a role in mitochondrial translation. {ECO:0000269|PubMed:19427859}.Q9UPY5XCTCystine/glutamate transporterxSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15151999}; Multi-pass membrane protein {ECO:0000269|PubMed:15151999}.amino acid transport [GO:0006865]; blood coagulation [GO:0007596]; brain development [GO:0007420]; ion transport [GO:0006811]; lens fiber cell differentiation [GO:0070306]; leukocyte migration [GO:0050900]; L-glutamate transmembrane transport [GO:0089711]; platelet aggregation [GO:0070527]; response to nicotine [GO:0035094]; response to oxidative stress [GO:0006979]; response to toxic substance [GO:0009636]; transmembrane transport [GO:0055085]2cystine:glutamate antiporter activity [GO:0015327]cell surface [GO:0009986]; cytoskeleton [GO:0005856]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate. {ECO:0000269|PubMed:15151999}.Q9NQC3RTN4 Reticulon-4SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains.apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; axonogenesis [GO:0007409]; cardiac epithelial to mesenchymal transition [GO:0060317]; cerebral cortex radial glia guided migration [GO:0021801]; endoplasmic reticulum tubular network organization [GO:0071786]; negative regulation of axon extension [GO:0030517]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell growth [GO:0030308]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of apoptotic process [GO:0042981]; regulation of axonogenesis [GO:0050770]; regulation of branching morphogenesis of a nerve [GO:2000172]; regulation of cell migration [GO:0030334]0endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; integral component of endoplasmic reticulum membrane [GO:0030176]; intracellular [GO:0005622]; neuronal postsynaptic density [GO:0097481]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]FUNCTION: Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing. {ECO:0000250, ECO:0000269|PubMed:10667797, ECO:0000269|PubMed:11201742, ECO:0000269|PubMed:16965550}.Q7Z4R8CF120UPF0669 protein C6orf120[SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22340178}. Note=Secreted by hepatocytes.FUNCTION: May be involved in induction of apoptosis in CD4(+) T-cells, but not CD8(+) T-cells or hepatocytes. {ECO:0000269|PubMed:22340178}.Q7Z6K5ARPINArpinSUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with the WAVE complex at lamelliupodium tip. {ECO:0000250}.directional locomotion [GO:0033058]; negative regulation of actin nucleation [GO:0051126]; negative regulation of cell migration [GO:0030336]; negative regulation of lamellipodium morphogenesis [GO:2000393]lamellipodium [GO:0030027]FUNCTION: Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence. {ECO:0000269|PubMed:24132237}.Q96QK1VPS35.Vacuolar protein sorting-associated protein 35SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome {ECO:0000269|PubMed:15078903}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}. Note=Localizes to tubular profiles adjacent to endosomes. {ECO:0000269|PubMed:15078903}.intracellular protein transport [GO:0006886]; negative regulation of late endosome to lysosome transport [GO:1902823]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde transport, endosome to plasma membrane [GO:1990126]; transcytosis [GO:0045056]cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; neuronal postsynaptic density [GO:0097481]; retromer complex [GO:0030904]; tubular endosome [GO:0097422]FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plas< ma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for endosomal localization of FAM21C (PubMed:22070227). Mediates the association of the CSC with the WASH complex via FAM21 (PubMed:22070227, PubMed:24980502, PubMed:24819384). Required for the endosomal localization of TBC1D5 (PubMed:20923837). {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:20164305, ECO:0000269|PubMed:20923837, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:22070227, ECO:0000303|PubMed:22513087, ECO:0000303|PubMed:23563491}.P50542PEX5'Peroxisomal targeting signal 1 receptorSUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Peripheral membrane protein. Note=Its distribution appears to be dynamic. It is probably a cycling receptor found mainly in the cytoplasm and as well associated to the peroxisomal membrane through a docking factor (PEX13).}negative regulation of protein homotetramerization [GO:1901094]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, translocation [GO:0016561]; protein import into peroxisome membrane [GO:0045046]; protein targeting to peroxisome [GO:0006625]; protein tetramerization [GO:0051262]enzyme binding [GO:0019899]; peroxisome matrix targeting signal-1 binding [GO:0005052]; peroxisome targeting sequence binding [GO:0000268]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]; small GTPase binding [GO:0031267]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; membrane [GO:0016020]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein complex [GO:0043234]FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. {ECO:0000269|PubMed:7706321, ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}.Q9GZT8GTPC1+Putative GTP cyclohydrolase 1 type 2 NIF3L1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11124544, ECO:0000269|PubMed:12951069}. Nucleus {ECO:0000250|UniProtKB:Q9EQ80}. Note=Interaction with COPS2 may regulate localization to the nucleus. {ECO:0000250|UniProtKB:Q9EQ80}.negative regulation of nucleic acid-templated transcription [GO:1903507]; neuron differentiation [GO:0030182]; positive regulation of transcription, DNA-templated [GO:0045893]Qidentical protein binding [GO:0042802]; transcription factor binding [GO:0008134]FUNCTION: May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation. {ECO:0000250|UniProtKB:Q9EQ80}.P82094TMF1TATA element modulatory factorSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Golgi apparatus membrane. Note=Concentrated at the budding structures localized at the tips of cisternae.acrosome assembly [GO:0001675]; cellular response to organic cyclic compound [GO:0071407]; defense response to bacterium [GO:0042742]; Leydig cell differentiation [GO:0033327]; luteinizing hormone secretion [GO:0032275]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; positive regulation of cytokine production [GO:0001819]; positive regulation of testosterone secretion [GO:2000845]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of transcription, DNA-templated [GO:0006355]; spermatid nucleus differentiation [GO:0007289]; sperm motility [GO:0030317]; transcription from RNA polymerase II promoter [GO:0006366]FDNA binding [GO:0003677]; transcription cofactor activity [GO:0003712]sendoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]FUNCTION: Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). {ECO:0000269|PubMed:10428808, ECO:0000269|PubMed:1409643, ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:17698061}.Q9Y512SAM503Sorting and assembly machinery component 50 homologSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:15644312}; Multi-pass membrane protein. Cytoplasm {ECO:0000250|UniProtKB:Q6AXV4}. Mitochondrion {ECO:0000269|PubMed:25781180}.cellular protein metabolic process [GO:0044267]; cristae formation [GO:0042407]; mitochondrial respiratory chain complex assembly [GO:0033108]; protein import into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrial sorting and assembly machinery complex [GO:0001401]; mitochondrion [GO:0005739]mFUNCTION: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes (PubMed:22252321, PubMed:25781180). Required for the assembly of TOMM40 into the TOM complex (PubMed:15644312). {ECO:0000269|PubMed:15644312, ECO:0000269|PubMed:22252321, ECO:0000269|PubMed:25781180}.Q9GZZ9UBA5+Ubiquitin-like modifier-activating enzyme 5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18442052}. Nucleus {ECO:0000269|PubMed:18442052}. Note=Localizes mainly in cytoplasm, while it mainly localizes to the nucleus in presence of SUMO2.fATP binding [GO:0005524]; metal ion binding [GO:0046872]; UFM1 activating enzyme activity [GO:0071566]ycytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]FUNCTION: E1-like enzyme which activates UFM1 and SUMO2. {ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:20368332}.Q9NRA84ET7Eukaryotic translation initiation factor 4E transporterySUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22090346}. Nucleus {ECO:0000269|PubMed:22090346}. Nucleus, PML body {ECO:0000269|PubMed:22090346}. Nucleus speckle {ECO:0000269|PubMed:22090346}. Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localization to nuclear foci and speckles requires active transcription.negative regulation of neuron differentiation [GO:0045665]; negative regulation of translation [GO:0017148]; stem cell maintenance [GO:0019827]fmRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; protein transporter activity [GO:0008565]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; PML body [GO:0016605]jFUNCTION: Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism.P08238HS90BHeat shock protein HSP 90-betaSUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.axon guidance [GO:0007411]; cellular response to heat [GO:0034605]; cellular response to interleukin-4 [GO:0071353]; ce< llular response to organic cyclic compound [GO:0071407]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibril organization [GO:0097435]; innate immune response [GO:0045087]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; placenta development [GO:0001890]; positive regulation of cell size [GO:0045793]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of protein binding [GO:0032092]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; protein folding [GO:0006457]; regulation of cellular response to heat [GO:1900034]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; response to salt stress [GO:0009651]; response to unfolded protein [GO:0006986]; virion attachment to host cell [GO:0019062]uATP binding [GO:0005524]; CTP binding [GO:0002135]; dATP binding [GO:0032564]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; kinase binding [GO:0019900]; MHC class II protein complex binding [GO:0023026]; nitric-oxide synthase regulator activity [GO:0030235]; poly(A) RNA binding [GO:0044822]; TPR domain binding [GO:0030911]; UTP binding [GO:0002134]aapical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; inclusion body [GO:0016234]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]5FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:19696785}.O15013ARHGA)Rho guanine nucleotide exchange factor 10$activation of GTPase activity [GO:0090630]; centrosome duplication [GO:0051298]; mitotic spindle assembly [GO:0090307]; myelination in peripheral nervous system [GO:0022011]; positive regulation of stress fiber assembly [GO:0051496]; regulation of Rho protein signal transduction [GO:0035023]Ykinesin binding [GO:0019894]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]kFUNCTION: May play a role in developmental myelination of peripheral nerves. {ECO:0000269|PubMed:14508709}.Q9H825METL8 Methyltransferase-like protein 8'methyltransferase activity [GO:0008168]4FUNCTION: Probable methyltransferase. {ECO:0000250}.Q9UGI8TESTestinhSUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Note=Detected along actin stress fibers.cell junction [GO:0030054]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]OFUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth. {ECO:0000269|PubMed:11420696, ECO:0000269|PubMed:12571287, ECO:0000269|PubMed:12695497}.Q9UJY5GGA1,ADP-ribosylation factor-binding protein GGA1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein.intracellular protein transport [GO:0006886]; positive regulation of protein catabolic process [GO:0045732]; toxin transport [GO:1901998]; vesicle-mediated transport [GO:0016192]clathrin adaptor complex [GO:0030131]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]BFUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif. {ECO:0000269|PubMed:11301005}.Q9NVP1DDX18 ATP-dependent RNA helicase DDX18GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16963496}.*FUNCTION: Probable RNA-dependent helicase.O75581LRP62Low-density lipoprotein receptor-related protein 61SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Note=On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on palmitoylation. Mono-ubiquitination retains it in the endoplasmic reticulum in the absence of palmitoylation. On Wnt signaling, phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at the plasma membrane in LRP6-signalsomes. Chaperoned to the plasma membrane by MESD (By similarity). {ECO:0000250}.axis elongation involved in somitogenesis [GO:0090245]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in neural crest cell differentiation [GO:0044335]; canonical Wnt signaling pathway involved in regulation of cell proliferation [GO:0044340]; cellular response to cholesterol [GO:0071397]; cerebellum morphogenesis [GO:0021587]; cerebral cortex development [GO:0021987]; convergent extension [GO:0060026]; embryonic pattern specification [GO:0009880]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; external genitalia morphogenesis [GO:0035261]; face morphogenesis [GO:0060325]; midbrain development [GO:0030901]; midbrain-hindbrain boundary development [GO:0030917]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; neural crest cell differentiation [GO:0014033]; neural crest formation [GO:0014029]; neural tube closure [GO:0001843]; odontogenesis of dentin-containing tooth [GO:0042475]; palate development [GO:0060021]; pericardium morphogenesis [GO:0003344]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell cycle [GO:0045787]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification [GO:2000055]; primitive streak formation [GO:0090009]; receptor-mediated endocytosis of low-density lipoprotein particle involved in cholesterol transport [GO:0090118]; synaptic transmission [GO:0007268]; thalamus development [GO:0021794]; toxin transport [GO:1901998]; trachea cartilage morphogenesis [GO:0060535]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway involved in dorsal/ventral axis specification [GO:0044332]; Wnt signaling pathway involved in somitogenesis [GO:0090244]apolipoprotein binding [GO:0034185]; coreceptor activity involved in Wnt signaling pathway [GO:0071936]; frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; kinase inhibitor activity [GO:0019210]; low-density lipoprotein receptor activity [GO:0005041]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; toxin transporter activity [GO:0019534]; Wnt-activated rec< eptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]Icell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synapse [GO:0045202]FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250}.P22033MUTA'Methylmalonyl-CoA mutase, mitochondrialcellular lipid metabolic process [GO:0044255]; cobalamin metabolic process [GO:0009235]; fatty acid beta-oxidation [GO:0006635]; homocysteine metabolic process [GO:0050667]; post-embryonic development [GO:0009791]; short-chain fatty acid catabolic process [GO:0019626]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]cobalamin binding [GO:0031419]; metal ion binding [GO:0046872]; methylmalonyl-CoA mutase activity [GO:0004494]; modified amino acid binding [GO:0072341]FUNCTION: Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.Q8IWZ3ANKH11Ankyrin repeat and KH domain-containing protein 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16098192, ECO:0000269|PubMed:16956752}.FUNCTION: May play a role as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. Isoform 2 may possess an antiapoptotic effect and protect cells during normal cell survival through its regulation of caspases. {ECO:0000269|PubMed:16098192}.Q9H0U4RAB1BRas-related protein Rab-1BMSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11389151}. Membrane {ECO:0000269|PubMed:11389151}; Lipid-anchor {ECO:0000269|PubMed:11389151}; Cytoplasmic side {ECO:0000269|PubMed:11389151}. Preautophagosomal structure membrane {ECO:0000269|PubMed:20545908}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). {ECO:0000250}.<autophagy [GO:0006914]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; positive regulation of glycoprotein metabolic process [GO:1903020]; Rab protein signal transduction [GO:0032482]; regulation of autophagosome assembly [GO:2000785]; virion assembly [GO:0019068]endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; mitochondrion [GO:0005739]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. {ECO:0000269|PubMed:20545908, ECO:0000269|PubMed:9437002}.P43686PRS6B"26S protease regulatory subunit 6Btanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; proteasome-activating ATPase activity [GO:0036402]; TBP-class protein binding [GO:0017025]ncytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; inclusion body [GO:0016234]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. {ECO:0000269|PubMed:8060531}.Q5UIP0RIF1 Telomere-associated protein RIF1SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Cytoplasm, cytoskeleton, spindle. Note=Exhibits ATM- and TP53BP1-dependent localization to uncapped or aberrant telomeres and to DNA double strand breaks (DSBs). Does not associate with normal telomere structures. Localizes to microtubules of the midzone of the mitotic spindle during anaphase, and to condensed chromosomes in telophase.cell cycle [GO:0007049]; cellular response to DNA damage stimulus [GO:0006974]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; stem cell maintenance [GO:0019827]; telomere maintenance [GO:0000723]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle [GO:0005819]FUNCTION: Required for checkpoint mediated arrest of cell cycle progression in response to DNA damage during S-phase (the intra-S-phase checkpoint). This checkpoint requires activation of at least 2 parallel pathways by the ATM kinase: one involves the MRN (MRE11A-RAD50-NBS1) complex, while the second requires CHEK2. RIF1 seems to ac< t independently of both these pathways. Seems to play no role in either the G1/S or G2/M DNA damage checkpoints. {ECO:0000269|PubMed:15342490}.Q9UQ35SRRM2+Serine/arginine repetitive matrix protein 2wC2H2 zinc finger domain binding [GO:0070742]; poly(A) RNA binding [GO:0044822]; protein N-terminus binding [GO:0047485]xCajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]3FUNCTION: Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity). Binds to RNA. {ECO:0000250, ECO:0000269|PubMed:10668804}.O14523C2C2L#C2 domain-containing protein 2-likegpositive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]Q8NBK3SUMF1Sulfatase-modifying factor 1mSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15962010}.Dmetal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]@FUNCTION: Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE. {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15657036}.P20339RAB5ARas-related protein Rab-5ASUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Melanosome. Cytoplasmic vesicle {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Membrane. Cytoplasm, cytosol. Note=Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms.2blood coagulation [GO:0007596]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; positive regulation of exocytosis [GO:0045921]; Rab protein signal transduction [GO:0032482]; receptor internalization involved in canonical Wnt signaling pathway [GO:2000286]; regulation of endocytosis [GO:0030100]; regulation of endosome size [GO:0051036]; regulation of filopodium assembly [GO:0051489]; regulation of synaptic vesicle exocytosis [GO:2000300]; synaptic vesicle recycling [GO:0036465]vactin cytoskeleton [GO:0015629]; axon [GO:0030424]; axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytoplasmic side of early endosome membrane [GO:0098559]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; somatodendritic compartment [GO:0036477]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. {ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:16410077}.P09936UCHL10Ubiquitin carboxyl-terminal hydrolase isozyme L1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261853}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19261853}; Lipid-anchor {ECO:0000269|PubMed:19261853}. Note=About 30% of total UCHL1 is associated with membranes in brain.adult walking behavior [GO:0007628]; axon target recognition [GO:0007412]; axon transport of mitochondrion [GO:0019896]; cell proliferation [GO:0008283]; eating behavior [GO:0042755]; muscle fiber development [GO:0048747]; negative regulation of MAP kinase activity [GO:0043407]; neuromuscular process [GO:0050905]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; response to ischemia [GO:0002931]; sensory perception of pain [GO:0019233]+alpha-2A adrenergic receptor binding [GO:0031694]; cysteine-type endopeptidase activity [GO:0004197]; ligase activity [GO:0016874]; omega peptidase activity [GO:0008242]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]FUNCTION: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. {ECO:0000269|PubMed:12408865, ECO:0000269|PubMed:9790970}.O60518RNBP6Ran-binding protein 6OFUNCTION: May function in nuclear protein import as nuclear transport receptor.Q8N335GPD1L1Glycerol-3-phosphate dehydrogenase 1-like proteinsSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17967977}. Note=Localized to the region of the plasma membrane.carbohydrate metabolic process [GO:0005975]; cellular lipid metabolic process [GO:0044255]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerophospholipid biosynthetic process [GO:0046474]; NADH metabolic process [GO:0006734]; NAD metabolic process [GO:0019674]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of protein kinase C signaling [GO:0090038]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of sodium ion transport [GO:0010765]; regulation of heart rate [GO:0002027]; regulation of sodium ion transmembrane transporter activity [GO:2000649]; regulation of ventricular cardiac muscle cell membrane depolarization [GO:0060373]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; ventricular cardiac muscle cell action potential [GO:0086005]glycerol-3-phosphate dehydrogenase [NAD+] activity [GO:0004367]; ion channel binding [GO:0044325]; NAD binding [GO:0051287]; sodium channel regulator activity [GO:0017080]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]; plasma membrane [GO:0005886]FUNCTION: Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L. {ECO:0000269|PubMed:19666841, ECO:0000269|PubMed:19745168}.Q15269PWP2%Periodic tryptophan protein 2 homologmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit assembly [GO:0000028]cytoplasm [GO:0005737]; nucleolus [GO:0005730]; Pwp2p-containing subcomplex of 90S preribosome [GO:0034388]; small-subunit processome [GO:0032040]Q6P1J9CDC73 ParafibrominvSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622}.fcell cycle [GO:0007049]; cellular response to lipopolysaccharide [GO:0071222]; endodermal c< ell fate commitment [GO:0001711]; histone H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; mRNA polyadenylation [GO:0006378]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of Wnt signaling pathway [GO:0030177]; protein destabilization [GO:0031648]; stem cell maintenance [GO:0019827]; transcription elongation from RNA polymerase II promoter [GO:0006368]; Wnt signaling pathway [GO:0016055]+RNA polymerase II core binding [GO:0000993]OCdc73/Paf1 complex [GO:0016593]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]]FUNCTION: Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors. {ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820, ECO:0000269|PubMed:16989776, ECO:0000269|PubMed:19136632, ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.Q12841FSTL1Follistatin-related protein 1GBMP signaling pathway [GO:0030509]; response to starvation [GO:0042594]>calcium ion binding [GO:0005509]; heparin binding [GO:0008201]FUNCTION: May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity). {ECO:0000250}.Q9NZT2OGFROpioid growth factor receptorSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The OGF/OGFR complex is probably translocated to the nucleus.Vopioid receptor signaling pathway [GO:0038003]; regulation of cell growth [GO:0001558]%opioid receptor activity [GO:0004985]{FUNCTION: Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation.Q6ZUT6CO052 Uncharacterized protein C15orf52Q93063EXT2 Exostosin-2Lcarbohydrate metabolic process [GO:0005975]; cell differentiation [GO:0030154]; cellular polysaccharide biosynthetic process [GO:0033692]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; mesoderm formation [GO:0001707]; ossification [GO:0001503]; protein glycosylation [GO:0006486]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0050508]; glucuronosyltransferase activity [GO:0015020]; heparan sulfate N-acetylglucosaminyltransferase activity [GO:0042328]; metal ion binding [GO:0046872]; N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity [GO:0050509]; protein heterodimerization activity [GO:0046982]; transferase activity, transferring glycosyl groups [GO:0016757],endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; UDP-N-acetylglucosamine transferase complex [GO:0043541]FUNCTION: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor.P98198AT8B2#Phospholipid-transporting ATPase IDSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein. Cell membrane. Note=TMEM30A, but not TMEM30B, is required for its export from ER to the plasma membrane.Golgi organization [GO:0007030]; ion transmembrane transport [GO:0034220]; phospholipid translocation [GO:0045332]; transmembrane transport [GO:0055085]Q9BRS2RIOK1$Serine/threonine-protein kinase RIO1P49711CTCFTranscriptional repressor CTCFSSUBCELLULAR LOCATION: Nucleus, nucleoplasm. Chromosome. Chromosome, centromere. Note=May translocate to the nucleolus upon cell differentiation. Associates with both centromeres and chromosomal arms during metaphase. Associates with the H19 ICR in mitotic chromosomes. May be preferentially excluded from heterochromatin during interphase.chromatin modification [GO:0016568]; chromosome segregation [GO:0007059]; DNA methylation [GO:0006306]; maintenance of DNA methylation [GO:0010216]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome positioning [GO:0016584]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of centromeric sister chromatid cohesion [GO:0070602]; regulation of gene expression, epigenetic [GO:0040029]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of histone acetylation [GO:0035065]; regulation of histone methylation [GO:0031060]; regulation of molecular function, epigenetic [GO:0040030]chromatin insulator sequence binding [GO:0043035]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]; transcription regulatory region DNA binding [GO:0044212]; zinc ion binding [GO:0008270]chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; nucleolus [< GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Chromatin binding factor that binds to DNA sequence specific sites. Involved in transcriptional regulation by binding to chromatin insulators and preventing interaction between promoter and nearby enhancers and silencers. Acts as transcriptional repressor binding to promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene expression. Plays an essential role in oocyte and preimplantation embryo development by activating or repressing transcription. Seems to act as tumor suppressor. Plays a critical role in the epigenetic regulation. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, binding within the H19 imprinting control region (ICR) mediates maternally inherited higher-order chromatin conformation to restrict enhancer access to IGF2. Plays a critical role in gene silencing over considerable distances in the genome. Preferentially interacts with unmethylated DNA, preventing spreading of CpG methylation and maintaining methylation-free zones. Inversely, binding to target sites is prevented by CpG methylation. Plays a important role in chromatin remodeling. Can dimerize when it is bound to different DNA sequences, mediating long-range chromatin looping. Mediates interchromosomal association between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a common transcription factory. Causes local loss of histone acetylation and gain of histone methylation in the beta-globin locus, without affecting transcription. When bound to chromatin, it provides an anchor point for nucleosomes positioning. Seems to be essential for homologous X-chromosome pairing. May participate with Tsix in establishing a regulatable epigenetic switch for X chromosome inactivation. May play a role in preventing the propagation of stable methylation at the escape genes from X- inactivation. Involved in sister chromatid cohesion. Associates with both centromeres and chromosomal arms during metaphase and required for cohesin localization to CTCF sites. Regulates asynchronous replication of IGF2/H19. {ECO:0000269|PubMed:11743158, ECO:0000269|PubMed:16815976, ECO:0000269|PubMed:17827499, ECO:0000269|PubMed:18347100, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18550811, ECO:0000269|PubMed:18654629, ECO:0000269|PubMed:19322193, ECO:0000269|PubMed:8649389, ECO:0000269|PubMed:9591631}.Q96F46I17RAInterleukin-17 receptor ASUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted.$cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; fibroblast activation [GO:0072537]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of interleukin-23 production [GO:0032747]-interleukin-17 receptor activity [GO:0030368]Uextracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]FUNCTION: Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling. {ECO:0000269|PubMed:19838198, ECO:0000269|PubMed:21993848}.O15091MRRP3&Mitochondrial ribonuclease P protein 3BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18984158}.FUNCTION: Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. {ECO:0000269|PubMed:18984158}.P19438TNR1A4Tumor necrosis factor receptor superfamily member 1ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22801493}; Single-pass type I membrane protein {ECO:0000269|PubMed:22801493}. Golgi apparatus membrane {ECO:0000269|PubMed:22801493}; Single-pass type I membrane protein {ECO:0000269|PubMed:22801493}. Secreted {ECO:0000269|PubMed:22801493}. Note=A secreted form is produced through proteolytic processing.; SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; cytokine-mediated signaling pathway [GO:0019221]; death-inducing signaling complex assembly [GO:0071550]; defense response to bacterium [GO:0042742]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; negative regulation of inflammatory response [GO:0050728]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of inflammatory response [GO:0050729]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tyrosine phosphorylation of Stat1 protein [GO:0042511]; prostaglandin metabolic process [GO:0006693]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; viral process [GO:0016032]>tumor necrosis factor-activated receptor activity [GO:0005031]cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.Q9H0R8GBRL1:Gamma-aminobutyric acid receptor-associated protein-like 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Lipid-anchor. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, autophagosome.autophagosome assembly [GO:0000045]; membrane fusion [GO:0061025]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]beta-tubulin binding [GO:0048487]; GABA receptor binding [GO:0050811]; microtubule binding [GO:0008017]; Tat protein binding [GO:0030957]autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cell body [GO:0044297]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; dendrite membrane [GO:0032590]; endoplasmic reticulum [GO:0005783]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; microtubule [GO:0005874]; pre-autophagosomal structure [GO:0000407]FUNCTION: Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:16431922, ECO:0000269|PubMed:20404487}.O00213APBB1;Amyloid beta A4 precursor protein-binding family B member 1SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. Cell projection, growth cone {ECO:0000250}. Nucleus speckle. Note=Colocalizes with TSHZ3 in axonal growth cone (By similarity). In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP. Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus. Nuclear translocation is under the regulation of APP. Colocalizes with TSHZ3 in the nucleus. Colocal< izes with NEK6 at the nuclear speckles. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). {ECO:0000250}.4apoptotic process [GO:0006915]; axonogenesis [GO:0007409]; cell cycle arrest [GO:0007050]; cellular response to DNA damage stimulus [GO:0006974]; histone H4 acetylation [GO:0043967]; negative regulation of cell growth [GO:0030308]; negative regulation of thymidylate synthase biosynthetic process [GO:0050760]; positive regulation of apoptotic process [GO:0043065]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]beta-amyloid binding [GO:0001540]; chromatin binding [GO:0003682]; histone binding [GO:0042393]; proline-rich region binding [GO:0070064]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]oFUNCTION: Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). {ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19343227}.P783143BP2SH3 domain-binding protein 2Ypositive regulation of signal transduction [GO:0009967]; signal transduction [GO:0007165]%SH3/SH2 adaptor activity [GO:0005070]FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism.Q8ND56LS14AProtein LSM14 homolog AzSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Note=Targeted to stress granules (SGs) in response to cellular stress. cytoplasmic mRNA processing body assembly [GO:0033962]; multicellular organismal development [GO:0007275]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; regulation of translation [GO:0006417]; RIG-I signaling pathway [GO:0039529]double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; single-stranded RNA binding [GO:0003727]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytoplasmic stress granule [GO:0010494]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs. {ECO:0000269|PubMed:16484376, ECO:0000269|PubMed:17074753}.P13647K2C5Keratin, type II cytoskeletal 5lcell junction assembly [GO:0034329]; epidermis development [GO:0008544]; hemidesmosome assembly [GO:0031581]Zscaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q9H8Y5ANKZ1:Ankyrin repeat and zinc finger domain-containing protein 1ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; nucleus-associated proteasomal ubiquitin-dependent protein catabolic process [GO:0071630]ICdc48p-Npl4p-Vms1p AAA ATPase complex [GO:0036266]; membrane [GO:0016020]jFUNCTION: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. {ECO:0000250}.Q99985SEM3C Semaphorin-3Caxon guidance [GO:0007411]; blood vessel remodeling [GO:0001974]; cardiac right ventricle morphogenesis [GO:0003215]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; immune response [GO:0006955]; limb bud formation [GO:0060174]; neural crest cell migration [GO:0001755]; neural tube development [GO:0021915]; outflow tract morphogenesis [GO:0003151]; post-embryonic development [GO:0009791]; pulmonary myocardium development [GO:0003350]; response to drug [GO:0042493]; somitogenesis [GO:0001756]GFUNCTION: Binds to plexin family members and plays an important role in the regulation of developmental processes. Required for normal cardiovascular development during embryogenesis. Functions as attractant for growing axons, and thereby plays an important role in axon growth and axon guidance (By similarity). {ECO:0000250}.Q14166TTL12(Tubulin--tyrosine ligase-like protein 122cellular protein modification process [GO:0006464]P42898MTHR#Methylenetetrahydrofolate reductaseblood circulation [GO:0008015]; cellular amino acid metabolic process [GO:0006520]; folic acid metabolic process [GO:0046655]; heterochromatin maintenance [GO:0070829]; homocysteine metabolic process [GO:0050667]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; regulation of histone methylation [GO:0031060]; response to drug [GO:0042493]; response to folic acid [GO:0051593]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; response to vitamin B2 [GO:0033274]; S-adenosylmethionine metabolic process [GO:0046500]; small molecule metabolic process [GO:0044281]; tetrahydrofolate interconversion [GO:0035999]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]flavin adenine dinucleotide binding [GO:0050660]; methylenetetrahydrofolate reductase (NAD(P)H) activity [GO:0004489]; modified amino acid binding [GO:0072341]; NADP binding [GO:0050661]; protein complex binding [GO:0032403]4cytosol [GO:0005829]; neuron projection [GO:0043005]FUNCTION: Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine.P60002ELOF1)Transcription elongation factor 1 homologFUNCTION: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions. {ECO:0000250}.P55060XPO2 Exportin-2^SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm.iapoptotic process [GO:0006915]; cell proliferation [GO:0008283]; protein export from nucleus [GO:0006611]4importin-alpha export receptor activity [GO:0008262]FUNCTION: Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric d< istribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:9323134}.O15021MAST48Microtubule-associated serine/threonine-protein kinase 4\intracellular signal transduction [GO:0035556]; peptidyl-serine phosphorylation [GO:0018105]sATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine/threonine kinase activity [GO:0004674]2cytoplasm [GO:0005737]; intracellular [GO:0005622]Q9BYC5FUT8Alpha-(1,6)-fucosyltransferaseSUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.cell migration [GO:0016477]; cellular protein metabolic process [GO:0044267]; GDP-L-fucose metabolic process [GO:0046368]; integrin-mediated signaling pathway [GO:0007229]; in utero embryonic development [GO:0001701]; L-fucose catabolic process [GO:0042355]; N-glycan fucosylation [GO:0036071]; N-glycan processing [GO:0006491]; oligosaccharide biosynthetic process [GO:0009312]; post-translational protein modification [GO:0043687]; protein glycosylation in Golgi [GO:0033578]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; receptor metabolic process [GO:0043112]; respiratory gaseous exchange [GO:0007585]; transforming growth factor beta receptor signaling pathway [GO:0007179]?glycoprotein 6-alpha-L-fucosyltransferase activity [GO:0008424]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. {ECO:0000269|PubMed:17172260, ECO:0000269|PubMed:9133635}.Q13153PAK1%Serine/threonine-protein kinase PAK 1JSUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Cell membrane. Cell projection, ruffle membrane. Note=Recruited to the cell membrane by interaction with CDC42 and RAC1. Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin.}actin cytoskeleton reorganization [GO:0031532]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; branching morphogenesis of an epithelial tube [GO:0048754]; cell migration [GO:0016477]; dendrite development [GO:0016358]; ephrin receptor signaling pathway [GO:0048013]; exocytosis [GO:0006887]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; negative regulation of cell proliferation involved in contact inhibition [GO:0060244]; neuromuscular junction development [GO:0007528]; neuron projection morphogenesis [GO:0048812]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stress fiber assembly [GO:0051496]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; receptor clustering [GO:0043113]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated protein kinase signaling cascade [GO:0031098]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; wound healing [GO:0042060]ATP binding [GO:0005524]; collagen binding [GO:0005518]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; Rac GTPase binding [GO:0048365]axon [GO:0030424]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; intercalated disc [GO:0014704]; neuronal postsynaptic density [GO:0097481]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; Z disc [GO:0030018] FUNCTION: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. {ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:12876277, ECO:0000269|PubMed:14585966, ECO:0000269|PubMed:15611088, ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:16278681, ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677, ECO:0000269|PubMed:8805275, ECO:0000269|PubMed:9032240, ECO:0000269|PubMed:9395435, ECO:0000269|PubMed:9528787}.P29084T2EB0Transcription initiation factor IIE subunit betawcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor TFIIE complex [GO:0005673]FUNCTION: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.Q9H6H4REEP4'Receptor expression-enhancing protein 4SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23911198}; Multi-pass membrane protein {ECO:0000269|PubMed:23911198}.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope reassembly [GO:0007084]; nuclear envelope organization [GO:0006998]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; microtubule [GO:0005874]5FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering t< he endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes. {ECO:0000269|PubMed:23911198}.P55210CASP7 Caspase-7activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; execution phase of apoptosis [GO:0097194]; intrinsic apoptotic signaling pathway [GO:0097193]; programmed cell death [GO:0012501]; proteolysis [GO:0006508]cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; cysteine-type peptidase activity [GO:0008234]1FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.O95832CLD1 Claudin-1calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; establishment of skin barrier [GO:0061436]; viral process [GO:0016032]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lateral plasma membrane [GO:0016328]FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (PubMed:23407391). CLDN1 acts as a coreceptor for HCV entry into hepatic cells. {ECO:0000269|PubMed:23407391}.Q9H4L7SMRCDlSWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage.ATP-dependent chromatin remodeling [GO:0043044]; chromatin modification [GO:0016568]; chromatin remodeling [GO:0006338]; chromosome separation [GO:0051304]; DNA double-strand break processing [GO:0000729]; histone H3 deacetylation [GO:0070932]; histone H4 deacetylation [GO:0070933]; nucleotide metabolic process [GO:0009117]; positive regulation of transcription, DNA-templated [GO:0045893]; protein homooligomerization [GO:0051260]; regulation of DNA recombination [GO:0000018]uATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; nucleic acid binding [GO:0003676]heterochromatin [GO:0000792]; nuclear matrix [GO:0016363]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; site of double-strand break [GO:0035861]FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing. {ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:22960744}.P07237PDIA1Protein disulfide-isomeraseSUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000305}.Ycell redox homeostasis [GO:0045454]; cellular response to hypoxia [GO:0071456]; extracellular matrix organization [GO:0030198]; lipoprotein metabolic process [GO:0042157]; peptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]; positive regulation of viral entry into host cell [GO:0046598]; protein folding [GO:0006457]; proteolysis [GO:0006508]; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902175]; response to endoplasmic reticulum stress [GO:0034976]; response to reactive oxygen species [GO:0000302]; small molecule metabolic process [GO:0044281]endopeptidase activity [GO:0004175]; poly(A) RNA binding [GO:0044822]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; melanosome [GO:0042470]; procollagen-proline 4-dioxygenase complex [GO:0016222]MFUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997}.Q3ZCQ8TIM50=Mitochondrial import inner membrane translocase subunit TIM50-SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15044455, ECO:0000269|PubMed:16008839}; Single-pass membrane protein {ECO:0000269|PubMed:15044455, ECO:0000269|PubMed:16008839}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus speckle. Note=Nuclear and enriched in speckles with snRNPs.[cellular protein metabolic process [GO:0044267]; mitochondrial membrane organization [GO:0007006]; peptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]; release of cytochrome c from mitochondria [GO:0001836]interleukin-2 receptor binding [GO:0005134]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial inner membrane presequence translocase complex [GO:0005744]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]wFUNCTION: Essential component of the TIM23 complex, a complex that media< tes the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Has some phosphatase activity in vitro; however such activity may not be relevant in vivo. Isoform 2 may participate in the release of snRNPs and SMN from the Cajal body. {ECO:0000269|PubMed:15044455}.Q5VWQ0RSBN1Round spermatid basic protein 1P05362ICAM1!Intercellular adhesion molecule 1adhesionw acute inflammatory response to antigenic stimulus [GO:0002438]; adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell aging [GO:0007569]; cellular response to alkaloid [GO:0071312]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nutrient levels [GO:0031669]; cellular response to tumor necrosis factor [GO:0071356]; cytokine-mediated signaling pathway [GO:0019221]; establishment of endothelial barrier [GO:0061028]; establishment of Sertoli cell barrier [GO:0097368]; extracellular matrix organization [GO:0030198]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; interferon-gamma-mediated signaling pathway [GO:0060333]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; membrane to membrane docking [GO:0022614]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; ovarian follicle development [GO:0001541]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cellular extravasation [GO:0002693]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of vasoconstriction [GO:0045907]; receptor-mediated virion attachment to host cell [GO:0046813]; regulation of cell adhesion [GO:0030155]; regulation of cell shape [GO:0008360]; regulation of immune response [GO:0050776]; regulation of leukocyte mediated cytotoxicity [GO:0001910]; regulation of ruffle assembly [GO:1900027]; response to amino acid [GO:0043200]; response to amphetamine [GO:0001975]; response to copper ion [GO:0046688]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to gonadotropin [GO:0034698]; response to ionizing radiation [GO:0010212]; response to organic cyclic compound [GO:0014070]; response to sulfur dioxide [GO:0010477]; sensory perception of sound [GO:0007605]; T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:0002291]; T cell antigen processing and presentation [GO:0002457]integrin binding [GO:0005178]; receptor activity [GO:0004872]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618]Tcell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742, ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.Q86XN7PRSR1!Proline and serine-rich protein 1O95487SC24B Protein transport protein Sec24BSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Endoplasmic reticulum membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000250}.Qantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; aorta morphogenesis [GO:0035909]; auditory receptor cell stereocilium organization [GO:0060088]; cellular protein metabolic process [GO:0044267]; cochlear nucleus development [GO:0021747]; COPII vesicle coating [GO:0048208]; coronary artery morphogenesis [GO:0060982]; ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; lung lobe morphogenesis [GO:0060463]; membrane organization [GO:0061024]; neural tube closure [GO:0001843]; outflow tract morphogenesis [GO:0003151]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; pulmonary artery morphogenesis [GO:0061156]; regulation of cargo loading into COPII-coated vesicle [GO:1901301]; regulation of establishment of planar polarity involved in neural tube closure [GO:0090178]; small molecule metabolic process [GO:0044281]; vesicle-mediated transport [GO:0016192]@transporter activity [GO:0005215]; zinc ion binding [GO:0008270]COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]Q7Z460CLAP1CLIP-associating protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Golgi apparatus, trans-Golgi network {ECO:0000305}. Note=Localizes to microtubule plus ends. Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase. In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2.axon guidance [GO:0007411]; cell division [GO:0051301]; establishment of epithelial cell polarity [GO:0090162]; establishment of spindle orientation [GO:0051294]; establishment or maintenance of cell polarity [GO:0007163]; exit from mitosis [GO:0010458]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi organization [GO:0007030]; microtubule anchoring [GO:0034453]; microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleation [GO:0007020]; microtubule organizing center organization [GO:0031023]; mitotic cell cycle [GO:0000278]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of microtubule polymerization or depolymerization [GO:0031111]; negative regulation of stress fiber assembly [GO:0051497]; negative regulation of wound healing, spreading of epidermal cells [GO:1903690]; organelle organization [GO:0006996]; positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of exocytosis [GO:0045921]; positive regulation of extracellular matrix disassembly [GO:0090091]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; regulation of gastrulation [GO:0010470]; regulation of microtubule cytoskeleton organization [GO:0070507]; small GTPase mediated signal transduction [GO:0007264]; vesicle targeting [GO:0006903]dystroglycan binding [GO:0002162]; kinetochore binding [GO:0043515]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]basal cortex [GO:0045180]; cell cortex [GO:0005938]; centrosomal corona [GO:0031592]; centrosome [GO:00< 05813]; condensed chromosome kinetochore [GO:0000777]; cortical microtubule cytoskeleton [GO:0030981]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; membrane [GO:0016020]; spindle microtubule [GO:0005876]FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:12837247, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864}.Q96KC8DNJC1!DnaJ homolog subfamily C member 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane; Single-pass type I membrane protein. Microsome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.negative regulation of proteolysis [GO:0045861]; positive regulation of ATPase activity [GO:0032781]; protein folding [GO:0006457]; regulation of protein secretion [GO:0050708]; regulation of translation [GO:0006417]@ATPase activator activity [GO:0001671]; DNA binding [GO:0003677]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]8FUNCTION: May modulate protein synthesis. {ECO:0000250}.O43765SGTAFSmall glutamine-rich tetratricopeptide repeat-containing protein alpha{positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; viral process [GO:0016032]!BAT3 complex binding [GO:1904288]FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. {ECO:0000269|PubMed:18759457}.P35568IRS1Insulin receptor substrate 1)Aldosterone-regulated sodium reabsorptioncellular response to insulin stimulus [GO:0032869]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glucose homeostasis [GO:0042593]; innate immune response [GO:0045087]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin receptor signaling pathway [GO:0008286]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; lipid catabolic process [GO:0016042]; mammary gland development [GO:0030879]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of insulin secretion [GO:0046676]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of fatty acid beta-oxidation [GO:0032000]; positive regulation of glucose import [GO:0046326]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; protein kinase B signaling [GO:0043491]; protein localization to nucleus [GO:0034504]; regulation of gene expression [GO:0010468]; response to insulin [GO:0032868]; response to peptide hormone [GO:0043434]; signal transduction [GO:0007165]Rinsulin-like growth factor receptor binding [GO:0005159]; insulin receptor binding [GO:0005158]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein kinase C binding [GO:0005080]; SH2 domain binding [GO:0042169]; signal transducer activity [GO:0004871]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]caveola [GO:0005901]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; insulin receptor complex [GO:0005899]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]jFUNCTION: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity). {ECO:0000250}.P51687SUOXSulfite oxidase, mitochondrial Energy metabolismXcellular nitrogen compound metabolic process [GO:0034641]; nitrate assimilation [GO:0042128]; response to nutrient [GO:0007584]; small molecule metabolic process [GO:0044281]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]; sulfur amino acid catabolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; sulfite oxidase activity [GO:0008482]gcytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]Q6PJI9WDR59WD repeat-containing protein 59jcellular response to amino acid starvation [GO:0034198]; positive regulation of TOR signaling [GO:0032008]GATOR2 complex [GO:0061700]FUNCTION: As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.Q96EU7C1GLCC1GALT1-specific chaperone 15cellular protein metabolic process [GO:0044267]; O-glycan processing [GO:0016266]; platelet activation [GO:0030168]; platelet morphogenesis [GO:0036344]; positive regulation of transferase activity [GO:0051347]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]Cpolypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]XFUNCTION: Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1). {ECO:0000269|PubMed:12464682}.Q02790FKBP4)Peptidyl-prolyl cis-trans isomerase FKBP4SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Mitochondrion. Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor.androgen receptor signaling pathway [GO:0030521]; cellular response to heat [GO:0034605]; chaperone-mediated protein folding [GO:0061077]; copper ion transport [GO:0006825]; embryo implantation [GO:0007566]; male sex differentiation [GO:0046661]; negative regulation of microtubule polymerization [GO:0031115]; negative regulation of microtubule polymerization or depolymerization [GO:0031111]; negative regulation of neuron projection development [GO:0010977]; prostate gland development [GO:0030850]; protein complex localization [GO:0031503]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of cellular response to heat [GO:1900034]; steroid hormone receptor complex assembly [GO:0006463]ATP binding [GO:0005524]; FK506 binding [GO< :0005528]; GTP binding [GO:0005525]; heat shock protein binding [GO:0031072]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]; protein binding, bridging [GO:0030674]=axonal growth cone [GO:0044295]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. {ECO:0000269|PubMed:1279700, ECO:0000269|PubMed:1376003, ECO:0000269|PubMed:19945390, ECO:0000269|PubMed:21730050, ECO:0000269|PubMed:2378870}.O43688LPP2"Lipid phosphate phosphohydrolase 2dephosphorylation [GO:0016311]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]aphosphatidate phosphatase activity [GO:0008195]; phosphoprotein phosphatase activity [GO:0004721]`integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886] FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P.A6NEF3GG6L43Putative golgin subfamily A member 6-like protein 4Q9BU23LMF2Lipase maturation factor 2FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. May be required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway (By similarity). {ECO:0000250}.Q96DI7SNR401U5 small nuclear ribonucleoprotein 40 kDa protein;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9731529}.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; small nucleolar ribonucleoprotein complex [GO:0005732]; U5 snRNP [GO:0005682]FUNCTION: Component of the U5 small nuclear ribonucleoprotein (snRNP) complex. The U5 snRNP is part of the spliceosome, a multiprotein complex that catalyzes the removal of introns from pre-messenger RNAs. {ECO:0000269|PubMed:9774689}.Q9ULU4PKCB1"Protein kinase C-binding protein 1Qnegative regulation of transcription from RNA polymerase II promoter [GO:0000122]repressing transcription factor binding [GO:0070491]; RNA polymerase II transcription corepressor activity [GO:0001106]; zinc ion binding [GO:0008270]P30046DOPDD-dopachrome decarboxylase)melanin biosynthetic process [GO:0042438]\D-dopachrome decarboxylase activity [GO:0033981]; dopachrome isomerase activity [GO:0004167]aFUNCTION: Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).Q8NEL9DDHD1Phospholipase DDHD1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15623529}._lipid catabolic process [GO:0016042]; positive regulation of mitochondrial fission [GO:0090141]FUNCTION: Phospholipase that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid. The different isoforms may change the substrate specificity. {ECO:0000269|PubMed:22922100}.P23786CPT21Carnitine O-palmitoyltransferase 2, mitochondrialcarnitine shuttle [GO:0006853]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; small molecule metabolic process [GO:0044281]wmitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]Q13393PLD1Phospholipase D1rSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.fcell motility [GO:0048870]; chemotaxis [GO:0006935]; defense response to Gram-positive bacterium [GO:0050830]; exocytosis [GO:0006887]; glycerophospholipid biosynthetic process [GO:0046474]; inositol lipid-mediated signaling [GO:0048017]; membrane lipid metabolic process [GO:0006643]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; Ras protein signal transduction [GO:0007265]; regulation of cell migration [GO:0030334]; regulation of microvillus assembly [GO:0032534]; regulation of phagocytosis [GO:0050764]; regulation of vesicle-mediated transport [GO:0060627]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]N-acylphosphatidylethanolamine-specific phospholipase D activity [GO:0070290]; phosphatidylinositol binding [GO:0035091]; phospholipase D activity [GO:0004630]Mapical plasma membrane [GO:0016324]; endocytic vesicle [GO:0030139]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471] FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity). {ECO:0000250}.Q6UW63KDEL1KDEL motif-containing protein 1)glycolipid metabolic process [GO:0006664])glucosyltransferase activity [GO:0046527]Q96LJ7DHRS1+Dehydrogenase/reductase SDR family member 1Mendoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]Q92538GBF1JGolgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1pSUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027, ECO:0000269|PubMed:15616190}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:12808027}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23386609}. Cytoplasm {ECO:0000269|PubMed:22573891}. Lipid droplet {ECO:0000269|PubMed:21789191}. Membrane; Peripheral membrane protein {ECO:0000305}. Note=Cycles rapidly on and off early Golgi membranes (PubMed:15616190). Stabilized on membranes when complexed with ARF1-GDP and is released from both ARF1 and membranes after it catalyzes GDP displacement and ARF1 binds GTP. Continuous cycles of recruitment and dissociation of GBF1 to membranes are required for sustained ARF activation and COP I recruitment (PubMed:15813748). In neutrophils is translocated from the Golgi to the leading edge upon GPCR stimulation (PubMed:22573891). Localization to lipid droplets is questionable (PubMed:22185782). {ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891, ECO:0000305|PubMed:15616190, ECO:0000305|PubMed:15813748}.cell activation involved in immune response [GO:0002263]; COPI coating of Golgi vesicle [GO:0048205]; endoplasmic reticulum-Golgi intermediate compartment organization [GO:0097111]; establishment of monopolar cell polarity [GO:0061162]; Golgi disassembly [GO:0090166]; G< olgi organization [GO:0007030]; Golgi to endosome transport [GO:0006895]; membrane organization [GO:0061024]; neutrophil chemotaxis [GO:0030593]; organelle organization [GO:0006996]; positive regulation of GTPase activity [GO:0043547]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization to endoplasmic reticulum exit site [GO:0070973]; protein localization to endoplasmic reticulum tubular network [GO:1903420]; protein localization to Golgi apparatus [GO:0034067]; protein transport [GO:0015031]; reactive oxygen species biosynthetic process [GO:1903409]; regulation of ARF protein signal transduction [GO:0032012]; regulation of cell adhesion [GO:0030155]; regulation of mitotic cell cycle [GO:0007346]; regulation of protein localization to cell surface [GO:2000008]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; viral process [GO:0016032]ARF guanyl-nucleotide exchange factor activity [GO:0005086]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]cell leading edge [GO:0031252]; cis-Golgi network [GO:0005801]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the Arf family of small GTPases involved in trafficking in the early secretory pathway; its GEF activity initiates the coating of nascent vesicles via the localized generation of activated ARFs through replacement of GDP with GTP. Recruitment to cis-Golgi membranes requires membrane association of Arf-GDP and can be regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat complex to the endoplasmic reticulum exit sites (ERES), and the endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi compartments which implicates ARF1 activation. Involved in COPI vesicle-dependent retrograde transport from the ERGIC and cis-Golgi compartments to the endoplasmatic reticulum (ER) (PubMed:16926190, PubMed:17956946, PubMed:18003980, PubMed:12047556, PubMed:12808027, PubMed:19039328, PubMed:24213530). Involved in the trans-Golgi network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1 adaptor protein complex related to chlathrin-dependent transport; the function requires its GEF activity (probably at least in part on ARF4 and ARF5) (PubMed:23386609). Has GEF activity towards ARF1 (PubMed:15616190). Has in vitro GEF activity towards ARF5 (By similarity). Involved in the processing of PSAP (PubMed:17666033). Required for the assembly of the Golgi apparatus (PubMed:12808027, PubMed:18003980). The AMPK-phosphorylated form is involved in Golgi disassembly during mitotis and under stress conditions (PubMed:18063581, PubMed:23418352). May be involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid droplets; however, this function is under debate (PubMed:19461073, PubMed:22185782). In neutrophils, involved in G protein-coupled receptor (GPCR)-mediated chemotaxis und superoxide production. Proposed to be recruited by phosphatidylinositol-phosphates generated upon GPCR stimulation to the leading edge where it recruits and activates ARF1, and is involved in recruitment of GIT2 and the NADPH oxidase complex (PubMed:22573891). {ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027, ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:16926190, ECO:0000269|PubMed:17666033, ECO:0000269|PubMed:17956946, ECO:0000269|PubMed:18003980, ECO:0000269|PubMed:18063581, ECO:0000269|PubMed:19461073, ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891, ECO:0000269|PubMed:23386609, ECO:0000269|PubMed:23418352, ECO:0000269|PubMed:24213530, ECO:0000305|PubMed:19039328, ECO:0000305|PubMed:22573891}.Q5RI15COX20'Cytochrome c oxidase protein 20 homologfSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.Q9GZX9TWSG1&Twisted gastrulation protein homolog 1BMP signaling pathway [GO:0030509]; camera-type eye development [GO:0043010]; cell differentiation [GO:0030154]; forebrain development [GO:0030900]; hemopoiesis [GO:0030097]; mesoderm formation [GO:0001707]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of osteoblast differentiation [GO:0045668]; ossification [GO:0001503]; positive regulation of BMP signaling pathway [GO:0030513]; salivary gland morphogenesis [GO:0007435]FUNCTION: May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases BMPs from ternary complexes. May be an important modulator of BMP-regulated cartilage development and chondrocyte differentiation. May play a role in thymocyte development (By similarity). {ECO:0000250}.Q96KQ7EHMT2(Histone-lysine N-methyltransferase EHMT2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11316813}. Chromosome {ECO:0000269|PubMed:11316813}. Note=Associates with euchromatic regions. Does not associate with heterochromatin.chromatin organization [GO:0006325]; DNA methylation [GO:0006306]; histone H3-K27 methylation [GO:0070734]; histone H3-K9 methylation [GO:0051567]; histone lysine methylation [GO:0034968]; histone methylation [GO:0016571]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; peptidyl-lysine dimethylation [GO:0018027]; regulation of DNA replication [GO:0006275]^C2H2 zinc finger domain binding [GO:0070742]; histone-lysine N-methyltransferase activity [GO:0018024]; histone methyltransferase activity (H3-K27 specific) [GO:0046976]; histone methyltransferase activity (H3-K9 specific) [GO:0046974]; p53 binding [GO:0002039]; protein-lysine N-methyltransferase activity [GO:0016279]; zinc ion binding [GO:0008270]intermediate filament cytoskeleton [GO:0045111]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:18438403, ECO:0000269|PubMed:20084102, ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22387026, ECO:0000269|PubMed:8457211}.Q8N5K1CISD2-CDGSH iron-sulfur domain-containing protein 2GSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein. Note=According to PubMed:20010695, it mainly localizes to the endoplasmic reticulum. However, experiments in mouse showed that it mainly localizes to the mitochondrion outer membrane.ymitochondrion degradation [GO:0000422]; multicellular organismal aging [GO:0010259]; regulation of autophagy [GO:0010506]< 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; protein complex [GO:0043234]FUNCTION: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy. {ECO:0000269|PubMed:17846994, ECO:0000269|PubMed:20010695}.Q8IZU8DSEL'Dermatan-sulfate epimerase-like proteincarbohydrate metabolic process [GO:0005975]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; glycosaminoglycan metabolic process [GO:0030203]; small molecule metabolic process [GO:0044281]achondroitin-glucuronate 5-epimerase activity [GO:0047757]; sulfotransferase activity [GO:0008146]O00161SNP23"Synaptosomal-associated protein 23SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome. Note=Mainly localized to the plasma membrane.aexocytosis [GO:0006887]; histamine secretion by mast cell [GO:0002553]; membrane fusion [GO:0061025]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle targeting [GO:0006903]@azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mast cell granule [GO:0042629]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; specific granule [GO:0042581]; synapse [GO:0045202]FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.Q9BXY0MAK16Protein MAK16 homologdSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849}.Mintracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]Q5VSL9STRP1Striatin-interacting protein 1dSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}. Note=Enriched on the plasma membrane.dcortical actin cytoskeleton organization [GO:0030866]; regulation of cell morphogenesis [GO:0022604]FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. {ECO:0000269|PubMed:21834987}.Q7Z2W4ZCCHV)Zinc finger CCCH-type antiviral protein 1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of viral genome replication [GO:0045071]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of RIG-I signaling pathway [GO:1900246]; positive regulation of type I interferon production [GO:0032481]; regulation of defense response to virus by host [GO:0050691]; response to virus [GO:0009615]; suppression by virus of host molecular function [GO:0039507]smetal ion binding [GO:0046872]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; poly(A) RNA binding [GO:0044822]}cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; nucleus [GO:0005634]PFUNCTION: Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1), moloney and murine leukemia virus (MoMLV) and xenotropic MuLV-related virus (XMRV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs). {ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21102435, ECO:0000269|PubMed:21876179, ECO:0000269|PubMed:22720057}.Q9NRN9METL5 Methyltransferase-like protein 5Q8WTW3COG1,Conserved oligomeric Golgi complex subunit 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:11980916}; Peripheral membrane protein {ECO:0000305|PubMed:11980916}; Cytoplasmic side {ECO:0000305|PubMed:11980916}.tGolgi organization [GO:0007030]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]_Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]Q5VUB5F1711Protein FAM171A1Q9H9B1EHMT1(Histone-lysine N-methyltransferase EHMT1TSUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with euchromatic regions.chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; DNA methylation [GO:0006306]; embryo development [GO:0009790]; histone H3-K27 methylation [GO:0070734]; histone H3-K9 methylation [GO:0051567]; histone methylation [GO:0016571]; negative regulation of transcription, DNA-templated [GO:0045892]; peptidyl-lysine dimethylation [GO:0018027]; peptidyl-lysine monomethylation [GO:0018026]Yhistone-lysine N-methyltransferase activity [GO:0018024]; histone methyltransferase activity (H3-K27 specific) [GO:0046976]; histone methyltransferase activity (H3-K9 specific) [GO:0046974]; methyltransferase activity [GO:0008168]; p53 binding [GO:0002039]; protein-lysine N-methyltransferase activity [GO:0016279]; zinc ion binding [GO:0008270]}chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. {ECO:0000269|PubMed:12004135, E< CO:0000269|PubMed:20118233}.P25686DNJB2!DnaJ homolog subfamily B member 20ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of inclusion body assembly [GO:0090084]; negative regulation of protein deubiquitination [GO:0090086]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; protein folding [GO:0006457]; protein refolding [GO:0042026]; response to unfolded protein [GO:0006986]chaperone binding [GO:0051087]; Hsp70 protein binding [GO:0030544]; polyubiquitin binding [GO:0031593]; proteasome binding [GO:0070628]; unfolded protein binding [GO:0051082]Gcytosol [GO:0005829]; inclusion body [GO:0016234]; nucleus [GO:0005634]Q13595TRA2A#Transformer-2 protein homolog alpha;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9546399}.FUNCTION: Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. {ECO:0000269|PubMed:9546399}.Q6UWY0ARSKArylsulfatase KKendoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]Q9H6E4CC134)Coiled-coil domain-containing protein 134Q92783STAM1%Signal transducing adapter molecule 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.endosomal transport [GO:0016197]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of signal transduction [GO:0009967]; regulation of extracellular exosome assembly [GO:1903551]; signal transduction [GO:0007165]:cytosol [GO:0005829]; early endosome membrane [GO:0031901]6FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes.P48426PI42A6Phosphatidylinositol 5-phosphate 4-kinase type-2 alphaSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20583997}. Cytoplasm {ECO:0000269|PubMed:20583997}. Note=May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light (By similarity). Localization to the nucleus is modulated by the interaction with PIP4K2B. {ECO:0000250}.megakaryocyte development [GO:0035855]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]Hcytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size. {ECO:0000269|PubMed:18364242}.Q9BZE4NOG1Nucleolar GTP-binding protein 1wSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11316846, ECO:0000269|PubMed:12429849, ECO:0000269|Ref.8}.negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of collagen binding [GO:0033342]; negative regulation of DNA replication [GO:0008156]; negative regulation of protein ubiquitination [GO:0031397]; osteoblast differentiation [GO:0001649]; protein stabilization [GO:0050821]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; ribosome biogenesis [GO:0042254]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]QFUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. {ECO:0000250}.Q92633LPAR1 Lysophosphatidic acid receptor 19SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:19306925}. Cell membrane {ECO:0000269|PubMed:19306925}; Multi-pass membrane protein {ECO:0000269|PubMed:19306925}. Note=Prior to LPA treatment found predominantly at the cell surface but in the presence of LPA colocalizes with RALA in the endocytic vesicles.hactivation of MAPK activity [GO:0000187]; activation of phospholipase C activity [GO:0007202]; bleb assembly [GO:0032060]; cellular response to oxygen levels [GO:0071453]; G-protein coupled receptor signaling pathway [GO:0007186]; myelination [GO:0042552]; negative regulation of neuron projection development [GO:0010977]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway [GO:0051482]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of smooth muscle cell chemotaxis [GO:0071673]G-protein coupled receptor activity [GO:0004930]; lysophosphatidic acid receptor activity [GO:0070915]; phospholipid binding [GO:0005543]cell surface [GO:0009986]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]9FUNCTION: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Stimulates phospholipase C (PLC) activity in a manner that is dependent on RALA activation. {ECO:0000269|PubMed:19306925}.Q8TDI8TMC1$Transmembrane channel-like protein 1auditory receptor cell development [GO:0060117]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; vestibular reflex [GO:0060005]3voltage-gated calcium channel activity [GO:0005245]external side of plasma membrane [GO:0009897]; integral component of membrane [GO:0016021]; stereocilium bundle tip [GO:0032426]fFUNCTION: Probable ion channel required for the normal function of cochlear hair cells. {ECO:0000250}.O15541R113ARING finger protein 113AP12236ADT3ADP/ATP translocase 3SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. {ECO:0000250}.active induction of host immune response by virus [GO:0046732]; ADP transport [GO:0015866]; apoptotic process [GO:0006915]; ATP transport [GO:0015867]; cellular protein metabolic process [GO:0044267]; energy reserve me< tabolic process [GO:0006112]; modulation by virus of host morphology or physiology [GO:0019048]; protein targeting to mitochondrion [GO:0006626]; regulation of insulin secretion [GO:0050796]; small molecule metabolic process [GO:0044281]; viral life cycle [GO:0019058]; viral process [GO:0016032](ATP:ADP antiporter activity [GO:0005471]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial inner membrane presequence translocase complex [GO:0005744]; mitochondrion [GO:0005739]; nucleus [GO:0005634]5FUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. {ECO:0000269|PubMed:15033708}.Q9NWS1PARIPCNA-interacting partnerSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20931645, ECO:0000269|PubMed:22153967}. Note=Localizes to chromatin in response to S phase arrest but not in mitosis. Targeted to chromatin via its interaction with PCNA.tDNA repair [GO:0006281]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]Hchromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by interfering with the formation of the RAD51-DNA homologous recombination structure. Binds single-strand DNA and poly(A) homopolymers. Positively regulate the poly(ADP-ribosyl)ation activity of PARP1; however such function may be indirect. {ECO:0000269|PubMed:20931645, ECO:0000269|PubMed:22153967}.Q9Y277VDAC33Voltage-dependent anion-selective channel protein 33SUBCELLULAR LOCATION: Mitochondrion outer membrane.adenine transport [GO:0015853]; regulation of anion transmembrane transport [GO:1903959]; regulation of cilium assembly [GO:1902017]extracellular exosome [GO:0070062]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; pore complex [GO:0046930]FUNCTION: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. {ECO:0000250}.Q04771ACVR1Activin receptor type-1activin receptor signaling pathway [GO:0032924]; acute inflammatory response [GO:0002526]; atrial septum primum morphogenesis [GO:0003289]; BMP signaling pathway [GO:0030509]; cardiac muscle cell fate commitment [GO:0060923]; cellular response to BMP stimulus [GO:0071773]; determination of left/right symmetry [GO:0007368]; embryonic heart tube morphogenesis [GO:0003143]; endocardial cushion cell fate commitment [GO:0061445]; G1/S transition of mitotic cell cycle [GO:0000082]; gastrulation with mouth forming second [GO:0001702]; germ cell development [GO:0007281]; in utero embryonic development [GO:0001701]; mesoderm formation [GO:0001707]; mitral valve morphogenesis [GO:0003183]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of signal transduction [GO:0009968]; neural crest cell migration [GO:0001755]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; patterning of blood vessels [GO:0001569]; peptidyl-threonine phosphorylation [GO:0018107]; pharyngeal system development [GO:0060037]; positive regulation of bone mineralization [GO:0030501]; positive regulation of determination of dorsal identity [GO:2000017]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of ossification [GO:0030278]; smooth muscle cell differentiation [GO:0051145]; transforming growth factor beta receptor signaling pathway [GO:0007179]jactivin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; peptide hormone binding [GO:0017046]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; receptor signaling protein serine/threonine kinase activity [GO:0004702]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]; transmembrane receptor protein serine/threonine kinase activity [GO:0004675]{activin receptor complex [GO:0048179]; apical part of cell [GO:0045177]; integral component of plasma membrane [GO:0005887]FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity). {ECO:0000250}.Q9NQX7ITM2CIntegral membrane protein 2CSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:19114711}; Single-pass type II membrane protein {ECO:0000269|PubMed:19114711}.negative regulation of neuron projection development [GO:0010977]; neuron differentiation [GO:0030182]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238];ATP binding [GO:0005524]; beta-amyloid binding [GO:0001540]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Negative regulator of beta amyloid peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity). {ECO:0000250}.Q6PI78TMM65Transmembrane protein 65Q8N511TM199Transmembrane protein 199Mendomembrane system [GO:0012505]; integral component of membrane [GO:0016021]Q9Y5N5HEMK2&HemK methyltransferase family member 2Qpositive regulation of cell growth [GO:0030307]; protein methylation [GO:0006479]Rnucleic acid binding [GO:0003676]; protein methyltransferase activity [GO:0008276]protein complex [GO:0043234]FUNCTION: Heterodimeric methyltransferase that catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated. May play a role in the modulation of arsenic-induced toxicity. May be involved in the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid. {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:21193388}.Q9NR50EI2BG2Translation initiation factor eIF-2B subunit gammacellular protein metabolic process [GO:0044267]; cellular response to stimulus [GO:0051716]; gene expression [GO:0010467]; negative regulation of translational initiation in response to stress [GO:0032057]; oligodendrocyte development [GO:0014003]; positive regulation of GTPase activity [GO:0043547]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to peptide hormone [GO:0043434]; translation [GO:0006412]; translational initiation [GO:0006413]guanyl-nucleotide exchange factor activity [GO:0005085]; nucleotidyltransferase activity [GO:0016779]; translation initiation factor activity [GO:0003743]ncytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]< Q86TX2ACOT1Acyl-coenzyme A thioesterase 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16940157}.acyl-CoA metabolic process [GO:0006637]; long-chain fatty acid metabolic process [GO:0001676]; very long-chain fatty acid metabolic process [GO:0000038]acyl-CoA hydrolase activity [GO:0047617]; carboxylic ester hydrolase activity [GO:0052689]; palmitoyl-CoA hydrolase activity [GO:0016290]OFUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active towards fatty acyl-CoA with chain-lengths of C12-C16 (By similarity). {ECO:0000250}.O75818RPP40"Ribonuclease P protein subunit p40xFUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.P49746TSP3Thrombospondin-3bone trabecula formation [GO:0060346]; cell-matrix adhesion [GO:0007160]; growth plate cartilage development [GO:0003417]; ossification involved in bone maturation [GO:0043931]Oextracellular region [GO:0005576]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Can bind to fibrinogen, fibronectin, laminin and type V collagen.Q14137BOP1 Ribosome biogenesis protein BOP1SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12429849}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:12429849}.Mcell proliferation [GO:0008283]; cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; regulation of cell cycle [GO:0051726]; ribosome biogenesis [GO:0042254]Ppoly(A) RNA binding [GO:0044822]; ribonucleoprotein complex binding [GO:0043021]nucleoplasm [GO:0005654]; PeBoW complex [GO:0070545]; preribosome, large subunit precursor [GO:0030687]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:17353269}.Q8N8N7PTGR2Prostaglandin reductase 2,prostaglandin metabolic process [GO:0006693]f13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]8FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha with highest activity towards 15-keto-PGE2. Overexpression represses transcriptional activity of PPARG and inhibits adipocyte differentiation (By similarity). {ECO:0000250}.O14936CSKP'Peripheral plasma membrane protein CASKSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.jcalcium ion import [GO:0070509]; cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of wound healing [GO:0061045]; neurotransmitter secretion [GO:0007269]; nucleotide phosphorylation [GO:0046939]; positive regulation of calcium ion import [GO:0090280]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; synaptic transmission [GO:0007268]wATP binding [GO:0005524]; guanylate kinase activity [GO:0004385]; protein serine/threonine kinase activity [GO:0004674]actin cytoskeleton [GO:0015629]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; vesicle [GO:0031982]FUNCTION: Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1.D6RF30GOG8KGolgin subfamily A member 8KO15354GPR37Prosaposin receptor GPR37SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; dopamine biosynthetic process [GO:0042416]; G-protein coupled receptor signaling pathway [GO:0007186]; locomotion involved in locomotory behavior [GO:0031987]; negative regulation of hydrogen peroxide-induced cell death [GO:1903206]; positive regulation of dopamine metabolic process [GO:0045964]; positive regulation of MAPK cascade [GO:0043410]/G-protein coupled peptide receptor activity [GO:0008528]; G-protein coupled receptor activity [GO:0004930]; heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; peptide binding [GO:0042277]; prosaposin receptor activity [GO:0036505]; ubiquitin protein ligase binding [GO:0031625]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ubiquitin ligase complex [GO:0000151]FUNCTION: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade. {ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:9526070}.Q9NZ45CISD1-CDGSH iron-sulfur domain-containing protein 1DSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}; Single-pass type III membrane protein {ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}./regulation of cellular respiration [GO:0043457]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] FUNCTION: Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions. {ECO:0000250, ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766440}.Q96GF1RN185"E3 ubiquitin-protein ligase RNF185SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.autophagy [GO:0006914]; ERAD pathway [GO:0036503]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; protein autoubiquitination [GO:0051865]ligase activity [GO:0016874]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]; ubiquitin protein ligase activity involved in ERAD pathway [GO:1904264]; zinc ion binding [GO:0008270]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]mFUNCTION: E3 ubiquitin-protein ligase that regulates selective mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination of BNIP1. Responsible for the cotranslational ubiquitination and degradation of CFTR in the ERAD pathway. Preferentially associates with the < E2 enzymes UBE2J1 and UBE2J2. {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:24019521}.O00522KRIT1"Krev interaction trapped protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in a ITGB1BP1-dependent manner.angiogenesis [GO:0001525]; cell redox homeostasis [GO:0045454]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of protein binding [GO:0032092]; regulation of catalytic activity [GO:0050790]; regulation of establishment of cell polarity [GO:2000114]; small GTPase mediated signal transduction [GO:0007264]GTPase regulator activity [GO:0030695]; microtubule binding [GO:0008017]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein complex binding [GO:0032403]cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; microtubule [GO:0005874]; plasma membrane [GO:0005886]FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. {ECO:0000250, ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20616044, ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:21633110, ECO:0000269|Ref.20}.P11586C1TC*C-1-tetrahydrofolate synthase, cytoplasmicH10-formyltetrahydrofolate biosynthetic process [GO:0009257]; embryonic neurocranium morphogenesis [GO:0048702]; embryonic viscerocranium morphogenesis [GO:0048703]; folic acid metabolic process [GO:0046655]; heart development [GO:0007507]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; neural tube closure [GO:0001843]; one-carbon metabolic process [GO:0006730]; purine nucleotide biosynthetic process [GO:0006164]; serine family amino acid biosynthetic process [GO:0009070]; serine family amino acid metabolic process [GO:0009069]; small molecule metabolic process [GO:0044281]; somite development [GO:0061053]; tetrahydrofolate interconversion [GO:0035999]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]dATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]; methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity [GO:0004486]Q96RP7G3ST4 Galactose-3-O-sulfotransferase 4cell-cell signaling [GO:0007267]; glycoprotein metabolic process [GO:0009100]; oligosaccharide metabolic process [GO:0009311]; proteoglycan biosynthetic process [GO:0030166]; sulfur compound metabolic process [GO:0006790]3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; galactose 3-O-sulfotransferase activity [GO:0050694]; galactosylceramide sulfotransferase activity [GO:0001733]; proteoglycan sulfotransferase activity [GO:0050698]extracellular exosome [GO:0070062]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Catalyzes the transfer of sulfate to beta-1,3-linked galactose residues in O-linked glycoproteins. Good substrates include asialofetuin, Gal-beta-1,3-GalNAc and Gal-beta-1,3 (GlcNAc-beta-1,6)GalNAc. {ECO:0000269|PubMed:11333265}.Q03426KIMEMevalonate kinase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14730012}.cholesterol biosynthetic process [GO:0006695]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; isoprenoid biosynthetic process [GO:0008299]; negative regulation of inflammatory response [GO:0050728]; small molecule metabolic process [GO:0044281]iATP binding [GO:0005524]; identical protein binding [GO:0042802]; mevalonate kinase activity [GO:0004496]GFUNCTION: May be a regulatory site in cholesterol biosynthetic pathway.Q8NHY6ZFP28Zinc finger protein 28 homologDNA binding [GO:0003677]; metal ion binding [GO:0046872]; sequence-specific DNA binding transcription factor activity [GO:0003700]bFUNCTION: May be involved in transcriptional regulation. May have a role in embryonic development.A6NFQ2F115CProtein FAM115CSUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000269|PubMed:25559186}. Note=Colocalizes with TRPM8 on the plasma membrane. {ECO:0000269|PubMed:25559186}.hematopoietic progenitor cell differentiation [GO:0002244]; negative regulation of anion channel activity [GO:0010360]; positive regulation of cell migration [GO:0030335]; positive regulation of protein targeting to membrane [GO:0090314]; transport [GO:0006810]FUNCTION: Isoform 2: Negatively regulates the plasma membrane cation channel TRPM8 activity. Involved in the recruitment of TRPM8 to the cell surface. Promotes prostate cancer cell migration stimulation in a TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}.Q8WVF5KCTD4'BTB/POZ domain-containing protein KCTD4Q92629SGCDDelta-sarcoglycanoSUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasm, cytoskeleton.cardiac muscle tissue development [GO:0048738]; heart contraction [GO:0060047]; membrane organization [GO:0061024]; muscle cell development [GO:0055001]; muscle organ development [GO:0007517]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystrophin-associated glycoprotein complex [GO:0016010]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; sarcoglycan complex [GO:0016012]; sarcolemma [GO:0042383]Q13952NFYC,Nuclear transcription factor Y subunit gammaprotein folding [GO:0006457]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; small molecule metabolic process [GO:0044281]DNA binding [GO:0003677]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:00037< 13]{CCAAT-binding factor complex [GO:0016602]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.Q9ULP9TBC24TBC1 domain family member 24oSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20727515}. Note=Partially expressed at the plasma membrane.*neuron projection development [GO:0031175]Ycytoplasm [GO:0005737]; neuromuscular junction [GO:0031594]; terminal bouton [GO:0043195]FUNCTION: May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function. {ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:20797691}.Q9NVS9PNPOPyridoxine-5'-phosphate oxidaseactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; positive regulation of defense response to virus by host [GO:0002230]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615]; small molecule metabolic process [GO:0044281]; vitamin B6 metabolic process [GO:0042816]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]NFMN binding [GO:0010181]; pyridoxamine-phosphate oxidase activity [GO:0004733]FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). {ECO:0000269|PubMed:12824491}.P12268IMDH2(Inosine-5'-monophosphate dehydrogenase 2cellular response to interleukin-4 [GO:0071353]; GMP biosynthetic process [GO:0006177]; lymphocyte proliferation [GO:0046651]; nucleobase-containing small molecule metabolic process [GO:0055086]; protein homotetramerization [GO:0051289]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; retina development in camera-type eye [GO:0060041]; small molecule metabolic process [GO:0044281]DNA binding [GO:0003677]; IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]Q9H3H5GPTQUDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferasecellular protein metabolic process [GO:0044267]; dolichol biosynthetic process [GO:0019408]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; protein oligomerization [GO:0051259]; UDP-N-acetylglucosamine metabolic process [GO:0006047]phospho-N-acetylmuramoyl-pentapeptide-transferase activity [GO:0008963]; transferase activity, transferring glycosyl groups [GO:0016757]; UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity [GO:0003975]endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]WFUNCTION: Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.Q9H7B2RPF2$Ribosome production factor 2 homologSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:19170763}. Note=Associated with the nucleolus in an RNA-dependent manner.maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit assembly [GO:0000027]O15228GNPAT*Dihydroxyacetone phosphate acyltransferase Membrane lipid metabolismSUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250}.Dcellular lipid metabolic process [GO:0044255]; cerebellum morphogenesis [GO:0021587]; ether lipid biosynthetic process [GO:0008611]; glycerophospholipid biosynthetic process [GO:0046474]; membrane organization [GO:0061024]; paranodal junction assembly [GO:0030913]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; response to drug [GO:0042493]; response to fatty acid [GO:0070542]; response to nutrient [GO:0007584]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]; synapse assembly [GO:0007416]glycerone-phosphate O-acyltransferase activity [GO:0016287]; palmitoyl-CoA hydrolase activity [GO:0016290]; receptor binding [GO:0005102]membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]Q5SW79CE170Centrosomal protein of 170 kDa)SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15616186}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15616186}. Note=Associated with the mature mother centriole. Associated with spindle microtubules during mitosis.centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; nuclear membrane [GO:0031965]; spindle [GO:0005819]RFUNCTION: Plays a role in microtubule organization. {ECO:0000269|PubMed:15616186}.Q7Z3E5ARMC9$LisH domain-containing protein ARMC9Q96C01F136AProtein FAM136AQ7Z7K0COXM1*COX assembly mitochondrial protein homolog`SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18443040}. Note=Colocalizes with MT-CO1.hFUNCTION: Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. {ECO:0000250}.Q86SQ9DHDDS9Dehydrodolichyl diphosphate syntase complex subunit DHDDSSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14652022}; Peripheral membrane protein {ECO:0000269|PubMed:14652022}. Note=colocalizes with calnexin.cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichyl diphosphate biosynthetic process [GO:0006489]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]Xtransferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765]^FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. {ECO:0000269|PubMed:25066056, ECO:0000303|PubMed:21572394}.Q8IWE5PKHM27Pleckstrin homology domain-containing family M member 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15905402}.PGolgi organization [GO:0007030]; regulation of protein localization [GO:0032880]FUNCTION: May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation. {ECO:0000269|PubMed:15905402}.P51795CLCN5!H(+)/Cl(-) exchange transporter 5\SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}. Endosome membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}. Cell membrane {ECO:0000269|PubMed:19019917}; Multi-pass membrane protein {ECO:0000269|PubMed:19019917}.chloride transmemb< rane transport [GO:1902476]; endocytosis [GO:0006897]; excretion [GO:0007588]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]; transport [GO:0006810]antiporter activity [GO:0015297]; ATP binding [GO:0005524]; chloride channel activity [GO:0005254]; voltage-gated chloride channel activity [GO:0005247]apical part of cell [GO:0045177]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. Important for normal acidification of the endosome lumen. May play an important role in renal tubular function.Q9H0U3MAGT1Magnesium transporter protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19717468}; Multi-pass membrane protein {ECO:0000269|PubMed:19717468}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.2cellular protein metabolic process [GO:0044267]; cognition [GO:0050890]; magnesium ion transport [GO:0015693]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; transmembrane transport [GO:0055085]integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; oligosaccharyltransferase complex [GO:0008250]; plasma membrane [GO:0005886]FUNCTION: May be involved in N-glycosylation through its association with N-oligosaccharyl transferase. May be involved in Mg(2+) transport in epithelial cells. {ECO:0000269|PubMed:15804357, ECO:0000269|PubMed:19717468}.Q13951PEBB Core-binding factor subunit betavcell maturation [GO:0048469]; definitive hemopoiesis [GO:0060216]; lymphocyte differentiation [GO:0030098]; myeloid cell differentiation [GO:0030099]; osteoblast differentiation [GO:0001649]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein polyubiquitination [GO:0000209]; transcription from RNA polymerase II promoter [GO:0006366]DNA binding [GO:0003677]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBFB enhances DNA binding by RUNX1.P33121ACSL1#Long-chain-fatty-acid--CoA ligase 15adiponectin-activated signaling pathway [GO:0033211]; alpha-linolenic acid metabolic process [GO:0036109]; cellular lipid metabolic process [GO:0044255]; linoleic acid metabolic process [GO:0043651]; lipid biosynthetic process [GO:0008610]; long-chain fatty acid import [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; response to drug [GO:0042493]; response to nutrient [GO:0007584]; response to oleic acid [GO:0034201]; response to organic cyclic compound [GO:0014070]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; unsaturated fatty acid metabolic process [GO:0033559]; xenobiotic catabolic process [GO:0042178]PATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886]FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate.Q9UHD8Septin-9SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:17922164}. Note=In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes partly with actin stress fibers. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria._cell cycle [GO:0007049]; cell division [GO:0051301]; protein heterooligomerization [GO:0051291]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471]; stress fiber [GO:0001725]FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. {ECO:0000250, ECO:0000305}.Q8N111CEND6Cell cycle exit and neuronal differentiation protein 1(adult walking behavior [GO:0007628]; cerebellar granular layer maturation [GO:0021686]; cerebellar Purkinje cell differentiation [GO:0021702]; negative regulation of cerebellar granule cell precursor proliferation [GO:0021941]; radial glia guided migration of cerebellar granule cell [GO:0021933]HFUNCTION: Involved in neuroblastoma cell differentiation. {ECO:0000250}.P10109ADXAdrenodoxin, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:20547883}._C21-steroid hormone biosynthetic process [GO:0006700]; cholesterol metabolic process [GO:0008203]; hormone biosynthetic process [GO:0042446]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]; sterol metabolic process [GO:0016125]; xenobiotic metabolic process [GO:0006805]t2 iron, 2 sulfur cluster binding [GO:0051537]; electron carrier activity [GO:0009055]; iron ion binding [GO:0005506]FUNCTION: Participates in the synthesis of thyroid hormones. Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. {ECO:0000269|PubMed:20547883, ECO:0000269|PubMed:21636783}.Q2TB10ZN800Zinc finger protein 800Q9NUP1BL1S4=Biogenesis of lysosome-related organelles complex 1 subunit 4anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; intracellular transport [GO:0046907]; melanosome organization [GO:0032438]; membrane organization [GO:0061024]; neuromuscular process controlling balance [GO:0050885]; neuron projection development [GO:0031175]; platelet aggregation [GO:0070527]; post-Golgi vesicle-mediated transport [GO:0006892]IBLOC-1 complex [GO:0031083]; cytoplasm [GO:0005737]; cytosol [GO:0005829]Q9H6V9CB043UPF0554 protein C2orf43"SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:17135363}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8BVA5}. Note=Localizes to the endoplasmic reticulum in absence of lipid droplets and translocates to lipid droplets upon lipid storage induction. {ECO:0000250|UniProtKB:Q8BVA5}.@lipid catabolic process [GO:0016042]; lipid storage [GO:0019915]lipase activity [GO:0016298]?endoplasmic reticulum [GO:0005783]; lipid particle [GO:0005811]FUNCTION: Serine lipid hydrolase associated with lipid droplets. Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages. {ECO:0000250|UniProtKB:Q8BVA5}.Q14324MYPC2#Myosin-binding protein C, fast-type@cell adhesion [GO:0007155]; muscle filament sliding [GO:0030049]-structural constituent of muscle [GO:0008307]2cytosol [GO:0005829]; myosin filament [GO:0032982]1FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.Q96CV9< OPTN OptineurinSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle. Recycling endosome. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy.+cell death [GO:0008219]; cytokine secretion [GO:0050663]; defense response to Gram-negative bacterium [GO:0050829]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; Golgi to plasma membrane protein transport [GO:0043001]; macroautophagy [GO:0016236]; mitotic cell cycle [GO:0000278]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of receptor recycling [GO:0001920]; positive regulation of cell proliferation [GO:0008284]; protein homooligomerization [GO:0051260]; protein targeting to Golgi [GO:0000042]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; signal transduction [GO:0007165]; wound healing [GO:0042060]identical protein binding [GO:0042802]; K63-linked polyubiquitin binding [GO:0070530]; polyubiquitin binding [GO:0031593]; protein binding, bridging [GO:0030674]; protein C-terminus binding [GO:0008022]; Rab GTPase binding [GO:0017137]Wautophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]FUNCTION: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as of transferrin receptor (TFRC/TfR); regulates Rab8 recruitnment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52. May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death. {ECO:0000269|PubMed:11834836, ECO:0000269|PubMed:15837803, ECO:0000269|PubMed:20085643, ECO:0000269|PubMed:20174559, ECO:0000269|PubMed:21617041, ECO:0000269|PubMed:22854040}.Q7Z4F1LRP103Low-density lipoprotein receptor-related protein 10SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}.endocytosis [GO:0006897][coated pit [GO:0005905]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver (By similarity). {ECO:0000250}.P08123CO1A2Collagen alpha-2(I) chainblood coagulation [GO:0007596]; blood vessel development [GO:0001568]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; leukocyte migration [GO:0050900]; odontogenesis [GO:0042476]; platelet activation [GO:0030168]; protein heterotrimerization [GO:0070208]; receptor-mediated endocytosis [GO:0006898]; regulation of blood pressure [GO:0008217]; Rho protein signal transduction [GO:0007266]; skeletal system development [GO:0001501]; skin morphogenesis [GO:0043589]; transforming growth factor beta receptor signaling pathway [GO:0007179]extracellular matrix structural constituent [GO:0005201]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protein binding, bridging [GO:0030674]collagen type I trimer [GO:0005584]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]WFUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).P45954ACDSBCShort/branched chain specific acyl-CoA dehydrogenase, mitochondrial2branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty acid metabolic process [GO:0006631]; lipid homeostasis [GO:0055088]; small molecule metabolic process [GO:0044281]FUNCTION: Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.Q12906ILF3%Interleukin enhancer-binding factor 3SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus. Note=Localizes in the cytoplasm in response to viral dsRNA. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.jdefense response to virus [GO:0051607]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of translation [GO:0017148]; negative regulation of viral genome replication [GO:0045071]; positive regulation of transcription, DNA-templated [GO:0045893]; protein phosphorylation [GO:0006468]; transcription, DNA-templated [GO:0006351]~DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication (By similarity). {ECO:0000250}.Q8IZA0K319L1Dyslexia-associated protein KIAA0319-like proteinlSUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.qcytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]gFUNCTION: Possible role in axon guidance through in< teraction with RTN4R. {ECO:0000269|PubMed:20697954}.O60447EVI52Ecotropic viral integration site 5 protein homolog SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis.cell cycle [GO:0007049]; cell division [GO:0051301]; cell proliferation [GO:0008283]; multicellular organismal development [GO:0007275]; positive regulation of GTPase activity [GO:0043547]; retrograde transport, endosome to Golgi [GO:0042147]cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis. {ECO:0000269|PubMed:16439210}.Q96BZ8LENG1#Leukocyte receptor cluster member 1Q9NZM3ITSN2 Intersectin-2endocytosis [GO:0006897]; positive regulation of dendrite extension [GO:1903861]; positive regulation of signal transduction [GO:0009967]; regulation of Rho protein signal transduction [GO:0035023]calcium ion binding [GO:0005509]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]; SH3/SH2 adaptor activity [GO:0005070]Scentrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). {ECO:0000269|PubMed:19458185, ECO:0000269|PubMed:22648170}.P17987TCPA!T-complex protein 1 subunit alphadSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.de novo' posttranslational protein folding [GO:0051084]; binding of sperm to zona pellucida [GO:0007339]; cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]; regulation of macrophage apoptotic process [GO:2000109]; toxin transport [GO:1901998]; translocation of peptides or proteins into host cell cytoplasm [GO:0044053]; tubulin complex assembly [GO:0007021]acrosomal vesicle [GO:0001669]; cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; nuclear heterochromatin [GO:0005720]; pericentriolar material [GO:0000242]; zona pellucida receptor complex [GO:0002199]QFUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. {ECO:0000269|PubMed:20080638}.Q9BSB4ATGA1Autophagy-related protein 101ULK/ATGSSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19597335}. Preautophagosomal structure {ECO:0000269|PubMed:19597335}. Note=Under starvation conditions, it is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation.#autophagosome assembly [GO:0000045])pre-autophagosomal structure [GO:0000407]FUNCTION: Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation. {ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:19597335}.P60468SC61B,Protein transport protein Sec61 subunit betaSSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein.antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; gene expression [GO:0010467]; IRE1-mediated unfolded protein response [GO:0036498]; protein import into nucleus, translocation [GO:0000060]; retrograde protein transport, ER to cytosol [GO:0030970]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]mepidermal growth factor binding [GO:0048408]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum Sec complex [GO:0031205]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; Sec61 translocon complex [GO:0005784]KFUNCTION: Necessary for protein translocation in the endoplasmic reticulum.O95081AGFG21Arf-GAP domain and FG repeat-containing protein 2Q9UJ70NAGKN-acetyl-D-glucosamine kinasecarbohydrate phosphorylation [GO:0046835]; N-acetylglucosamine metabolic process [GO:0006044]; N-acetylmannosamine metabolic process [GO:0006051]; N-acetylneuraminate catabolic process [GO:0019262]zATP binding [GO:0005524]; N-acetylglucosamine kinase activity [GO:0045127]; N-acylmannosamine kinase activity [GO:0009384]FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity. {ECO:0000269|PubMed:22692205}.Q9BQ61CS043 Uncharacterized protein C19orf43Q9H5N1RABE2%Rab GTPase-binding effector protein 2jSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9524116}. Early endosome {ECO:0000269|PubMed:9524116}.jcytoplasm [GO:0005737]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]tFUNCTION: Plays a role in membrane trafficking and in homotypic early endosome fusion. {ECO:0000269|PubMed:9524116}.Q92793CBPCREB-binding proteinSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence of ALX1 relocalizes from the cytoplasm to the nucleus.cell proliferation [GO:0008283]; cellular lipid metabolic process [GO:0044255]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to UV [GO:0034644]; chromatin organization [GO:0006325]; embryonic digit morphogenesis [GO:0042733]; gene expression [GO:0010467]; germ-line stem cell maintenance [GO:0030718]; histone acetylation [GO:0016573]; homeostatic process [GO:0042592]; innate immune response [GO:0045087]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; N-terminal peptidyl-lysine acetylation [GO:0018076]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of type I interferon production [GO:0032481]; protein acetylation [GO:0006473]; protein complex assembly [GO:0006461]; regulation of cellular response to heat [GO:1900034]; regulation of smoothened signaling pathway [GO:0008589]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; rhythmic process [GO:0048511]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; stimulatory C-< type lectin receptor signaling pathway [GO:0002223]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]acetyltransferase activity [GO:0016407]; chromatin binding [GO:0003682]; core promoter proximal region sequence-specific DNA binding [GO:0000987]; damaged DNA binding [GO:0003684]; histone acetyltransferase activity [GO:0004402]; MRF binding [GO:0043426]; p53 binding [GO:0002039]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription coactivator activity [GO:0001105]; RNA polymerase II transcription factor binding [GO:0001085]; RNA polymerase II transcription factor binding transcription repressor activity [GO:0001191]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]condensed chromosome outer kinetochore [GO:0000940]; cytoplasm [GO:0005737]; histone acetyltransferase complex [GO:0000123]; nuclear body [GO:0016604]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). {ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12929931, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:9707565}.Q9H0N5PHS2*Pterin-4-alpha-carbinolamine dehydratase 2positive regulation of transcription, DNA-templated [GO:0045893]; protein heterooligomerization [GO:0051291]; protein homotetramerization [GO:0051289]; tetrahydrobiopterin biosynthetic process [GO:0006729]y4-alpha-hydroxytetrahydrobiopterin dehydratase activity [GO:0008124]; phenylalanine 4-monooxygenase activity [GO:0004505]IFUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity). {ECO:0000250}.; FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. {ECO:0000269|PubMed:11980910}.Q17RN3FA98CProtein FAM98C)tRNA-splicing ligase complex [GO:0072669]Q8N5M4TTC9C#Tetratricopeptide repeat protein 9CQ6UWP2DHR11,Dehydrogenase/reductase SDR family member 11Q08945SSRP1FACT complex subunit SSRP1SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; gene expression [GO:0010467]; positive regulation of viral transcription [GO:0050434]; regulation of transcription, DNA-templated [GO:0006355]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]wchromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63. {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}.Q9NP58ABCB69ATP-binding cassette sub-family B member 6, mitochondrialSUBCELLULAR LOCATION: Cell membrane. Mitochondrion outer membrane; Multi-pass membrane protein. Endoplasmic reticulum. Golgi apparatus. Endosome {ECO:0000250}. Note=localized to the endosome-like compartement and dendrite tips.brain development [GO:0007420]; cellular iron ion homeostasis [GO:0006879]; heme transport [GO:0015886]; porphyrin-containing compound biosynthetic process [GO:0006779]; skin development [GO:0043588]; transmembrane transport [GO:0055085]; transport [GO:0006810]ATP binding [GO:0005524]; efflux transmembrane transporter activity [GO:0015562]; heme binding [GO:0020037]; heme transporter activity [GO:0015232]; heme-transporting ATPase activity [GO:0015439]ATP-binding cassette (ABC) transporter complex [GO:0043190]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of mitochondrial outer membrane [GO:0031307]; mitochondrial envelope [GO:0005740]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. {ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:17006453}.Q9BV79MECR*Trans-2-enoyl-CoA reductase, mitochondrialSUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:12654921}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:25031892}. Nucleus {ECO:0000269|PubMed:25031892}.Wfatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]Xtrans-2-enoyl-CoA reductase (NADPH) activity [GO:0019166]; zinc ion binding [GO:0008270] FUNCTION: Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. {ECO:0000269|PubMed:18479707}.Q8TCT9HM13$Minor histocompatibility antigen H13SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000250|UniProtKB:Q9D8V0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D8V0}.membrane protein proteolysis [GO:0033619]; membrane protein proteolysis involved in retrograde protein transport, ER to cytosol [GO:1904211]; protein homotetramerization [GO:0051289]aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; peptidase activity < [GO:0008233]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]scell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of cytoplasmic side of endoplasmic reticulum membrane [GO:0071458]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; membrane [GO:0016020]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides (PubMed:11714810). May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein (PubMed:12145199). Involved in the intramembrane cleavage of the integral membrane protein PSEN1 (PubMed:12077416, PubMed:11714810, PubMed:14741365). Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (PubMed:25239945). May play a role in graft rejection (By similarity). {ECO:0000250|UniProtKB:Q9D8V0, ECO:0000269|PubMed:11714810, ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:12145199, ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:25239945}.Q13546RIPK16Receptor-interacting serine/threonine-protein kinase 1=SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of JUN kinase activity [GO:0007257]; amyloid fibril formation [GO:1990000]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular protein catabolic process [GO:0044257]; cellular response to growth factor stimulus [GO:0071363]; cellular response to tumor necrosis factor [GO:0071356]; death-inducing signaling complex assembly [GO:0071550]; extrinsic apoptotic signaling pathway [GO:0097191]; innate immune response [GO:0045087]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; necroptotic signaling pathway [GO:0097527]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; peptidyl-serine autophosphorylation [GO:0036289]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of necroptotic process [GO:0060545]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of programmed cell death [GO:0043068]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I interferon production [GO:0032481]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein autophosphorylation [GO:0046777]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; regulation of ATP:ADP antiporter activity [GO:0070926]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of necrotic cell death [GO:0010939]; response to tumor necrosis factor [GO:0034612]; ripoptosome assembly [GO:0097343]; ripoptosome assembly involved in necroptotic process [GO:1901026]; T cell apoptotic process [GO:0070231]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; tumor necrosis factor-mediated signaling pathway [GO:0033209]:ATP binding [GO:0005524]; death domain binding [GO:0070513]; death receptor binding [GO:0005123]; identical protein binding [GO:0042802]; protein complex binding [GO:0032403]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; death-inducing signaling complex [GO:0031264]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; receptor complex [GO:0043235]; ripoptosome [GO:0097342]FUNCTION: Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex. {ECO:0000269|PubMed:11101870, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:19524512, ECO:0000269|PubMed:19524513}.Q10570CPSF19Cleavage and polyadenylation specificity factor subunit 1gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; pre-mRNA cleavage required for polyadenylation [GO:0098789]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Lenzyme binding [GO:0019899]; mRNA 3'-UTR AU-rich region binding [GO:0035925]cmRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction. {ECO:0000269|PubMed:14749727}.Q92845KIFA3Kinesin-associated protein 3antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; membrane organization [GO:0061024]; microtubule-based movement [GO:0007018]; microtubule-based process [GO:0007017]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; organelle organization [GO:0006996]; plus-end-directed vesicle transport along microtubule [GO:0072383]; positive regulation of calcium-dependent cell-cell adhesion [GO:0046587]; protein complex assembly [GO:0006461]; protein localization [GO:0008104]; signal transduction [GO:0007165]axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; condense< d nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intraciliary transport particle [GO:0030990]; kinesin II complex [GO:0016939]; microtubule cytoskeleton [GO:0015630]; periciliary membrane compartment [GO:1990075]; photoreceptor connecting cilium [GO:0032391]; primary cilium [GO:0072372]FUNCTION: Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity). {ECO:0000250}.Q7Z392TPC11/Trafficking protein particle complex subunit 11GSUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.FUNCTION: Involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000269|PubMed:21525244}.O75179ANR17+Ankyrin repeat domain-containing protein 17USUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:22328336}. Nucleus {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336}. Note=Detected around the nucleolus. Localized on chromatin in a cell cycle-dependent manner. {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984}.Cblood vessel maturation [GO:0001955]; defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; negative regulation of smooth muscle cell differentiation [GO:0051151]; positive regulation of cell cycle [GO:0045787]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of MDA-5 signaling pathway [GO:1900245]; positive regulation of RIG-I signaling pathway [GO:1900246]; regulation of DNA replication [GO:0006275]; viral process [GO:0016032][chromatin [GO:0000785]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Could play pivotal roles in cell cycle and DNA regulation (PubMed:19150984). Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too (PubMed:23711367). Target of enterovirus 71 which is the major etiological agent of HFMD (hand, foot and mouth disease) (PubMed:17276651). Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}.P38435VKGC%Vitamin K-dependent gamma-carboxylaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10910912}; Multi-pass membrane protein {ECO:0000269|PubMed:10910912}.blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; peptidyl-glutamic acid carboxylation [GO:0017187]; post-translational protein modification [GO:0043687]0gamma-glutamyl carboxylase activity [GO:0008488] FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. {ECO:0000269|PubMed:17073445}.Q8TC07TBC15TBC1 domain family member 15_positive regulation of GTPase activity [GO:0043547]; regulation of GTPase activity [GO:0043087]{FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity). {ECO:0000250}.Q587I9SFT2CVesicle transport protein SFT2CFUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}.P29692EF1DElongation factor 1-deltaGSUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:21597468}.cellular protein metabolic process [GO:0044267]; cellular response to ionizing radiation [GO:0071479]; gene expression [GO:0010467]; mRNA transcription [GO:0009299]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; regulation of cell death [GO:0010941]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; translational elongation [GO:0006414] activating transcription factor binding [GO:0033613]; DNA binding [GO:0003677]; heat shock protein binding [GO:0031072]; signal transducer activity [GO:0004871]; translation elongation factor activity [GO:0003746]; translation factor activity, RNA binding [GO:0008135]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic translation elongation factor 1 complex [GO:0005853]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; FUNCTION: Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).Q09161NCBP1%Nuclear cap-binding protein subunit 17-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of viral transcription [GO:0050434]; pre-mRNA cleavage required for polyadenylation [GO:0098789]; regulation of translational initiation [GO:0006446]; RNA splicing [GO:0008380]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Xpoly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; mRNA cap binding complex [GO:0005845]; nuclear cap binding complex [GO:0005846]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell prol< iferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:12093754, ECO:0000269|PubMed:15059963, ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:16186820, ECO:0000269|PubMed:16317009, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182, ECO:0000269|PubMed:19648179, ECO:0000269|PubMed:7651522, ECO:0000269|PubMed:8069914}.Q92797SYMPK SymplekinXSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, tight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Nucleus, nucleoplasm. Note=Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in cells without TJ). Nuclear bodies of heat-stressed cells.|cell adhesion [GO:0007155]; mRNA polyadenylation [GO:0006378]; positive regulation of protein dephosphorylation [GO:0035307]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity. {ECO:0000269|PubMed:16230528, ECO:0000269|PubMed:20861839}.Q5VYS8TUT7Terminal uridylyltransferase 7>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25480299}."RNA 3'-end processing [GO:0031123]npoly(A) RNA binding [GO:0044822]; RNA uridylyltransferase activity [GO:0050265]; zinc ion binding [GO:0008270]]FUNCTION: Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:19703396, PubMed:25480299). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299). Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult. {ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:25480299}.Q03154ACY1Aminoacylase-1cellular amino acid metabolic process [GO:0006520]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]jaminoacylase activity [GO:0004046]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). {ECO:0000269|PubMed:12933810}.Q96T60PNKP.Bifunctional polynucleotide phosphatase/kinase<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10446193}. base-excision repair [GO:0006284]; dephosphorylation [GO:0016311]; DNA 3' dephosphorylation involved in DNA repair [GO:0098504]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide phosphorylation [GO:0046939]; polynucleotide 3' dephosphorylation [GO:0098506]; response to oxidative stress [GO:0006979]; response to radiation [GO:0009314]^ATP binding [GO:0005524]; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity [GO:0046404]; damaged DNA binding [GO:0003684]; double-stranded DNA binding [GO:0003690]; endonuclease activity [GO:0004519]; nucleotide kinase activity [GO:0019201]; polynucleotide 3'-phosphatase activity [GO:0046403]; purine nucleotide binding [GO:0017076]FUNCTION: Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. {ECO:0000269|PubMed:10446192}.Q96ME7ZN512Zinc finger protein 512Q4G176ACSF32Acyl-CoA synthetase family member 3, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21841779}.fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; malonate catabolic process [GO:0090410]oacid-thiol ligase activity [GO:0016878]; ATP binding [GO:0005524]; malonyl-CoA synthetase activity [GO:0090409]-FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates. {ECO:0000269|PubMed:17762044, ECO:0000269|PubMed:21841779}.Q8IVL0NAV3Neuron navigator 3;SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}.#nuclear outer membrane [GO:0005640]xFUNCTION: May regulate IL2 production by T-cells. May be involved in neuron regeneration. {ECO:0000269|PubMed:16166283}.Q8WWC4CB047.Uncharacterized protein C2orf47, mitochondrialQ9Y5B9SP16HFACT complex subunit SPT16SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10421373}. Chromosome {ECO:0000269|PubMed:10421373}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.DNA repair [GO:0006281]; DNA replication [GO:0006260]; gene expression [GO:0010467]; nucleosome disassembly [GO:0006337]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of viral transcription [GO:0050434]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Gchromosome [GO:0005694]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). {ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12934006, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704, ECO:0000269|PubMed:9836642}.P28370SMCA1.Probable global transcription activator SNF2L1*ATP-dependent chromatin remodeling [GO:0043044]; brain development [GO:0007420]; chromatin remodeling [GO:0006338]; DNA strand renaturation [GO:0000733]; neuron differentiation [GO:0030182]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]annealing helicase activity [GO:0036310]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004< 386]JCERF complex [GO:0090537]; nucleus [GO:0005634]; NURF complex [GO:0016589]FUNCTION: Energy-transducing component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes. Both complexes facilitate the perturbation of chromatin structure in an ATP-dependent manner. Potentiates neurite outgrowth. May be involved in brain development by regulating En-1 and En-2 expression. May be involved in the development of luteal cells. {ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:16740656}.Q9NP66HM20AHigh mobility group protein 20AESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.9chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Plays a role in neuronal differentiation as chromatin-associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4 (By similarity). {ECO:0000250}.P63096GNAI17Guanine nucleotide-binding protein G(i) subunit alpha-1SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Note=Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane (By similarity). Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. {ECO:0000250}.adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; blood coagulation [GO:0007596]; cell cycle [GO:0007049]; cell division [GO:0051301]; G-protein coupled receptor signaling pathway [GO:0007186]; negative regulation of synaptic transmission [GO:0050805]; platelet activation [GO:0030168]; response to peptide hormone [GO:0043434]; synaptic transmission [GO:0007268]GDP binding [GO:0019003]; G-protein beta/gamma-subunit complex binding [GO:0031683]; G-protein coupled serotonin receptor binding [GO:0031821]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871] centrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]$FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division. {ECO:0000269|PubMed:17264214, ECO:0000269|PubMed:17635935}.Q2TAL8QRIC1Glutamine-rich protein 1Q6ZN55ZN574Zinc finger protein 574Q9BZK7TBL1R/F-box-like/WD repeat-containing protein TBL1XR1 N-CoR_SMRTcanonical Wnt signaling pathway [GO:0060070]; cellular lipid metabolic process [GO:0044255]; chromatin organization [GO:0006325]; fat pad development [GO:0060613]; histone deacetylation [GO:0016575]; lipid catabolic process [GO:0016042]; multicellular organism growth [GO:0035264]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cAMP metabolic process [GO:0030814]; regulation of triglyceride metabolic process [GO:0090207]; response to dietary excess [GO:0002021]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; white fat cell differentiation [GO:0050872]beta-catenin binding [GO:0008013]; histone binding [GO:0042393]; protein N-terminus binding [GO:0047485]; transcription corepressor activity [GO:0003714]; transcription regulatory region DNA binding [GO:0044212]nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; transcriptional repressor complex [GO:0017053] FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of the N-Cor corepressor complex that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of N-Cor complex, thereby allowing cofactor exchange, and transcription activation. {ECO:0000269|PubMed:14980219}.P42858HD HuntingtinSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The mutant Huntingtin protein colocalizes with AKAP8L in the nuclear matrix of Huntington disease neurons. Shuttles between cytoplasm and nucleus in a Ran GTPase-independent manner.anterior/posterior pattern specification [GO:0009952]; axon cargo transport [GO:0008088]; cell aging [GO:0007569]; citrulline metabolic process [GO:0000052]; determination of adult lifespan [GO:0008340]; dopamine receptor signaling pathway [GO:0007212]; endoplasmic reticulum organization [GO:0007029]; endosomal transport [GO:0016197]; ER to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; grooming behavior [GO:0007625]; hormone metabolic process [GO:0042445]; insulin secretion [GO:0030073]; iron ion homeostasis [GO:0055072]; lactate biosynthetic process from pyruvate [GO:0019244]; L-glutamate import [GO:0051938]; locomotory behavior [GO:0007626]; mRNA transport [GO:0051028]; negative regulation of cysteine-type endopeptidase activity [GO:2000117]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; neural plate formation [GO:0021990]; neuron apoptotic process [GO:0051402]; neuron development [GO:0048666]; olfactory lobe development [GO:0021988]; organ development [GO:0048513]; paraxial mesoderm formation [GO:0048341]; positive regulation of cilium assembly [GO:0045724]; positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0031587]; protein import into nucleus [GO:0006606]; quinolinate biosynthetic process [GO:0019805]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of protein phosphatase type 2A activity [GO:0034047]; regulation of synaptic plasticity [GO:0048167]; response to calcium ion [GO:0051592]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; social behavior [GO:0035176]; spermatogenesis [GO:0007283]; striatum development [GO:0021756]; urea cycle [GO:0000050]; vesicle transport along microtubule [GO:0047496]; visual learning [GO:0008542]=beta-tubulin binding [GO:0048487]; diazepam binding [GO:0050809]; dynactin binding [GO:0034452]; dynein intermediate chain binding [GO:0045505]; identical protein binding [GO:0042802]; ion channel binding [GO:0044325]; p53 binding [GO:0002039]; profili< n binding [GO:0005522]; transcription factor binding [GO:0008134]5autophagosome [GO:0005776]; axon [GO:0030424]; centriole [GO:0005814]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; late endosome [GO:0005770]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; protein complex [GO:0043234]PFUNCTION: May play a role in microtubule-mediated transport or vesicle function.Q9P2K8E2AK49Eukaryotic translation initiation factor 2-alpha kinase 4Icellular response to starvation [GO:0009267]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of translation [GO:0017148]; protein phosphorylation [GO:0006468]; regulation of translational initiation [GO:0006446]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine/threonine kinase activity [GO:0004674]cytosolic ribosome [GO:0022626]kFUNCTION: Can phosphorylate the alpha subunit of EIF2 and may mediate translational control. {ECO:0000250}.O75586MED65Mediator of RNA polymerase II transcription subunit 6gene expression [GO:0010467]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription initiation from RNA polymerase II promoter [GO:0006367]RNA polymerase II transcription cofactor activity [GO:0001104]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]dmediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]'FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:16595664}.Q9Y5G0PCDGHProtocadherin gamma-B5Lhomophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]mextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.O75643U5203U5 small nuclear ribonucleoprotein 200 kDa helicase;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9539711}.cis assembly of pre-catalytic spliceosome [GO:0000354]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; ATP-dependent helicase activity [GO:0008026]; ATP-dependent RNA helicase activity [GO:0004004]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U5 snRNP [GO:0005682]FUNCTION: RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711}.O60264SMCA5]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5bSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:12434153}.7ATP-dependent chromatin remodeling [GO:0043044]; CENP-A containing nucleosome assembly [GO:0034080]; chromatin remodeling [GO:0006338]; chromatin silencing at rDNA [GO:0000183]; DNA-templated transcription, initiation [GO:0006352]; double-strand break repair [GO:0006302]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleosome assembly [GO:0006334]; nucleosome positioning [GO:0016584]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription from RNA polymerase II promoter [GO:0006357]pATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]chromatin silencing complex [GO:0005677]; condensed chromosome [GO:0000793]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NURF complex [GO:0016589]; RSF complex [GO:0031213]FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity. Complexes containing SMARCA5 are capable of forming ordered nucleosome arrays on chromatin; this may require intact histone H4 tails. Also required for replication of pericentric heterochromatin in S-phase specifically in conjunction with BAZ1A. Probably plays a role in repression of polI dependent transcription of the rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. {ECO:0000269|PubMed:10880450, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198550, ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771}.Q6I9Y2THOC7THO complex subunit 7 homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12951069}. Nucleus {ECO:0000269|PubMed:12951069, ECO:0000269|PubMed:19059247}. Nucleus speckle {ECO:0000305}. Note=Interaction with THOC5 is required for nuclear localization. {ECO:0000269|PubMed:19059247}.mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]; viral mRNA export from host cell nucleus [GO:0046784]FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:23222130}.; FUNCTION: The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:18974867}.O00170AIPAH receptor-interacting protein9negative regulation of cyclic-nucleotide phosphodiesterase act< ivity [GO:0051344]; protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]; regulation of protein kinase A signaling [GO:0010738]; signal transduction [GO:0007165]; xenobiotic metabolic process [GO:0006805]GAF domain binding [GO:0036004]; signal transducer activity [GO:0004871]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; unfolded protein binding [GO:0051082]aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.; FUNCTION: Cellular negative regulator of the hepatitis B virus (HBV) X protein.P07996TSP1Thrombospondin-1`SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}.activation of MAPK activity [GO:0000187]; behavioral response to pain [GO:0048266]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell cycle arrest [GO:0007050]; cell migration [GO:0016477]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; cellular response to nitric oxide [GO:0071732]; chronic inflammatory response [GO:0002544]; endocardial cushion development [GO:0003197]; engulfment of apoptotic cell [GO:0043652]; extracellular matrix organization [GO:0030198]; growth plate cartilage development [GO:0003417]; immune response [GO:0006955]; inflammatory response [GO:0006954]; negative regulation of angiogenesis [GO:0016525]; negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II [GO:0002581]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of dendritic cell antigen processing and presentation [GO:0002605]; negative regulation of endothelial cell chemotaxis [GO:2001027]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of nitric oxide mediated signal transduction [GO:0010751]; negative regulation of plasma membrane long-chain fatty acid transport [GO:0010748]; negative regulation of plasminogen activation [GO:0010757]; outflow tract morphogenesis [GO:0003151]; peptide cross-linking [GO:0018149]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood coagulation [GO:0030194]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of chemotaxis [GO:0050921]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of macrophage activation [GO:0043032]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of transforming growth factor beta1 production [GO:0032914]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of translation [GO:0045727]; positive regulation of tumor necrosis factor biosynthetic process [GO:0042535]; post-translational protein modification [GO:0043687]; protein O-linked fucosylation [GO:0036066]; protein O-linked glycosylation [GO:0006493]; regulation of cGMP metabolic process [GO:0030823]; response to calcium ion [GO:0051592]; response to drug [GO:0042493]; response to endoplasmic reticulum stress [GO:0034976]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; response to magnesium ion [GO:0032026]; response to progesterone [GO:0032570]; response to unfolded protein [GO:0006986]; sprouting angiogenesis [GO:0002040]calcium ion binding [GO:0005509]; collagen V binding [GO:0070052]; fibrinogen binding [GO:0070051]; fibroblast growth factor binding [GO:0017134]; fibronectin binding [GO:0001968]; glycoprotein binding [GO:0001948]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; low-density lipoprotein particle binding [GO:0030169]; phosphatidylserine binding [GO:0001786]; proteoglycan binding [GO:0043394]; transforming growth factor beta binding [GO:0050431]cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]; sarcoplasmic reticulum [GO:0016529]; secretory granule [GO:0030141]FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp (By similarity). Ligand for CD36 mediating antiangiogenic properties. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors (By similarity). {ECO:0000250}.P19367HXK1 Hexokinase-1SUBCELLULAR LOCATION: Mitochondrion outer membrane. Note=Its hydrophobic N-terminal sequence may be involved in membrane binding.canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; cellular glucose homeostasis [GO:0001678]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glucose transport [GO:0015758]; glycolytic process [GO:0006096]; hexose transport [GO:0008645]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; mannokinase activity [GO:0019158]cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; sperm principal piece [GO:0097228]Q9H7D0DOCK5"Dedicator of cytokinesis protein 5kpositive regulation of GTPase activity [GO:0043547]; small GTPase mediated signal transduction [GO:0007264]FUNCTION: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP.Q04941PLP2Proteolipid protein 2chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; ion transmembrane transport [GO:0034220]; ion transport [GO:0006811]Schemokine binding [GO:0019956]; ion transmembrane transporter activity [GO:0015075]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]OFUNCTION: May play a role in cell differentiation in the intestinal epithelium.< Q96GC9VMP1Vacuole membrane protein 1uSUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17724469}; Multi-pass membrane protein {ECO:0000269|PubMed:17724469}. Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:17724469}.!autophagy [GO:0006914]; cell junction assembly [GO:0034329]; embryo implantation [GO:0007566]; endoplasmic reticulum organization [GO:0007029]; exocytosis [GO:0006887]; Golgi organization [GO:0007030]; regulation of autophagy [GO:0010506]; single organismal cell-cell adhesion [GO:0016337]Bautophagosome membrane [GO:0000421]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; pre-autophagosomal structure [GO:0000407]FUNCTION: Stress-induced protein that, when overexpressed, promotes formation of intracellular vacuoles followed by cell death. May be involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis. Plays a role in the initial stages of the autophagic process through its interaction with BECN1 (By similarity). Involved in cell-cell adhesion. Plays an essential role in formation of cell junctions. {ECO:0000250, ECO:0000269|PubMed:17724469}.P61964WDR5WD repeat-containing protein 5YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:20018852}.chromatin organization [GO:0006325]; histone H3 acetylation [GO:0043966]; histone H3-K4 methylation [GO:0051568]; histone H4-K16 acetylation [GO:0043984]; histone H4-K5 acetylation [GO:0043981]; histone H4-K8 acetylation [GO:0043982]; neuron projection development [GO:0031175]; positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter [GO:0035948]; skeletal system development [GO:0001501]; transcription, DNA-templated [GO:0006351] Ada2/Gcn5/Ada3 transcription activator complex [GO:0005671]; histone acetyltransferase complex [GO:0000123]; histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]wFUNCTION: Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation. {ECO:0000269|PubMed:16600877, ECO:0000269|PubMed:16829960, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20018852}.Q13330MTA1"Metastasis-associated protein MTA1SUBCELLULAR LOCATION: Isoform Short: Cytoplasm.; SUBCELLULAR LOCATION: Isoform Long: Nucleus. Nucleus envelope. Cytoplasm. Cytoplasm, cytoskeleton. Note=Associated with microtubules. Localization at the nuclear envelope is TPR-dependent.chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; double-strand break repair [GO:0006302]; entrainment of circadian clock by photoperiod [GO:0043153]; female pregnancy [GO:0007565]; locomotor rhythm [GO:0045475]; negative regulation of nucleic acid-templated transcription [GO:1903507]; positive regulation of protein autoubiquitination [GO:1902499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of gene expression, epigenetic [GO:0040029]; regulation of inflammatory response [GO:0050727]; response to ionizing radiation [GO:0010212]; response to lipopolysaccharide [GO:0032496]; secretory granule organization [GO:0033363]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; core promoter sequence-specific DNA binding [GO:0001046]; RNA polymerase II repressing transcription factor binding [GO:0001103]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; microtubule [GO:0005874]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]FUNCTION: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24413532}.O43169CYB5BCytochrome b5 type BASUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}.mintegral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. {ECO:0000250}.Q8NEZ2VP37A/Vacuolar protein sorting-associated protein 37ASSUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein. Nucleus.{endosomal transport [GO:0016197]; intracellular transport of virus [GO:0075733]; membrane organization [GO:0061024]; protein transport [GO:0015031]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]centrosome [GO:0005813]; cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; nucleoplasm [GO:0005654]FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:1524< 0819}.P52272HNRPM)Heterogeneous nuclear ribonucleoprotein M=SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|Ref.5}.alternative mRNA splicing, via spliceosome [GO:0000380]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723]Hcatalytic step 2 spliceosome [GO:0071013]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; paraspeckles [GO:0042382]; spliceosomal complex [GO:0005681]pFUNCTION: Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.Q53GA4PHLA21Pleckstrin homology-like domain family A member 2#apoptotic process [GO:0006915]; organ morphogenesis [GO:0009887]; placenta development [GO:0001890]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]; regulation of gene expression [GO:0010468]; regulation of glycogen metabolic process [GO:0070873]FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids (By similarity). {ECO:0000250}.Q9Y6G5COMDA!COMM domain-containing protein 10Q9Y3A4RRP7A,Ribosomal RNA-processing protein 7 homolog Anblastocyst formation [GO:0001825]; ribosomal small subunit assembly [GO:0000028]; rRNA processing [GO:0006364]MCURI complex [GO:0032545]; cytoplasm [GO:0005737]; UTP-C complex [GO:0034456]Q13433S39A6Zinc transporter ZIP6}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12839489}; Multi-pass membrane protein {ECO:0000269|PubMed:12839489}.8zinc ion transmembrane transporter activity [GO:0005385]cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; integral component of plasma membrane [GO:0005887]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]NFUNCTION: May act as a zinc-influx transporter. {ECO:0000269|PubMed:12839489}.P04626ERBB2'Receptor tyrosine-protein kinase erbB-2eSUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. Cytoplasm, perinuclear region. Nucleus. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.axon guidance [GO:0007411]; cell proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; enzyme linked receptor protein signaling pathway [GO:0007167]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart development [GO:0007507]; innate immune response [GO:0045087]; motor neuron axon guidance [GO:0008045]; myelination [GO:0042552]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; neuromuscular junction development [GO:0007528]; neurotrophin TRK receptor signaling pathway [GO:0048011]; oligodendrocyte differentiation [GO:0048709]; peptidyl-tyrosine phosphorylation [GO:0018108]; peripheral nervous system development [GO:0007422]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of GTPase activity [GO:0043547]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase III promoter [GO:0045945]; positive regulation of transcription from RNA polymerase I promoter [GO:0045943]; positive regulation of translation [GO:0045727]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of angiogenesis [GO:0045765]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of microtubule-based process [GO:0032886]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; transcription, DNA-templated [GO:0006351]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; wound healing [GO:0042060]8ATP binding [GO:0005524]; ErbB-3 class receptor binding [GO:0043125]; identical protein binding [GO:0042802]; protein C-terminus binding [GO:0008022]; protein dimerization activity [GO:0046983]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; receptor signaling protein tyrosine kinase activity [GO:0004716]; RNA polymerase I core binding [GO:0001042]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane signaling receptor activity [GO:0004888]qapical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endosome membrane [GO:0010008]; integral component of membrane [GO:0016021]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]iFUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.; FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.Q9NRX5SERC1Serine incorporator 1]L-serine transport [GO:0015825]; phosphatidylserine metabolic process [GO:0006658]; phospholipid biosynthetic process [GO:0008654]; positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity [GO:1904219]; positive regulation of serine C-palmitoyltransferase activity [GO:1904222]; sphingolipid metabolic process [GO:0006665]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]hFUNCTION: Enhances the incorporation of serine into phosphatidylserine and sphingolipids. {ECO:0000250}.P61266STX1B Syntaxin-1BSUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18691641}. Note=Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma-tubulin in the pericentrosomal region of the mitotic spindle in dividing cells.exocytosis [GO:0006887]; intracellular protei< n transport [GO:0006886]; positive regulation of excitatory postsynaptic membrane potential [GO:2000463]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of gene expression [GO:0010468]; regulation of synaptic vesicle priming [GO:0010807]; spontaneous neurotransmitter secretion [GO:0061669]; synaptic vesicle docking [GO:0016081]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; vesicle docking [GO:0048278]dprotein kinase binding [GO:0019901]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]+cytosol [GO:0005829]; endomembrane system [GO:0012505]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). {ECO:0000250}.Q99500S1PR3"Sphingosine 1-phosphate receptor 3 adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; anatomical structure morphogenesis [GO:0009653]; cytokine production [GO:0001816]; G-protein coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; negative regulation of establishment of endothelial barrier [GO:1903141]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of interleukin-1 beta production [GO:0032651]G-protein coupled receptor activity [GO:0004930]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; sphingosine-1-phosphate receptor activity [GO:0038036]fcytosol [GO:0005829]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886][FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis. {ECO:0000269|PubMed:10617617}.Q16774KGUAGuanylate kinase>ATP metabolic process [GO:0046034]; dATP metabolic process [GO:0046060]; dGDP biosynthetic process [GO:0006185]; dGMP metabolic process [GO:0046054]; drug metabolic process [GO:0017144]; GDP biosynthetic process [GO:0046711]; GDP-mannose metabolic process [GO:0019673]; glycoprotein transport [GO:0034436]; GMP metabolic process [GO:0046037]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleotide metabolic process [GO:0006163]; small molecule metabolic process [GO:0044281];FUNCTION: Essential for recycling GMP and indirectly, cGMP.Q9H1E5TMX4+Thioredoxin-related transmembrane protein 4cell redox homeostasis [GO:0045454]; oxidation-reduction process [GO:0055114]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]O76061STC2Stanniocalcin-29cellular calcium ion homeostasis [GO:0006874]; cellular response to hypoxia [GO:0071456]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of gene expression [GO:0010629]; negative regulation of multicellular organism growth [GO:0040015]; regulation of hormone biosynthetic process [GO:0046885]; regulation of store-operated calcium entry [GO:2001256]; response to oxidative stress [GO:0006979]; response to peptide hormone [GO:0043434]; response to vitamin D [GO:0033280]fenzyme binding [GO:0019899]; heme binding [GO:0020037]; protein homodimerization activity [GO:0042803]endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]OFUNCTION: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.P12956XRCC6*X-ray repair cross-complementing protein 6fSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688}. Chromosome {ECO:0000269|PubMed:22442688}.DNA duplex unwinding [GO:0032508]; DNA ligation [GO:0006266]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of integrated proviral latency [GO:0075713]; innate immune response [GO:0045087]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of smooth muscle cell proliferation [GO:0048660]; telomere maintenance [GO:0000723]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; telomeric DNA binding [GO:0042162]; transcription regulatory region DNA binding [GO:0044212]cytosol [GO:0005829]; Ku70:Ku80 complex [GO:0043564]; membrane [GO:0016020]; nonhomologous end joining complex [GO:0070419]; nuclear telomere cap complex [GO:0000783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. {ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:2466842, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:9742108}.Q9NUP9LIN7CProtein lin-7 homolog CSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12967566}; Peripheral membrane protein {ECO:0000269|PubMed:12967566}. Basolateral cell membrane {ECO:0000269|PubMed:12967566}; Peripheral membrane protein {ECO:0000269|PubMed:12967566}. Cell junction {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Enriched in synaptosomes and at epithelial cell-cell junctions (By similarity). Mainly basolateral in renal epithelial cells. {ECO:0000250}.jasymmetric protein localization [GO:0008105]; exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; morphogenesis of an epithelial sheet [GO:0002011]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031]; synaptic transmission [GO:0007< 268]xcytoskeletal protein binding [GO:0008092]; L27 domain binding [GO:0097016]; protein domain specific binding [GO:0019904]mbasolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; MPP7-DLG1-LIN7 complex [GO:0097025]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202];FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.Q13891BT3L2#Transcription factor BTF3 homolog 2P78371TCPB T-complex protein 1 subunit beta>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}.de novo' posttranslational protein folding [GO:0051084]; binding of sperm to zona pellucida [GO:0007339]; cellular protein metabolic process [GO:0044267]; chaperone-mediated protein complex assembly [GO:0051131]; protein folding [GO:0006457]; toxin transport [GO:1901998]nATP binding [GO:0005524]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]cell body [GO:0044297]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; zona pellucida receptor complex [GO:0002199]O94813SLIT2Slit homolog 2 proteinSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10102268}. Note=The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated. apoptotic process involved in luteolysis [GO:0061364]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branching morphogenesis of an epithelial tube [GO:0048754]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to heparin [GO:0071504]; cellular response to hormone stimulus [GO:0032870]; chemorepulsion involved in postnatal olfactory bulb interneuron migration [GO:0021836]; corticospinal neuron axon guidance through spinal cord [GO:0021972]; dorsal/ventral axon guidance [GO:0033563]; induction of negative chemotaxis [GO:0050929]; in utero embryonic development [GO:0001701]; mammary duct terminal end bud growth [GO:0060763]; metanephros development [GO:0001656]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of axon extension [GO:0030517]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of gene expression [GO:0010629]; negative regulation of GTPase activity [GO:0034260]; negative regulation of inflammatory response [GO:0050728]; negative regulation of lamellipodium assembly [GO:0010593]; negative regulation of leukocyte chemotaxis [GO:0002689]; negative regulation of monocyte chemotaxis [GO:0090027]; negative regulation of mononuclear cell migration [GO:0071676]; negative regulation of neutrophil chemotaxis [GO:0090024]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of retinal ganglion cell axon guidance [GO:0090260]; negative regulation of small GTPase mediated signal transduction [GO:0051058]; negative regulation of smooth muscle cell chemotaxis [GO:0071672]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of vascular permeability [GO:0043116]; positive regulation of apoptotic process [GO:0043065]; positive regulation of axonogenesis [GO:0050772]; response to cortisol [GO:0051414]; response to nutrient levels [GO:0031667]; retinal ganglion cell axon guidance [GO:0031290]; Roundabout signaling pathway [GO:0035385]; single organismal cell-cell adhesion [GO:0016337]; spinal cord development [GO:0021510]; ureteric bud development [GO:0001657]Hcalcium ion binding [GO:0005509]; chemorepellent activity [GO:0045499]; GTPase inhibitor activity [GO:0005095]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; laminin-1 binding [GO:0043237]; protein homodimerization activity [GO:0042803]; proteoglycan binding [GO:0043394]; Roundabout binding [GO:0048495]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration. {ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:10864954, ECO:0000269|PubMed:10975526, ECO:0000269|PubMed:11239147, ECO:0000269|PubMed:11309622, ECO:0000269|PubMed:11404413}.O14972DSCR3'Down syndrome critical region protein 3,intracellular protein transport [GO:0006886]P366398ODP'7,8-dihydro-8-oxoguanine triphosphataseModulation of nucleotide poolsSUBCELLULAR LOCATION: Isoform p18: Cytoplasm. Mitochondrion matrix. Nucleus. Note=Mostly present in cytoplasm. Variant Met-124 has decreased efficiency in translocation to mitochondria.; SUBCELLULAR LOCATION: Isoform p26: Cytoplasm. Mitochondrion matrix.dATP catabolic process [GO:0046061]; dGTP catabolic process [GO:0006203]; DNA protection [GO:0042262]; DNA repair [GO:0006281]; nucleobase-containing small molecule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleotide catabolic process [GO:0006195]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]N8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [G< O:0035539]; 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; ATP diphosphatase activity [GO:0047693]; GTPase activity [GO:0003924]; GTP diphosphatase activity [GO:0036219]; metal ion binding [GO:0046872]; snoRNA binding [GO:0030515]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:10608900, ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:22556419}.P42224STAT1=Signal transducer and activator of transcription 1-alpha/beta SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15322115}. Nucleus {ECO:0000269|PubMed:15322115}. Note=Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4.apoptotic process [GO:0006915]; blood circulation [GO:0008015]; cellular response to interferon-beta [GO:0035458]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; interferon-gamma-mediated signaling pathway [GO:0060333]; JAK-STAT cascade [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; metanephric mesenchymal cell differentiation [GO:0072162]; metanephric mesenchymal cell proliferation involved in metanephros development [GO:0072136]; negative regulation by virus of viral protein levels in host cell [GO:0046725]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of macrophage fusion [GO:0034240]; negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003340]; negative regulation of metanephric nephron tubule epithelial cell differentiation [GO:0072308]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; renal tubule development [GO:0061326]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]; response to exogenous dsRNA [GO:0043330]; response to peptide hormone [GO:0043434]; transcription, DNA-templated [GO:0006351]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]Wdouble-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity [GO:0000983]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]; tumor necrosis factor receptor binding [GO:0005164]axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nuclear chromatin [GO:0000790]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. {ECO:0000269|PubMed:12764129, ECO:0000269|PubMed:12855578, ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:9724754}.O43567RNF13!E3 ubiquitin-protein ligase RNF13NSUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Golgi apparatus membrane. Late endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Lysosome membrane. Nucleus inner membrane {ECO:0000250}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250}.endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; nuclear inner membrane [GO:0005637]|FUNCTION: E3 ubiquitin-protein ligase that may play a role in controlling cell proliferation. {ECO:0000269|PubMed:18794910}.Q53H12AGK"Acylglycerol kinase, mitochondrialhSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:16269826}.Wceramide biosynthetic process [GO:0046513]; glycerolipid metabolic process [GO:0046486]acylglycerol kinase activity [GO:0047620]; ATP binding [GO:0005524]; ceramide kinase activity [GO:0001729]; diacylglycerol kinase activity [GO:0004143]vintracellular membrane-bounded organelle [GO:0043231]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth. {ECO:0000269|PubMed:15939762}.Q8TDJ6DMXL2DmX-like protein 2_SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11809763}; Peripheral membrane protein {ECO:0000269|PubMed:11809763}. Note=The external layer of the inferior boundary for the hypothalamus part of the human brain (the so called median eminence (ME)) displayed a punctate pattern of expression; expression also observed in the cell bodies lining the third ventricle, in the long processes extending from these cell bodies toward the external layer of the ME, in small clear vesicles, and in large dense core vesicles. {ECO:0000250|UniProtKB:Q8BPN8}.cell junction [GO:0030054]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]FUNCTION: May serve as a scaffold protein for MADD and RAB3GA on synaptic vesicles (PubMed:11809763). Pla< ys a role in the brain as a key controller of neuronal and endocrine homeostatic processes (By similarity). {ECO:0000250|UniProtKB:Q8BPN8, ECO:0000269|PubMed:11809763}.O75367H2AYCore histone macro-H2A.1chromatin modification [GO:0016568]; dosage compensation [GO:0007549]; establishment of protein localization to chromatin [GO:0071169]; negative regulation of cell cycle G2/M phase transition [GO:1902750]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of histone H3-K27 methylation [GO:0061086]; negative regulation of histone H3-K4 methylation [GO:0051572]; negative regulation of histone phosphorylation [GO:0033128]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter [GO:1901837]; nucleosome assembly [GO:0006334]; positive regulation of gene expression, epigenetic [GO:0045815]; positive regulation of keratinocyte differentiation [GO:0045618]; regulation of gene expression, epigenetic [GO:0040029]; regulation of lipid metabolic process [GO:0019216](chromatin DNA binding [GO:0031490]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; double-stranded methylated DNA binding [GO:0010385]; nucleosomal DNA binding [GO:0031492]; protein kinase binding [GO:0019901]; protein serine/threonine kinase inhibitor activity [GO:0030291]; rDNA binding [GO:0000182]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; transcription regulatory region DNA binding [GO:0044212]EBarr body [GO:0001740]; condensed chromosome [GO:0000793]; extracellular exosome [GO:0070062]; nuclear chromatin [GO:0000790]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; sex chromatin [GO:0001739]OFUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation. {ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16428466}.Q9Y3D0MIP185Mitotic spindle-associated MMXD complex subunit MIP18|SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}.}chromosome segregation [GO:0007059]; iron-sulfur cluster assembly [GO:0016226]; small molecule metabolic process [GO:0044281]CIA complex [GO:0097361]; cytoplasm [GO:0005737]; MMXD complex [GO:0071817]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. {ECO:0000269|PubMed:20797633}.Q96L91EP400E1A-binding protein p400ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.nchromatin organization [GO:0006325]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]RATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]NuA4 histone acetyltransferase complex [GO:0035267]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; Swr1 complex [GO:0000812]AFUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. May regulate ZNF42 transcription activity. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:24463511}.Q8IUD2RB6I2*ELKS/Rab6-interacting/CAST family member 1_SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=In neurons, localized closed to presynaptic membrane. Recruited on Golgi membranes by RAB6A in a GTP-dependent manner (By similarity). {ECO:0000250}.4I-kappaB phosphorylation [GO:0007252]; multicellular organismal development [GO:0007275]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein transport [GO:0015031]; regulation of transcription, DNA-templated [GO:0006355]; retrograde transport, endosome to Golgi [GO:0042147]lleucine zipper domain binding [GO:0043522]; PDZ domain binding [GO:0030165]; Rab GTPase binding [GO:0017137]cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]; IkappaB kinase complex [GO:0008385]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]FUNCTION: Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex. May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport. {ECO:0000269|PubMed:15218148}.P20936RASA1Ras GTPase-activating protein 1=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8360177}.)axon guidance [GO:0007411]; blood vessel morphogenesis [GO:0048514]; embryo development [GO:0009790]; ephrin receptor signaling pathway [GO:0048013]; intracellular signal transduction [GO:0035556]; mitotic cytokinesis [GO:0000281]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of GTPase activity [GO:0043547]; regulation of actin filament polymerization [GO:0030833]; regulation of cell shape [GO:0008360]; regulation of RNA metabolic process [GO:0051252]; signal transduction [GO:0007165]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vasculogenesis [GO:0001570]glycoprotein binding [GO:0001948]; GTPase activator activity [GO:0005096]; GTPase binding [GO:0051020]; potassium channel inhibitor activity [GO:0019870]; receptor binding [GO:0005102]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; ruffle [GO:0001726]FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the prese< nce of NCK1. {ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:8360177}.Q86YN1DOPP1Dolichyldiphosphatase 1rcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichyl diphosphate biosynthetic process [GO:0006489]; lipid biosynthetic process [GO:0008610]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]+dolichyldiphosphatase activity [GO:0047874]endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; intracellular membrane-bounded organelle [GO:0043231]5FUNCTION: Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity). {ECO:0000250|UniProtKB:Q9JMF7}.Q13636RAB31Ras-related protein Rab-31SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis. cellular response to insulin stimulus [GO:0032869]; Golgi to plasma membrane protein transport [GO:0043001]; phagosome maturation [GO:0090382]; Rab protein signal transduction [GO:0032482]; receptor internalization [GO:0031623]; regulated secretory pathway [GO:0045055]early endosome [GO:0005769]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; trans-Golgi network membrane [GO:0032588]FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17678623, ECO:0000269|PubMed:19725050, ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:21586568}.Q14764MVPMajor vault proteinSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex. Note=5% found in the nuclear pore complex. Translocates from the nucleus to the cytoplasm upon EGF treatment.ERBB signaling pathway [GO:0038127]; mRNA transport [GO:0051028]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of protein tyrosine kinase activity [GO:0061099]; negative regulation of signaling [GO:0023057]; protein transport [GO:0015031]Mprotein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear pore [GO:0005643]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:0030529]FUNCTION: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases. {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217, ECO:0000269|PubMed:16441665}.Q8TCS8PNPT1:Polyribonucleotide nucleotidyltransferase 1, mitochondrialoSUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Mitochondrion intermembrane space; Peripheral membrane protein.cellular response to interferon-beta [GO:0035458]; cellular response to oxidative stress [GO:0034599]; mitochondrial mRNA catabolic process [GO:0000958]; mitochondrial mRNA polyadenylation [GO:0097222]; mitochondrial RNA 3'-end processing [GO:0000965]; mitochondrial RNA 5'-end processing [GO:0000964]; mitochondrial RNA catabolic process [GO:0000957]; mitochondrion morphogenesis [GO:0070584]; mitotic cell cycle arrest [GO:0071850]; mRNA catabolic process [GO:0006402]; negative regulation of growth [GO:0045926]; nuclear polyadenylation-dependent mRNA catabolic process [GO:0071042]; positive regulation of miRNA catabolic process [GO:2000627]; positive regulation of mitochondrial RNA catabolic process [GO:0000962]; positive regulation of mRNA catabolic process [GO:0061014]; protein homooligomerization [GO:0051260]; protein homotrimerization [GO:0070207]; regulation of cellular respiration [GO:0043457]; regulation of cellular senescence [GO:2000772]; RNA catabolic process [GO:0006401]; RNA import into mitochondrion [GO:0035927]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; RNA polyadenylation [GO:0043631]; rRNA import into mitochondrion [GO:0035928]3'-5'-exoribonuclease activity [GO:0000175]; miRNA binding [GO:0035198]; poly(A) RNA binding [GO:0044822]; poly(G) binding [GO:0034046]; poly(U) RNA binding [GO:0008266]; polyribonucleotide nucleotidyltransferase activity [GO:0004654]cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrial degradosome [GO:0045025]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]FUNCTION: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA. {ECO:0000269|PubMed:12473748, ECO:0000269|PubMed:12721301, ECO:0000269|PubMed:12798676, ECO:0000269|PubMed:16055741, ECO:0000269|PubMed:16410805, ECO:0000269|PubMed:16934922, ECO:0000269|PubMed:18083836, ECO:0000269|PubMed:18083837, ECO:0000269|PubMed:18501193, ECO:0000269|PubMed:19509288, ECO:0000269|PubMed:20547861, ECO:0000269|PubMed:20691904}.Q6P2Q9PRP8%Pre-mRNA-processing-splicing factor 84SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]2K63-linked polyubiquitin binding [GO:0070530]; poly(A) RNA binding [GO:0044822]; pre-mRNA intronic binding [GO:0097157]; second spliceosomal transesterification activity [GO:0000386]; U1 snRNA bind< ing [GO:0030619]; U2 snRNA binding [GO:0030620]; U5 snRNA binding [GO:0030623]; U6 snRNA binding [GO:0017070]catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U5 snRNP [GO:0005682]FUNCTION: Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. {ECO:0000269|PubMed:20595234, ECO:0000303|PubMed:15840809}.Q9NZL4HPBP1Hsp70-binding protein 1negative regulation of catalytic activity [GO:0043086]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; protein folding [GO:0006457]; regulation of catalytic activity [GO:0050790]_adenyl-nucleotide exchange factor activity [GO:0000774]; enzyme inhibitor activity [GO:0004857]sFUNCTION: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. {ECO:0000269|PubMed:10786638, ECO:0000269|PubMed:12651857, ECO:0000269|PubMed:15215316, ECO:0000269|PubMed:9830037}.P48723HSP13Heat shock 70 kDa protein 13}endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]2FUNCTION: Has peptide-independent ATPase activity.Q9UK76HN12Hematological and neurological expressed 1 protein"developmental process [GO:0032502]O95297MPZL1"Myelin protein zero-like protein 1ocell-cell signaling [GO:0007267]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]jcell surface [GO:0009986]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]gFUNCTION: Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:12410637}.Q9H0U9TSYL1(Testis-specific Y-encoded-like protein 1Q6UWP7LCLT1!Lysocardiolipin acyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19075029}; Multi-pass membrane protein {ECO:0000269|PubMed:19075029}.cardiolipin acyl-chain remodeling [GO:0035965]; CDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; glycerophospholipid biosynthetic process [GO:0046474]; multicellular organismal development [GO:0007275]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]}FUNCTION: Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages. {ECO:0000269|PubMed:16620771, ECO:0000269|PubMed:19075029}.Q8IXH7NELFDNegative elongation factor C/D6gene expression [GO:0010467]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of viral transcription [GO:0050434]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Jmembrane [GO:0016020]; NELF complex [GO:0032021]; nucleoplasm [GO:0005654]`FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12612062}.Q9NYU2UGGG1.UDP-glucose:glycoprotein glucosyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:10694380}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:10694380}.de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-glucosylation [GO:0097359]iUDP-glucose:glycoprotein glucosyltransferase activity [GO:0003980]; unfolded protein binding [GO:0051082]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]vFUNCTION: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. {ECO:0000269|PubMed:10694380}.Q15717ELAV1ELAV-like protein 1uSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates into the cytoplasm following phosphorylation by MAPKAPK2.3'-UTR-mediated mRNA stabilization [GO:0070935]; gene expression [GO:0010467]; mRNA stabilization [GO:0048255]; multicellular organismal development [GO:0007275]; positive regulation of translation [GO:0045727]; regulation of stem cell maintenance [GO:2000036]>AU-rich element binding [GO:0017091]; double-stranded RNA binding [GO:0003725]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; RNA binding [GO:0003723]FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro. With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA. {ECO:0000269|PubMed:19029303}.Q9Y2L9LRCH1ELeucine-rich repeat and calponin homology domain-containing protein 1Q9NVI7ATD3A.ATPase family AAA domain-containing protein 3ASUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion matrix, mitochondrion nucleoid. Note=In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane. The N-terminal domain interacts w< ith the inner surface of the mitochondrial outer membrane and the C-terminal domain localizes in a specific matrix compartment, where it is associated with nucleoids.Ocell growth [GO:0016049]; negative regulation of apoptotic process [GO:0043066]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis. {ECO:0000269|PubMed:17210950, ECO:0000269|PubMed:20154147, ECO:0000269|PubMed:22453275}.P40227TCPZ T-complex protein 1 subunit zetade novo' posttranslational protein folding [GO:0051084]; binding of sperm to zona pellucida [GO:0007339]; cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]; toxin transport [GO:1901998]aATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; unfolded protein binding [GO:0051082]acrosomal vesicle [GO:0001669]; cell body [GO:0044297]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; zona pellucida receptor complex [GO:0002199]FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.Q16822PCKGM6Phosphoenolpyruvate carboxykinase [GTP], mitochondrial Glycolysis / Gluconeogenesis(66)carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]GTP binding [GO:0005525]; metal ion binding [GO:0046872]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; phosphoenolpyruvate carboxykinase activity [GO:0004611]FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. {ECO:0000250}.Q9UKL6PPCT$Phosphatidylcholine transfer protein?SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53808}.mcholesterol metabolic process [GO:0008203]; lipid transport [GO:0006869]; phospholipid transport [GO:0015914]_phosphatidylcholine binding [GO:0031210]; phosphatidylcholine transporter activity [GO:0008525]FUNCTION: Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule. {ECO:0000269|PubMed:12055623}.Q5T200ZC3HD-Zinc finger CCCH domain-containing protein 13Q04206TF65Transcription factor p65,SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Colocalized with DDX1 in the nucleus upon TNF-alpha induction (By similarity). Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in the nucleus after LPS stimulation. {ECO:0000250}.6acetaldehyde metabolic process [GO:0006117]; aging [GO:0007568]; cellular defense response [GO:0006968]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to nicotine [GO:0071316]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to tumor necrosis factor [GO:0071356]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; Fc-epsilon receptor signaling pathway [GO:0038095]; hair follicle development [GO:0001942]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; liver development [GO:0001889]; membrane protein intracellular domain proteolysis [GO:0031293]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of NIK/NF-kappaB signaling [GO:1901223]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neurotrophin TRK receptor signaling pathway [GO:0048011]; NIK/NF-kappaB signaling [GO:0038061]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; organ morphogenesis [GO:0009887]; positive regulation of cell proliferation [GO:0008284]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-12 biosynthetic process [GO:0045084]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of Schwann cell differentiation [GO:0014040]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of inflammatory response [GO:0050727]; response to amino acid [GO:0043200]; response to cAMP [GO:0051591]; response to cobalamin [GO:0033590]; response to drug [GO:0042493]; response to insulin [GO:0032868]; response to interleukin-1 [GO:0070555]; response to morphine [GO:0043278]; response to muramyl dipeptide [GO:0032495]; response to muscle stretch [GO:0035994]; response to organic substance [GO:0010033]; response to progesterone [GO:0032570]; response to UV-B [GO:0010224]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; viral process [GO:0016032]cactinin binding [GO:0042805]; activating transcription factor binding [GO:0033613]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; NF-kappaB binding [GO:0051059]; phosphate ion binding [GO:0042301]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]; repressing transcription factor binding [GO:0070491]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [< GO:0001205]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; I-kappaB/NF-kappaB complex [GO:0033256]; NF-kappaB complex [GO:0071159]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). {ECO:0000269|PubMed:10928981, ECO:0000269|PubMed:12748188, ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:19103749, ECO:0000269|PubMed:20547752}.Q5MNZ9WIPI17WD repeat domain phosphoinositide-interacting protein 1;SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Endosome. Cytoplasmic vesicle, clathrin-coated vesicle. Preautophagosomal structure membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Note=Trans elements of the Golgi and peripheral endosomes. Dynamically cycles through these compartments and is susceptible to conditions that modulate membrane flux. Enriched in clathrin-coated vesicles. Upon starvation-induced autophagy, accumulates at subcellular structures in the cytoplasm: enlarged vesicular and lasso-like structures, and large cup-shaped structures predominantly around the nucleus. Recruitment to autophagic membranes is controlled by MTMR14. Labile microtubules specifically recruit markers of autophagosome formation like WIPI1, whereas mature autophagosomes may bind to stable microtubules.autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular protein metabolic process [GO:0044267]; cellular response to nitrogen starvation [GO:0006995]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; protein lipidation [GO:0006497]; protein localization to pre-autophagosomal structure [GO:0034497]; vesicle targeting, trans-Golgi to endosome [GO:0048203]androgen receptor binding [GO:0050681]; estrogen receptor binding [GO:0030331]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; receptor binding [GO:0005102]~autophagosome membrane [GO:0000421]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; extrinsic component of membrane [GO:0019898]; Golgi membrane [GO:0000139]; pre-autophagosomal structure [GO:0000407]; pre-autophagosomal structure membrane [GO:0034045]; trans-Golgi network [GO:0005802]FUNCTION: Plays an important role in autophagy and in particular starvation- and calcium-mediated autophagy, as well as in mitophagy. Functions upstream of the ATG12-ATG5-ATG16L1 complex and LC3, and downstream of the ULK1 and PI3-kinase complexes. Involved in xenophagy of Staphylococcus aureus. Invading S.aureus cells become entrapped in autophagosome-like WIPI1 positive vesicles targeted for lysosomal degradation. Plays also a distinct role in controlling the transcription of melanogenic enzymes and melanosome maturation, a process that is distinct from starvation-induced autophagy. May also regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway. {ECO:0000269|PubMed:15020712, ECO:0000269|PubMed:15602573, ECO:0000269|PubMed:20114074, ECO:0000269|PubMed:20484055, ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21317285, ECO:0000269|PubMed:22829830, ECO:0000269|PubMed:23088497}.Q9Y5V3MAGD1Melanoma-associated antigen D1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF. {ECO:0000250}.apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; circadian regulation of gene expression [GO:0032922]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of transcription, DNA-templated [GO:0045892]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of transcription, DNA-templated [GO:0045893]; programmed cell death [GO:0012501]; regulation of apoptotic process [GO:0042981]; regulation of circadian rhythm [GO:0042752]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as ARNTL/BMAL1 and NFIL3, induced, or NR1D1, repressed. {ECO:0000269|PubMed:20864041}.Q96CP2FWCH2FLYWCH family member 2Q8WUA4TF3C2-General transcription factor 3C polypeptide 25S class rRNA transcription from RNA polymerase III type 1 promoter [GO:0042791]; gene expression [GO:0010467]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase III promoter [GO:0006383]; tRNA transcription from RNA poly< merase III promoter [GO:0042797]Jnucleoplasm [GO:0005654]; transcription factor TFIIIC complex [GO:0000127]3FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1.Q99700ATX2Ataxin-2Acerebellar Purkinje cell differentiation [GO:0021702]; cytoplasmic mRNA processing body assembly [GO:0033962]; homeostasis of number of cells [GO:0048872]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of receptor internalization [GO:0002091]; neuromuscular process [GO:0050905]; neuron projection morphogenesis [GO:0048812]; regulation of cytoplasmic mRNA processing body assembly [GO:0010603]; regulation of translation [GO:0006417]; RNA metabolic process [GO:0016070]; RNA transport [GO:0050658]; stress granule assembly [GO:0034063]epidermal growth factor receptor binding [GO:0005154]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]; trans-Golgi network [GO:0005802]FUNCTION: Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}.Q8WZA1PMGT1CProtein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1qSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.jbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity [GO:0047223]QFUNCTION: Participates in O-mannosyl glycosylation. May be responsible for the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity. {ECO:0000269|PubMed:11709191}.Q4G0J3LARP7La-related protein 7ISUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:18483487}.cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]wFUNCTION: Negative transcriptional regulator of polymerase II genes, acting by means of the 7SK RNP system. Within the 7SK RNP complex, the positive transcription elongation factor b (P-TEFb) is sequestered in an inactive form, preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. {ECO:0000269|PubMed:18249148, ECO:0000269|PubMed:18483487}.O15371EIF3D4Eukaryotic translation initiation factor 3 subunit DBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; membrane [GO:0016020]Q14914PTGR1Prostaglandin reductase 1arachidonic acid metabolic process [GO:0019369]; cyclooxygenase pathway [GO:0019371]; leukotriene metabolic process [GO:0006691]; lipoxin metabolic process [GO:2001300]; response to toxic substance [GO:0009636]; small molecule metabolic process [GO:0044281]13-prostaglandin reductase activity [GO:0036132]; 15-oxoprostaglandin 13-oxidase activity [GO:0047522]; 2-alkenal reductase [NAD(P)] activity [GO:0032440]; zinc ion binding [GO:0008270]FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha (By similarity). Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4. {ECO:0000250}.P63165SUMO1"Small ubiquitin-related modifier 1SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane {ECO:0000269|PubMed:19223394}. Note=Recruited by BCL11A into the nuclear body. {ECO:0000250}.cellular protein metabolic process [GO:0044267]; cytokine-mediated signaling pathway [GO:0019221]; DNA repair [GO:0006281]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of action potential [GO:0045759]; negative regulation of delayed rectifier potassium channel activity [GO:1902260]; negative regulation of DNA binding [GO:0043392]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; palate development [GO:0060021]; PML body organization [GO:0030578]; positive regulation of calcium-transporting ATPase activity [GO:1901896]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein complex assembly [GO:0031334]; post-translational protein modification [GO:0043687]; protein localization to nuclear pore [GO:0090204]; protein sumoylation [GO:0016925]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; regulation of protein localization [GO:0032880]; regulation of protein stability [GO:0031647]; viral process [GO:0016032]ion channel binding [GO:0044325]; poly(A) RNA binding [GO:0044822]; potassium channel regulator activity [GO:0015459]; SUMO transferase activity [GO:0019789]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]icytoplasm [GO:0005737]; dendrite [GO:0030425]; fibrillar center [GO:0001650]; heterochromatin [GO:0000792]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; synapse [GO:0045202]; XY body [GO:0001741]FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:19223394, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:9019411, ECO:0000269|PubMed:9162015}.P22301IL10Interleukin-10Ligand(IFN/IL10) aging [GO:0007568]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; branching involved in labyrinthine layer morphogenesis [GO:0060670]; cell-cell signaling [GO:0007267]; cellular response to estradiol stimulus [GO:0071392]; cellular response to lipopolysaccharide [GO:0071222]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; defense response to bacterium [GO:0042742]; defense response to protozoan [GO:0042832]; hemopoiesis [GO:0030097]; inflammatory response [GO:0006954]; leukocyte chemotaxis [GO:0030595]; negative regulation of apoptotic process [GO:0043066]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of chemokine (C-C< motif) ligand 5 production [GO:0071650]; negative regulation of chronic inflammatory response to antigenic stimulus [GO:0002875]; negative regulation of cytokine activity [GO:0060302]; negative regulation of cytokine secretion involved in immune response [GO:0002740]; negative regulation of growth of symbiont in host [GO:0044130]; negative regulation of interferon-alpha biosynthetic process [GO:0045355]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of interleukin-18 production [GO:0032701]; negative regulation of interleukin-1 production [GO:0032692]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of myeloid dendritic cell activation [GO:0030886]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of tumor necrosis factor biosynthetic process [GO:0042536]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of B cell apoptotic process [GO:0002904]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; receptor biosynthetic process [GO:0032800]; regulation of gene expression [GO:0010468]; regulation of isotype switching [GO:0045191]; regulation of sensory perception of pain [GO:0051930]; response to activity [GO:0014823]; response to carbon monoxide [GO:0034465]; response to drug [GO:0042493]; response to glucocorticoid [GO:0051384]; response to inactivity [GO:0014854]; response to insulin [GO:0032868]; response to molecule of bacterial origin [GO:0002237]; type 2 immune response [GO:0042092]qcytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-10 receptor binding [GO:0005141]8cytoplasm [GO:0005737]; extracellular space [GO:0005615]FUNCTION: Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.O75882ATRN AttractinSUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.; SUBCELLULAR LOCATION: Isoform 3: Secreted.cerebellum development [GO:0021549]; inflammatory response [GO:0006954]; myelination [GO:0042552]; pigmentation [GO:0043473]; regulation of multicellular organism growth [GO:0040014]; response to oxidative stress [GO:0006979]Acarbohydrate binding [GO:0030246]; receptor activity [GO:0004872]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines. May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system (By similarity). {ECO:0000250}.P17858PFKAL/ATP-dependent 6-phosphofructokinase, liver type canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; negative regulation of insulin secretion [GO:0046676]; protein homotetramerization [GO:0051289]; protein oligomerization [GO:0051259]; response to glucose [GO:0009749]; small molecule metabolic process [GO:0044281]6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; fructose-6-phosphate binding [GO:0070095]; fructose binding [GO:0070061]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]{6-phosphofructokinase complex [GO:0005945]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:22923583}.Q9BVK2ALG8MProbable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferasescellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; mannosylation [GO:0097502]; oligosaccharide-lipid intermediate biosynthetic process [GO:0006490]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]alpha-1,3-mannosyltransferase activity [GO:0000033]; dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity [GO:0042281]FUNCTION: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.Q9P013CWC15,Spliceosome-associated protein CWC15 homolog<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20176811}.|catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. {ECO:0000269|PubMed:20176811}.Q8IZK6MCLN2 Mucolipin-2calcium ion transmembrane transport [GO:0070588]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]Q8WUK0PTPM1APhosphatidylglycerophosphatase and protein-tyrosine phosphatase 1ySUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}. Note=Associated with the inner membrane. {ECO:0000250}.Scardiolipin biosynthetic process [GO:0032049]; glycerophospholipid biosynthetic process [GO:0046474]; inositol phosphate dephosphorylation [GO:0046855]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid metabolic process [GO:0006644]; protein dephosphorylation [GO:0006470]; small molecule metabolic process [GO:0044281]phosphatidylglycerophosphatase activity [GO:0008962]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]qintegral component of mitochondrial inner membrane [GO:0031305]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). {ECO:0000250}.Q16798MAON*NADP-dependent malic enzyme, mitochondrialaerobic respiration [GO:0009060]; malate metabolic process [GO:0006108]; oxidation-reduction process [GO:0055114]; oxygen metabolic process [GO:00725< 92]; pyruvate metabolic process [GO:0006090]8cofactor binding [GO:0048037]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; malic enzyme activity [GO:0004470]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; oxaloacetate decarboxylase activity [GO:0008948]P20933ASPG/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginaseaspartylglucosamimidaseEprotein deglycosylation [GO:0006517]; protein maturation [GO:0051604]dN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity [GO:0003948]; peptidase activity [GO:0008233]]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]uFUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.P60510PP4C8Serine/threonine-protein phosphatase 4 catalytic subunitcellular response to interleukin-1 [GO:0071347]; NIK/NF-kappaB signaling [GO:0038061]; regulation of double-strand break repair via homologous recombination [GO:0010569]metal ion binding [GO:0046872]; NF-kappaB-inducing kinase activity [GO:0004704]; protein serine/threonine phosphatase activity [GO:0004722]cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase 4 complex [GO:0030289]FUNCTION: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase (By similarity). In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin. {ECO:0000250, ECO:0000269|PubMed:11698396, ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:12934076, ECO:0000269|PubMed:1336397, ECO:0000269|PubMed:15805470, ECO:0000269|PubMed:18347064, ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705}.Q12979ABR0Active breakpoint cluster region-related proteinactin cytoskeleton organization [GO:0030036]; apoptotic signaling pathway [GO:0097190]; brain development [GO:0007420]; inner ear morphogenesis [GO:0042472]; negative regulation of blood vessel remodeling [GO:0060313]; negative regulation of cellular extravasation [GO:0002692]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neutrophil degranulation [GO:0043314]; neuromuscular process controlling balance [GO:0050885]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of phagocytosis [GO:0050766]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of vascular permeability [GO:0043114]; response to lipopolysaccharide [GO:0032496]; small GTPase mediated signal transduction [GO:0007264]cGTPase activator activity [GO:0005096]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them.O60427FADS1Fatty acid desaturase 1!SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:22619218}.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.Galpha-linolenic acid metabolic process [GO:0036109]; cell-cell signaling [GO:0007267]; cellular lipid metabolic process [GO:0044255]; cellular response to starvation [GO:0009267]; icosanoid biosynthetic process [GO:0046456]; linoleic acid metabolic process [GO:0043651]; phospholipid biosynthetic process [GO:0008654]; regulation of cell differentiation [GO:0045595]; regulation of transcription, DNA-templated [GO:0006355]; small molecule metabolic process [GO:0044281]; unsaturated fatty acid biosynthetic process [GO:0006636]; unsaturated fatty acid metabolic process [GO:0033559]QC-5 sterol desaturase activity [GO:0000248]; oxidoreductase activity [GO:0016491]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: Isoform 2 does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity (By similarity). Isoform 1 is a component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the desaturation of dihomo-gamma-linoleic acid (DHGLA) (20:3n-6) and eicosatetraenoic acid (20:4n-3) to generate arachidonic acid (AA) (20:4n-6) and eicosapentaenoic acid (EPA)(20:5n-3), respectively. {ECO:0000250, ECO:0000269|PubMed:10601301, ECO:0000269|PubMed:10769175}.Q9NRW3ABC3C#DNA dC->dU-editing enzyme APOBEC-3Ccytidine deamination [GO:0009972]; defense response to virus [GO:0051607]; DNA demethylation [GO:0080111]; innate immune response [GO:0045087]; negative regulation of transposition [GO:0010529]; negative regulation of viral genome replication [GO:0045071]; viral process [GO:0016032]hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines [GO:0016814]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]BFUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. {ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:15466872, ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21632763}.Q8IV48ERI13'-5' exoribonuclease 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16912046}. Nucleus {ECO:0000269|PubMed:16912046}. Nucleus, nucleolus {ECO:0000269|PubMed:16912046}. DNA catabolic process, exonucleolytic [GO:0000738]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; gene silencing by RNA [GO:0031047]; rRNA 3'-end processing [GO:0031125]3'-5' exonuclease activity [GO:0008408]; 3'-5'-exoribonuclease activity [GO:0000175]< ; histone pre-mRNA stem-loop binding [GO:0071207]; metal ion binding [GO:0046872]; ribosome binding [GO:0043022]; rRNA binding [GO:0019843]|cytoplasm [GO:0005737]; histone pre-mRNA 3'end processing complex [GO:0071204]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. {ECO:0000269|PubMed:14536070, ECO:0000269|PubMed:16912046}.Q15751HERC1*Probable E3 ubiquitin-protein ligase HERC1SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm, cytosol. Golgi apparatus. Note=Recruited onto actin-rich surface protrusions.cerebellar Purkinje cell differentiation [GO:0021702]; negative regulation of autophagy [GO:0010507]; neuromuscular process controlling balance [GO:0050885]; neuron projection development [GO:0031175]; positive regulation of GTPase activity [GO:0043547]; transport [GO:0006810]ARF guanyl-nucleotide exchange factor activity [GO:0005086]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]acytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]?FUNCTION: Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000269|PubMed:15642342, ECO:0000269|PubMed:8861955, ECO:0000269|PubMed:9233772}.Q8TAA9VANG1Vang-like protein 1Qintegral component of membrane [GO:0016021]; lateral plasma membrane [GO:0016328]Q8N9T8KRI1Protein KRI1 homologQ9GZT3SLIRP<SRA stem-loop-interacting RNA-binding protein, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16762838}. Nucleus {ECO:0000269|PubMed:16762838}. Note=Predominantly mitochondrial. Some fraction is nuclear. In the nucleus, it is recruited to nuclear receptor target promoters.9mitochondrion morphogenesis [GO:0070584]; negative regulation of mitochondrial RNA catabolic process [GO:0000961]; regulation of transcription, DNA-templated [GO:0006355]; single fertilization [GO:0007338]; spermatid development [GO:0007286]; sperm motility [GO:0030317]; transcription, DNA-templated [GO:0006351]acrosomal vesicle [GO:0001669]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:0030529]; sperm flagellum [GO:0036126]VFUNCTION: RNA-binding protein that acts as a nuclear receptor corepressor. Probably acts by binding the SRA RNA, and repressing the SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid (TR) and VDR-mediated transactivation. {ECO:0000269|PubMed:16762838}.P29144TPP2Tripeptidyl-peptidase 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19747897}. Nucleus {ECO:0000269|PubMed:19747897}. Note=Translocates to the nucleus in responce to gamma-irradiation.antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; tripeptidyl-peptidase activity [GO:0008240]+FUNCTION: Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity). {ECO:0000250}.Q9UKM9RALYRNA-binding protein RalyFUNCTION: Probable-RNA binding protein. Could be a heterogeneous nuclear ribonucleoprotein (hnRNP). May be involved in pre-mRNA splicing (By similarity). {ECO:0000250}.Q9Y3T9NOC2L#Nucleolar complex protein 2 homologHSUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Translocates from the nucleoli to the nucleoplasm in presence of several stressors like ultraviolet irradiation and actinomycin-D. Predominantly detected in the nucleoli in non-mitotic cells. Predominantly detected in nucleoplasma in cells undergoing mitosis.apoptotic process [GO:0006915]; cellular response to UV [GO:0034644]; chromatin assembly [GO:0031497]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of histone acetylation [GO:0035067]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleolus to nucleoplasm transport [GO:0032066]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; histone binding [GO:0042393]; nucleosome binding [GO:0031491]; poly(A) RNA binding [GO:0044822]; repressing transcription factor binding [GO:0070491]; transcription corepressor activity [GO:0003714]GFUNCTION: Acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. Acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent apoptosis. Associates together with TP63 isoform TA*-gamma to the p21/CDKN1A promoter. {ECO:0000269|PubMed:16322561, ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:20959462}.P53708ITA8Integrin alpha-8SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24439109}; Single-pass type I membrane protein {ECO:0000269|PubMed:24439109}. Cell membrane {ECO:0000269|PubMed:24439109}.0brain development [GO:0007420]; cell-matrix adhesion [GO:0007160]; cell projection organization [GO:0030030]; establishment of protein localization [GO:0045184]; extracellular matrix organization [GO:0030198]; inner ear morphogenesis [GO:0042472]; integrin-mediated signaling pathway [GO:0007229]; kidney development [GO:0001822]; memory [GO:0007613]; mesodermal cell differentiation [GO:0048333]; metanephros development [GO:0001656]; positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation [GO:2000721]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; single organismal cell-cell adhesion [GO:0016337]; smooth muscle tissue development [GO:0048745]; substrate adhesion-dependent cell spreading [GO:0034446]Hapical part of cell [GO:0045177]; cell surface [GO:0009986]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; integrin alpha8-beta1 complex [GO:0034678]; integrin complex [GO:0008305]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates< neurite outgrowth of sensory and motor neurons. {ECO:0000269|PubMed:12415008, ECO:0000269|PubMed:15721307}.Q12931TRAP1(Heat shock protein 75 kDa, mitochondrialHSP90SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23564345}. Mitochondrion inner membrane {ECO:0000269|PubMed:23564345}. Mitochondrion matrix {ECO:0000269|PubMed:23564345}.hchaperone-mediated protein folding [GO:0061077]; negative regulation of cellular respiration [GO:1901856]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; response to stress [GO:0006950]; translational attenuation [GO:0009386]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; tumor necrosis factor receptor binding [GO:0005164] extracellular exosome [GO:0070062]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. {ECO:0000269|PubMed:23525905, ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:23747254}.Q6DKK2TTC192Tetratricopeptide repeat protein 19, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody. Note=According to some authors, localizes to the centrosome during all stages of the cell cycle and is recruited to the midbody during cytokinesis (PubMed:20208530). However, the midbody localization could not be confirmed by others (PubMed:21278747). {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:21278747}.[cytokinesis [GO:0000910]; mitochondrial respiratory chain complex III assembly [GO:0034551]tcentrosome [GO:0005813]; midbody [GO:0030496]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]FUNCTION: Mitochondrial protein required for formation of the mitochondrial complex III (PubMed:21278747). May also be required for the abcission step in cytokinesis, possibly regulating the ESCRT-III complex via its interaction with CHMP4B (PubMed:20208530). However, the involvement in cytokinesis requires additional experimental evidence. {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:21278747}.Q15113PCOC1&Procollagen C-endopeptidase enhancer 1multicellular organismal development [GO:0007275]; positive regulation of peptidase activity [GO:0010952]; proteolysis [GO:0006508]fcollagen binding [GO:0005518]; heparin binding [GO:0008201]; peptidase activator activity [GO:0016504]FUNCTION: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity.; FUNCTION: C-terminal processed part of PCPE (CT-PCPE) may have an metalloproteinase inhibitory activity.Q969E4TCAL30Transcription elongation factor A protein-like 3P54259ATN1 Atrophin-10SUBCELLULAR LOCATION: Nucleus. Cytoplasm, perinuclear region. Cell junction {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells (By similarity). Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Asn (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles. {ECO:0000250}.cell migration [GO:0016477]; central nervous system development [GO:0007417]; maintenance of cell polarity [GO:0030011]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron apoptotic process [GO:0051402]; toxin metabolic process [GO:0009404]protein domain specific binding [GO:0019904]; RNA polymerase II transcription coactivator activity [GO:0001105]; transcription corepressor activity [GO:0003714]cell junction [GO:0030054]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity). Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Asn (polyQ) repeats. {ECO:0000250, ECO:0000269|PubMed:10085113, ECO:0000269|PubMed:10973986}.Q92859NEO1Neogeninaxon guidance [GO:0007411]; cell adhesion [GO:0007155]; iron ion homeostasis [GO:0055072]; muscle cell differentiation [GO:0042692]; myoblast fusion [GO:0007520]; negative regulation of protein secretion [GO:0050709]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of muscle cell differentiation [GO:0051149]; regulation of transcription, DNA-templated [GO:0006355]FUNCTION: Multi-functional cell surface receptor regulating cell adhesion in many diverse developmental processes, including neural tube and mammary gland formation, myogenesis and angiogenesis. Receptor for members of the BMP, netrin, and repulsive guidance molecule (RGM) families. Netrin-Neogenin interactions result in a chemoattractive axon guidance response and cell-cell adhesion, the interaction between NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response. {ECO:0000269|PubMed:21149453}.Q13885TBB2ATubulin beta-2A chaincytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; microtubule [GO:0005874]; nucleus [GO:0005634]Q02040AK17AA-kinase anchor protein 17AaSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16982639, ECO:0000269|PubMed:19840947}.B cell activation [GO:0042113]; mRNA processing [GO:0006397]; regulation of RNA splicing [GO:0043484]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]hnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein kinase A binding [GO:0051018]FUNCTION: Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner. {ECO:0000269|PubMed:16982639, ECO:0000269|PubMed:19840947}.Q8N4Q1MIA40@Mitochondrial intermembrane space import and assembly protein 40sSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:16185709, ECO:0000269|PubMed:23186364}.de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; protein import into mitochondrial intermembrane space [GO:0045041]; protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]6protein disulfide oxidoreductase activity [GO:0015035]Jmitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]7FUNCTION: Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. {ECO:0000269|PubMed:16185709, ECO:0000269|PubMed:19182799, ECO:0000269|Pu< bMed:21059946, ECO:0000269|PubMed:23186364}.Q96D53ADCK4'AarF domain-containing protein kinase 4SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:24270420}; Single-pass membrane protein {ECO:0000269|PubMed:24270420}. Cytoplasm, cytosol {ECO:0000269|PubMed:24270420}. Cell membrane {ECO:0000269|PubMed:24270420}.5protein serine/threonine kinase activity [GO:0004674]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]FUNCTION: May play a role in CoQ10 (COQ10A and/or COQ10B) biosynthesis, which is required for podocyte migration. {ECO:0000269|PubMed:24270420}.Q8TCG5CPT1C1Carnitine O-palmitoyltransferase 1, brain isoformSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite {ECO:0000269|PubMed:25751282}. Cell projection, axon {ECO:0000269|PubMed:25751282}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8BGD5}. Note=Localized in the soma and dendritic and axonal projections. {ECO:0000269|PubMed:25751282}.Pcarnitine metabolic process [GO:0009437]; fatty acid beta-oxidation [GO:0006635]Balpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex [GO:0032281]; axon [GO:0030424]; cell junction [GO:0030054]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; synapse [GO:0045202]TFUNCTION: May play a role in lipid metabolic process. {ECO:0000269|PubMed:25751282}.P50148GNAQ5Guanine nucleotide-binding protein G(q) subunit alphaSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Nucleus membrane {ECO:0000250}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250}.Iaction potential [GO:0001508]; activation of phospholipase C activity [GO:0007202]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; blood coagulation [GO:0007596]; developmental pigmentation [GO:0048066]; embryonic digit morphogenesis [GO:0042733]; entrainment of circadian clock [GO:0009649]; forebrain neuron development [GO:0021884]; glutamate receptor signaling pathway [GO:0007215]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; heart development [GO:0007507]; maternal behavior [GO:0042711]; negative regulation of protein kinase activity [GO:0006469]; neuron remodeling [GO:0016322]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; phototransduction, visible light [GO:0007603]; platelet activation [GO:0030168]; positive regulation of GTPase activity [GO:0043547]; post-embryonic development [GO:0009791]; protein stabilization [GO:0050821]; regulation of catenin import into nucleus [GO:0035412]; regulation of melanocyte differentiation [GO:0045634]; skeletal system development [GO:0001501]G-protein beta/gamma-subunit complex binding [GO:0031683]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]; type 2A serotonin receptor binding [GO:0031826]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; lysosomal membrane [GO:0005765]; nuclear membrane [GO:0031965]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]`FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). {ECO:0000250}.O75880SCO1#Protein SCO1 homolog, mitochondrialASUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9878253}.cellular copper ion homeostasis [GO:0006878]; copper ion transport [GO:0006825]; generation of precursor metabolites and energy [GO:0006091]; respiratory chain complex IV assembly [GO:0008535]]mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myofibril [GO:0030016]FUNCTION: Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. {ECO:0000269|PubMed:15659396, ECO:0000269|PubMed:16735468, ECO:0000269|PubMed:17189203}.Q9H8H0NOL11Nucleolar protein 11dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22916032}.maturation of SSU-rRNA [GO:0030490]; positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter [GO:1901838]; transcription, DNA-templated [GO:0006351]2nucleolus [GO:0005730]; t-UTP complex [GO:0034455]FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. {ECO:0000269|PubMed:22916032}.P05186PPBT0Alkaline phosphatase, tissue-nonspecific isozymecellular response to organic cyclic compound [GO:0071407]; cementum mineralization [GO:0071529]; developmental process involved in reproduction [GO:0003006]; endochondral ossification [GO:0001958]; osteoblast differentiation [GO:0001649]; response to antibiotic [GO:0046677]; response to glucocorticoid [GO:0051384]; response to lipopolysaccharide [GO:0032496]; response to vitamin D [GO:0033280]; skeletal system development [GO:0001501]qalkaline phosphatase activity [GO:0004035]; metal ion binding [GO:0046872]; pyrophosphatase activity [GO:0016462]anchored component of membrane [GO:0031225]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]BFUNCTION: This isozyme may play a role in skeletal mineralization.P50479PDLI4PDZ and LIM domain protein 4Q9H3Q1BORG4Cdc42 effector protein 4`SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Cytoplasm, cytoskeleton.positive regulation of actin filament polymerization [GO:0030838]; positive regulation of GTPase activity [GO:0043547]; positive regulation of pseudopodium assembly [GO:0031274]; regulation of cell shape [GO:0008360]; Rho protein signal transduction [GO:0007266]fGTPase activator activity [GO:0005096]; GTP-Rho binding [GO:0017049]; poly(A) RNA binding [GO:0044822]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.Q9H7B4SMYD3(Histone-lysine N-methyltransferase SMYD3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15235609}. Nucleus {ECO:0000269|PubMed:15235609}. Note=Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M.#chromatin organization [GO:0006325]Xhistone-lysine N-methyltransferase activity [GO:0018024]; metal ion binding [GO:0046872]sFUNCTION: Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences. {ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:22419068}.Q92888ARHG1(Rho guanine nucleotide exchange factor 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10747909}. Membrane {ECO:0000269|PubMed:10747909}. Note=Translocated to the membrane by activated GNA13 or LPA stimulation.cell proliferation [GO:0008283]; negative regulation of axonogenesis [GO:0050771]; neurotrophin TRK receptor sign< aling pathway [GO:0048011]; positive regulation of GTPase activity [GO:0043547]; regulation of axonogenesis [GO:0050770]; regulation of Rho protein signal transduction [GO:0035023]; Rho protein signal transduction [GO:0007266]; termination of G-protein coupled receptor signaling pathway [GO:0038032]GTPase activator activity [GO:0005096]; poly(A) RNA binding [GO:0044822]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]Jcytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]TFUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation. {ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:8810315, ECO:0000269|PubMed:9641915, ECO:0000269|PubMed:9641916}.Q9Y230RUVB2 RuvB-like 2SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes.cellular response to estradiol stimulus [GO:0071392]; cellular response to UV [GO:0034644]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; establishment of protein localization to chromatin [GO:0071169]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; negative regulation of estrogen receptor binding [GO:0071899]; positive regulation of histone acetylation [GO:0035066]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein folding [GO:0006457]; regulation of growth [GO:0040008]; transcription, DNA-templated [GO:0006351]; transcriptional activation by promoter-enhancer looping [GO:0071733]ATP binding [GO:0005524]; ATP-dependent 5'-3' DNA helicase activity [GO:0043141]; ATP-dependent DNA helicase activity [GO:0004003]; chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; identical protein binding [GO:0042802]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Ino80 complex [GO:0031011]; intracellular [GO:0005622]; membrane [GO:0016020]; MLL1 complex [GO:0071339]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear euchromatin [GO:0005719]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; Swr1 complex [GO:0000812])FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; FUNCTION: Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2.Q8TF66LRC15)Leucine-rich repeat-containing protein 15negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; positive regulation of cell migration [GO:0030335]; receptor-mediated virion attachment to host cell [GO:0046813]]collagen binding [GO:0005518]; fibronectin binding [GO:0001968]; laminin binding [GO:0043236]kextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]Q8TE02ELP5Elongator complex protein 5chromatin organization [GO:0006325]; positive regulation of cell migration [GO:0030335]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]Wcytoplasm [GO:0005737]; Elongator holoenzyme complex [GO:0033588]; nucleus [GO:0005634]FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration (By similarity). May be involved in TP53-mediated transcriptional regulation. {ECO:0000250, ECO:0000269|PubMed:16850183}.Q5W111SPRY7 SPRY domain-containing protein 7Q9Y265RUVB1 RuvB-like 1oSUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in the cytoplasm and associated with the cell membranes. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells.cell division [GO:0051301]; CENP-A containing nucleosome assembly [GO:0034080]; chromatin organization [GO:0006325]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; mitotic nuclear division [GO:0007067]; nucleosome assembly [GO:0006334]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of growth [GO:0040008]; regulation of mitochondrion degradation [GO:1903146]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]<ATP binding [GO:0005524]; DNA helicase activity [GO:0003678]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Ino80 complex [GO:0031011]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; MLL1 complex [GO:0071339]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Swr1 complex [GO:0000812]sFUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunit< s in the ring-like structure contribute to the ATPase activity.; FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; FUNCTION: Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation.; FUNCTION: May be able to bind plasminogen at cell surface and enhance plasminogen activation.Q9UJZ1STML2&Stomatin-like protein 2, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane. Mitochondrion intermembrane space. Cell membrane; Peripheral membrane protein. Membrane raft; Peripheral membrane protein. Note=Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells.CD4-positive, alpha-beta T cell activation [GO:0035710]; cellular calcium ion homeostasis [GO:0006874]; interleukin-2 production [GO:0032623]; lipid localization [GO:0010876]; mitochondrial ATP synthesis coupled proton transport [GO:0042776]; mitochondrial calcium ion transport [GO:0006851]; mitochondrial protein processing [GO:0034982]; mitochondrion organization [GO:0007005]; positive regulation of cardiolipin metabolic process [GO:1900210]; positive regulation of mitochondrial DNA replication [GO:0090297]; positive regulation of mitochondrial membrane potential [GO:0010918]; protein oligomerization [GO:0051259]; stress-induced mitochondrial fusion [GO:1990046]; T cell receptor signaling pathway [GO:0050852]\cardiolipin binding [GO:1901612]; GTPase binding [GO:0051020]; receptor binding [GO:0005102]cytoskeleton [GO:0005856]; extrinsic component of plasma membrane [GO:0019897]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]FUNCTION: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation. {ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:19597348, ECO:0000269|PubMed:19944461, ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.P31749AKT1)RAC-alpha serine/threonine-protein kinaseSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A. Phosphorylation on Tyr-176 by TNK2 results in its localization to the cell membrane where it is targeted for further phosphorylations on Thr-308 and Ser-473 leading to its activation and the activated form translocates to the nucleus.activation-induced cell death of T cells [GO:0006924]; aging [GO:0007568]; apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cell projection organization [GO:0030030]; cell proliferation [GO:0008283]; cellular protein modification process [GO:0006464]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to mechanical stimulus [GO:0071260]; cellular response to organic cyclic compound [GO:0071407]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endocrine pancreas development [GO:0031018]; epidermal growth factor receptor signaling pathway [GO:0007173]; execution phase of apoptosis [GO:0097194]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; germ cell development [GO:0007281]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glucose transport [GO:0015758]; glycogen biosynthetic process [GO:0005978]; glycogen cell differentiation involved in embryonic placenta development [GO:0060709]; G-protein coupled receptor signaling pathway [GO:0007186]; hyaluronan metabolic process [GO:0030212]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway [GO:0097193]; labyrinthine layer blood vessel development [GO:0060716]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; mammary gland epithelial cell differentiation [GO:0060644]; maternal placenta development [GO:0001893]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of cell size [GO:0045792]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of JNK cascade [GO:0046329]; negative regulation of neuron death [GO:1901215]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of plasma membrane long-chain fatty acid transport [GO:0010748]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of proteolysis [GO:0045861]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neurotrophin TRK receptor signaling pathway [GO:0048011]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide metabolic process [GO:0046209]; osteoblast differentiation [GO:0001649]; peptidyl-serine phosphorylation [GO:0018105]; peripheral nervous system myelin maintenance [GO:0032287]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; platelet activation [GO:0030168]; positive regulation of blood vessel endothelial cell migration [G< O:0043536]; positive regulation of cell growth [GO:0030307]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of glucose import [GO:0046326]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of sodium ion transport [GO:0010765]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of vasoconstriction [GO:0045907]; programmed cell death [GO:0012501]; protein autophosphorylation [GO:0046777]; protein catabolic process [GO:0030163]; protein import into nucleus, translocation [GO:0000060]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; protein ubiquitination [GO:0016567]; regulation of cell cycle checkpoint [GO:1901976]; regulation of cell migration [GO:0030334]; regulation of glycogen biosynthetic process [GO:0005979]; regulation of myelination [GO:0031641]; regulation of neuron projection development [GO:0010975]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of translation [GO:0006417]; response to fluid shear stress [GO:0034405]; response to food [GO:0032094]; response to growth hormone [GO:0060416]; response to heat [GO:0009408]; response to insulin-like growth factor stimulus [GO:1990418]; response to oxidative stress [GO:0006979]; response to UV-A [GO:0070141]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; striated muscle cell differentiation [GO:0051146]; T cell costimulation [GO:0031295]; transcription initiation from RNA polymerase II promoter [GO:0006367]; translation [GO:0006412]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; nitric-oxide synthase regulator activity [GO:0030235]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; protein kinase activity [GO:0004672]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein serine/threonine kinase activity [GO:0004674]3cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; spindle [GO:0005819]5FUNCTION: AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53.; FUNCTION: AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A< , for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation.O94985CSTN1 Calsyntenin-1nSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein {ECO:0000269|PubMed:17332754}. Golgi apparatus membrane {ECO:0000269|PubMed:17332754}. Cell projection {ECO:0000269|PubMed:17332754}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17332754}. Note=Neurite tips. Localized in the postsynaptic membrane of both excitatory and inhibitory synapses (By similarity). The AlcICD fragment is translocated to the nucleus upon interaction with APBB1. {ECO:0000250}.cell adhesion [GO:0007155]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission [GO:0050806]; regulation of cell growth [GO:0001558]beta-amyloid binding [GO:0001540]; calcium ion binding [GO:0005509]; kinesin binding [GO:0019894]; X11-like protein binding [GO:0042988]6cell junction [GO:0030054]; cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; neuronal postsynaptic density [GO:0097481]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211]FUNCTION: Induces KLC1 association with vesicles and functions as a cargo in axonal anterograde transport. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP. The intracellular fragment AlcICD suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1-binding. May modulate calcium-mediated postsynaptic signals (By similarity). {ECO:0000250}.Q99717SMAD5)Mothers against decapentaplegic homolog 5SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4.BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; cardiac muscle contraction [GO:0060048]; cartilage development [GO:0051216]; cellular response to BMP stimulus [GO:0071773]; cellular response to organic cyclic compound [GO:0071407]; embryonic pattern specification [GO:0009880]; erythrocyte differentiation [GO:0030218]; germ cell development [GO:0007281]; intracellular signal transduction [GO:0035556]; Mullerian duct regression [GO:0001880]; osteoblast fate commitment [GO:0002051]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus [GO:1901522]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]; SMAD protein signal transduction [GO:0060395]; transcription, DNA-templated [GO:0006351]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]|metal ion binding [GO:0046872]; receptor signaling protein activity [GO:0005057]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity [GO:0030618]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; SMAD protein complex [GO:0071141]; transcription factor complex [GO:0005667]FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD).Q96DA6TIM14=Mitochondrial import inner membrane translocase subunit TIM14SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12592411}; Single-pass membrane protein {ECO:0000305|PubMed:12592411}..cellular protein metabolic process [GO:0044267]; genitalia development [GO:0048806]; positive regulation of ATPase activity [GO:0032781]; protein folding [GO:0006457]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]; visual perception [GO:0007601]&ATPase activator activity [GO:0001671]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; presequence translocase-associated import motor [GO:0001405]; protein complex [GO:0043234]6FUNCTION: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity). {ECO:0000250}.Q8NDV7TNR6A/Trinucleotide repeat-containing gene 6A proteinSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:11950943, ECO:0000269|PubMed:13130130, ECO:0000269|PubMed:15494374, ECO:0000269|PubMed:15908945, ECO:0000269|PubMed:16284622, ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:18946079, ECO:0000269|PubMed:19056672, ECO:0000269|PubMed:19324964}. Note=Mammalian P-bodies are also known as GW bodies (GWBs).hcellular response to starvation [GO:0009267]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; gene silencing by miRNA [GO:0035195]; innate immune response [GO:0045087]; negative regulation of translation involved in gene silencing by miRNA [GO:0035278]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; phosphatidylinositol-mediated signaling [GO:0048015]; posttranscriptional gene silencing [GO:0016441]cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; micro-ribonucleoprotein complex [GO:0035068]; nucleoplasm [GO:0005654]jFUNCTION: Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent repression of translation and for siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes. {ECO:0000269|PubMed:16284622, ECO:0000269|PubMed:16284623, ECO:0000269|PubMed:17596515, ECO:0000269|PubMed:17671087, ECO:0000269|PubMed:19056672, ECO:0000269|PubMed:19304925}.Q5T2E6CJ076UPF0668 protein C10orf76O00459P85B5Phosphatidylinositol 3-kinase regulatory subunit betaWblood coagulation [GO:0007596]; cellular glucose homeostasis [GO:0001678]; cellular response to insulin stimulus [GO:0032869]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; leukocyte migration [GO:0050900]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-3-phosphate bios< ynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein transport [GO:0015031]; regulation of autophagy [GO:0010506]; regulation of phosphatidylinositol 3-kinase activity [GO:0043551]; regulation of small GTPase mediated signal transduction [GO:0051056]; response to endoplasmic reticulum stress [GO:0034976]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; receptor tyrosine kinase binding [GO:0030971]^cytosol [GO:0005829]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (PubMed:23604317). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity). {ECO:0000250|UniProtKB:O08908, ECO:0000269|PubMed:23604317}.Q13190STX5 Syntaxin-5)SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Localizes throughout the Golgi apparatus, but most abundant in the cis-most cisternae. {ECO:0000250}.early endosome to Golgi transport [GO:0034498]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi disassembly [GO:0090166]; intracellular protein transport [GO:0006886]; positive regulation of protein catabolic process [GO:0045732]; regulation of Golgi organization [GO:1903358]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle fusion with Golgi apparatus [GO:0048280]hprotein N-terminus binding [GO:0047485]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]Dendomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201]; vesicle [GO:0031982]KFUNCTION: Mediates endoplasmic reticulum to Golgi transport. {ECO:0000250}.Q9BPY8HOPHomeodomain-only proteinESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.Bheart development [GO:0007507]; histone deacetylation [GO:0016575]; lung alveolus development [GO:0048286]; negative regulation of cell differentiation [GO:0045596]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of skeletal muscle tissue regeneration [GO:0043415]; positive regulation of striated muscle cell differentiation [GO:0051155]; regulation of heart contraction [GO:0008016]; regulation of protein binding [GO:0043393]; transcription, DNA-templated [GO:0006351]; trophectodermal cell differentiation [GO:0001829]FUNCTION: Atypical homeodomain protein which does not bind DNA and is required to modulate cardiac growth and development. Acts via its interaction with SRF, thereby modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. Prevents SRF-dependent transcription either by inhibiting SRF binding to DNA or by recruiting histone deacetylase (HDAC) proteins that prevent transcription by SRF. Overexpression causes cardiac hypertrophy (By similarity). May act as a tumor suppressor. {ECO:0000250}.Q13618CUL3Cullin-3/SUBCELLULAR LOCATION: Nucleus. Golgi apparatus.cell cycle arrest [GO:0007050]; cell migration [GO:0016477]; COPII vesicle coating [GO:0048208]; embryonic cleavage [GO:0040016]; ER to Golgi vesicle-mediated transport [GO:0006888]; fibroblast apoptotic process [GO:0044346]; G1/S transition of mitotic cell cycle [GO:0000082]; gastrulation [GO:0007369]; integrin-mediated signaling pathway [GO:0007229]; intrinsic apoptotic signaling pathway [GO:0097193]; liver morphogenesis [GO:0072576]; mitotic metaphase plate congression [GO:0007080]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cyclin-dependent protein serine/threonine kinase by cyclin degradation [GO:0008054]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; stem cell division [GO:0017145]; stress fiber assembly [GO:0043149]; trophectodermal cellular morphogenesis [GO:0001831]; Wnt signaling pathway [GO:0016055]POZ domain binding [GO:0031208]Cul3-RING ubiquitin ligase complex [GO:0031463]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; polar microtubule [GO:0005827]j FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4. The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it medi< ates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (PubMed:20389280, PubMed:21840486, PubMed:21670212, PubMed:24768539). The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1). Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. {ECO:0000250, ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:11311237, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:23387299, ECO:0000269|PubMed:23453970, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23576762, ECO:0000269|PubMed:24768539}.Q9UFC0LRWD16Leucine-rich repeat and WD repeat-containing protein 1SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, telomere. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes to heterochromatin during G1 phase. Restricted to centromeres or telomeres as cells progress though S phase. When cells enter mitosis, relocalizes to centromeres. Recruitment to pericentric heterochromatin largely depends on the presence of H3K9me3.chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; DNA replication initiation [GO:0006270]; establishment of protein localization to chromatin [GO:0071169]hchromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; methyl-CpG binding [GO:0008327]cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nuclear origin of replication recognition complex [GO:0005664]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; telomeric heterochromatin [GO:0031933]FUNCTION: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. {ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:20932478, ECO:0000269|PubMed:21029866, ECO:0000269|PubMed:22427655, ECO:0000269|PubMed:22645314}.O95456PSMG1Proteasome assembly chaperone 17SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum.cerebellar granule cell precursor proliferation [GO:0021930]; proteasome assembly [GO:0043248]; proteasome core complex assembly [GO:0080129]Pcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]vFUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.Q9GZZ1NAA50N-alpha-acetyltransferase 50>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16507339}.histone H4 acetylation [GO:0043967]; mitotic sister chromatid cohesion, centromeric [GO:0071962]; N-terminal protein amino acid acetylation [GO:0006474]H4 histone acetyltransferase activity [GO:0010485]; peptide alpha-N-acetyltransferase activity [GO:0004596]; peptidyl-lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0052858]FUNCTION: Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity. {ECO:0000269|PubMed:16507339}.Q96ED9HOOK2Protein Hook homolog 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cytoplasm, cytoskeleton. Note=Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome. Also localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, the Golgi complex, multivesicular bodies (MVBs), lysosomes, or mitochondria. Often found in close association with microtubules.early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; lysosome organization [GO:0007040]; protein transport [GO:0015031]Kcentrosome [GO:0005813]; FHF complex [GO:0070695]; microtubule [GO:0005874] FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Contributes to the establishment and maintenance of centrosome function. May function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. {ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:17540036, ECO:0000269|PubMed:18799622}.Q01081U2AF1#Splicing factor U2AF 35 kDa subunitkSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15096518}. Nucleus speckle {ECO:0000269|PubMed:15096518}.gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of mitochondrion degradation [GO:1903146]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]FUNCTION: Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron. {ECO:0000269|PubMed:8647433}.P49810PSN2 Presenilin-2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8574969}; Multi-pass membrane protein {ECO:0000269|PubMed:8574969}. Golgi apparatus membrane {ECO:0000269|PubMed:8574969}; Multi-pass membrane protein {ECO:0000269|PubMed:8574969}.amyloid precursor protein catabolic process [GO:0042987]; apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; beta-amyloid metabolic process [GO:0050435]; brain morphogenesis [GO:0048854]; calcium ion transport [GO:0006816]; cardiac muscle contraction [GO:0060048]; cell fate specification [GO:0001708]; dorsal/ventral neural tube patterning [GO:0021904]; embryonic limb morphogenesis [GO:0030326]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; ephrin receptor signaling pathway [GO:0048013]; forebrain development < [GO:0030900]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; intracellular signal transduction [GO:0035556]; lung alveolus development [GO:0048286]; membrane protein ectodomain proteolysis [GO:0006509]; membrane protein intracellular domain proteolysis [GO:0031293]; memory [GO:0007613]; myeloid leukocyte differentiation [GO:0002573]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of protein binding [GO:0032091]; negative regulation of protein complex assembly [GO:0031333]; negative regulation of protein phosphorylation [GO:0001933]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; positive regulation of coagulation [GO:0050820]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation of epidermal growth factor-activated receptor activity [GO:0007176]; regulation of synaptic plasticity [GO:0048167]; somitogenesis [GO:0001756]; T cell activation involved in immune response [GO:0002286]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]Vaspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]japical plasma membrane [GO:0016324]; axon [GO:0030424]; cell cortex [GO:0005938]; cell surface [GO:0009986]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; integral component of plasma membrane [GO:0005887]; kinetochore [GO:0000776]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; Z disc [GO:0030018]#FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. {ECO:0000269|PubMed:10497236, ECO:0000269|PubMed:10652302}.Q5MNZ6WIPI37WD repeat domain phosphoinositide-interacting protein 3autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; protein lipidation [GO:0006497]; protein localization to pre-autophagosomal structure [GO:0034497]qphosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]vcytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; pre-autophagosomal structure membrane [GO:0034045]Q14142TRI14&Tripartite motif-containing protein 14 innate immune response [GO:0045087]; negative regulation of viral transcription [GO:0032897]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]bFUNCTION: Inhibits the transcriptional activity of SPI1 in a dose-dependent manner. {ECO:0000250}.P05771KPCBProtein kinase C beta typeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20228790}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}..apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; blood coagulation [GO:0007596]; calcium ion transport [GO:0006816]; cellular calcium ion homeostasis [GO:0006874]; cellular response to carbohydrate stimulus [GO:0071322]; histone H3-T6 phosphorylation [GO:0035408]; intracellular signal transduction [GO:0035556]; lipoprotein transport [GO:0042953]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; negative regulation of glucose transport [GO:0010829]; negative regulation of insulin receptor signaling pathway [GO:0046627]; platelet activation [GO:0030168]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; protein phosphorylation [GO:0006468]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; synaptic transmission [GO:0007268]; transcription, DNA-templated [GO:0006351]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]androgen receptor binding [GO:0050681]; ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; histone binding [GO:0042393]; histone kinase activity (H3-T6 specific) [GO:0035403]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; protein kinase C activity [GO:0004697]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]a FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endoth< elial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. {ECO:0000250, ECO:0000269|PubMed:11598012, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20228790}.Q9UMS0NFU18NFU1 iron-sulfur cluster scaffold homolog, mitochondrial8SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm, cytosol.L4 iron, 4 sulfur cluster binding [GO:0051539]; iron ion binding [GO:0005506]xcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Iron-sulfur cluster scaffold protein which can assemble [4Fe-2S] clusters and deliver them to target proteins. {ECO:0000269|PubMed:12886008}.Q96B36AKTS1Proline-rich AKT1 substrate 1mTORySUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Note=Found in the cytosolic fraction of the brain. {ECO:0000250}.|cellular response to heat [GO:0034605]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; negative regulation of cell size [GO:0045792]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of TOR signaling [GO:0032007]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; regulation of cellular response to heat [GO:1900034]; regulation of neuron apoptotic process [GO:0043523]dcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]LFUNCTION: Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection. {ECO:0000269|PubMed:16174443, ECO:0000269|PubMed:17277771, ECO:0000269|PubMed:17386266}.Q9Y2I1NISCH NischarinySUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Early endosome. Recycling endosome. Note=Enriched in the early/sorting and recycling endosomes. Colocalized in early/sorting endosomes with EEA1 and SNX2 and in recycling endosomes with transferrin receptor. Detected in the perinuclear region partially associated with punctate structures (By similarity). Colocalizes with PAK1 in cytoplasm, vesicular structures in the perinuclear area and membrane ruffles (By similarity). Colocalizes with RAC1 in the cytoplasm and vesicles structures (By similarity). Colocalized with MAPK1 and MAPK3 in RVLM neurons (By similarity). {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; apoptotic process [GO:0006915]; glucose metabolic process [GO:0006006]; G-protein coupled receptor signaling pathway [GO:0007186]; negative regulation of cell migration [GO:0030336]; norepinephrine secretion [GO:0048243]; Rac protein signal transduction [GO:0016601]; regulation of blood pressure [GO:0008217]; regulation of synaptic transmission, GABAergic [GO:0032228]cytosol [GO:0005829]; early endosome [GO:0005769]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]FUNCTION: Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension (By similarity). Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons (By similarity). Acts as a modulator of Rac-regulated signal transduction pathways (By similarity). Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity (By similarity). Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation (By similarity). Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation (By similarity). Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells (By similarity). Inhibits lamellipodia formation, when overexpressed (By similarity). Plays a role in protection against apoptosis. Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3. When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures. {ECO:0000250, ECO:0000269|PubMed:10882231, ECO:0000269|PubMed:12868002, ECO:0000269|PubMed:15028619, ECO:0000269|PubMed:15028621, ECO:0000269|PubMed:15475348}.Q9P1T7MDFIC/MyoD family inhibitor domain-containing protein5SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Note=Also shows a granular distribution in the cytoplasm.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:11139147, ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749}. Note=Weak expression in the nucleus.activation of JUN kinase activity [GO:0007257]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of viral transcription [GO:0050434]; regulation of Wnt signaling pathway [GO:0030111]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]hcyclin binding [GO:0030332]; Tat protein binding [GO:0030957]; transcription factor binding [GO:0008134]|cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]rFUNCTION: Acts as a transcriptional activator or repressor. Inhibits the transcriptional activation of Zic family proteins ZIC1, ZIC2 and ZIC3. Retains nuclear Zic proteins ZIC1, ZIC2 and ZIC3 in the cytoplasm. Modulates the expression from both cellular and viral promoters. Down-regulates Tat-dependent transcription of the human immunodeficiency virus type 1 (HIV-1) LTR by interacting with HIV-1 Tat and Rev and impairing their nuclear import, probably by rendering the NLS domains inaccessible to importin-beta. Also stimulates activation of human T-cell leukemia virus type I (HTLV-I) LTR. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways. {ECO:0000269|PubMed:10671520, ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:12944466, ECO:0000269|PubMed:16260749, ECO:0000269|Ref.6}.Q99729ROAA+Heterogeneous nuclear ribonucleoprotein A/BSUBCELLULAR< LOCATION: Nucleus {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.epithelial to mesenchymal transition [GO:0001837]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription, DNA-templated [GO:0045893]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; RNA polymerase II transcription factor complex [GO:0090575]FUNCTION: Binds single-stranded RNA. Has a high affinity for G-rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site.Q15058KIF14Kinesin-like protein KIF14iSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16431929}. Cytoplasm {ECO:0000269|PubMed:16648480}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16431929}. Midbody {ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:20309963}. Note=Nuclear localization observed during interphase (PubMed:16431929). Nuclear localization triggered by entry into mitosis (PubMed:16648480). Cytoplasmic in interphase (PubMed:16648480). Cytoplasmic in metaphase cells (PubMed:16431929). From prophase to metaphase, accumulates at the developing spindle poles and their associated microtubules. During anaphase, accumulates at the spindle midzone. Localization to the central spindle and midbody during anaphase is dependent upon PRC1 and CIT presence. In cells ready to undergo abscission, concentrates at the contractile ring. {ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480}.activation of protein kinase activity [GO:0032147]; cell division [GO:0051301]; cell proliferation in forebrain [GO:0021846]; cerebellar cortex development [GO:0021695]; cerebellar granular layer structural organization [GO:0021685]; cerebellar Purkinje cell layer structural organization [GO:0021693]; cerebral cortex development [GO:0021987]; cytoskeleton-dependent intracellular transport [GO:0030705]; establishment of protein localization [GO:0045184]; hippocampus development [GO:0021766]; microtubule-based movement [GO:0007018]; mitotic cell cycle process [GO:1903047]; mitotic metaphase plate congression [GO:0007080]; negative regulation of apoptotic process [GO:0043066]; negative regulation of integrin activation [GO:0033624]; negative regulation of neuron apoptotic process [GO:0043524]; olfactory bulb development [GO:0021772]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cytokinesis [GO:0032467]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell adhesion [GO:0030155]; regulation of cell growth [GO:0001558]; regulation of cell maturation [GO:1903429]; regulation of cell migration [GO:0030334]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of myelination [GO:0031641]; regulation of neuron apoptotic process [GO:0043523]; regulation of Rap protein signal transduction [GO:0032487]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; small GTPase mediated signal transduction [GO:0007264]; substrate adhesion-dependent cell spreading [GO:0034446]/ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; PDZ domain binding [GO:0030165]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631]cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle midzone [GO:0051233]FUNCTION: Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:24784001, PubMed:16648480). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250|UniProtKB:L0N7N1, ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480, ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001, ECO:0000269|PubMed:24854087}.Q9UNZ5L10K(Leydig cell tumor 10 kDa protein homologRFUNCTION: May have a potential role in hypercalcemia of malignancy. {ECO:0000250}.Q7L576CYFP1&Cytoplasmic FMR1-interacting protein 1wSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Highly expressed in the perinuclear region. Enriched in synaptosomes, membrane ruffles and at the tips of lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.axon extension [GO:0048675]; cognition [GO:0050890]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; lamellipodium assembly [GO:0030032]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; Rac protein signal transduction [GO:0016601]; regulation of cell shape [GO:0008360]; ruffle organization [GO:0031529]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]jactin filament binding [GO:0051015]; protein complex binding [GO:0032403]; Rac GTPase binding [GO:0048365],cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; mRNA cap binding complex [GO:0005845]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]; SCAR complex [GO:0031209]; synapse [GO:0045202]IFUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. {ECO:0000250, ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508, ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}.Q86U42PABP2Polyadenylate-binding protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10688363, ECO:0000269|PubMed:11001936, ECO:0000269|PubMed:14663186, ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. Its nuclear import may involve the nucleocytoplasmic transport receptor transportin and a RAN-GTP-sensitive import mechanism. Is exported to the cytoplas< m by a carrier-mediated pathway that is independent of mRNA traffic. Nucleus; nuclear speckle. Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By similarity). {ECO:0000250}.@gene expression [GO:0010467]; modification by virus of host mRNA processing [GO:0046778]; modulation by virus of host morphology or physiology [GO:0019048]; modulation by virus of host process [GO:0019054]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; muscle contraction [GO:0006936]; poly(A)+ mRNA export from nucleus [GO:0016973]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]; viral life cycle [GO:0019058]cytoplasm [GO:0005737]; nuclear inclusion body [GO:0042405]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity). {ECO:0000250}.Q9H1A4APC1$Anaphase-promoting complex subunit 1Wanaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]P35573GDEGlycogen debranching enzyme}SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17908927}. Note=Under glycogenolytic conditions localizes to the nucleus.#carbohydrate metabolic process [GO:0005975]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; response to glucocorticoid [GO:0051384]; response to nutrient [GO:0007584]; small molecule metabolic process [GO:0044281]4-alpha-glucanotransferase activity [GO:0004134]; amylo-alpha-1,6-glucosidase activity [GO:0004135]; glycogen debranching enzyme activity [GO:0004133]; polysaccharide binding [GO:0030247]cytoplasm [GO:0005737]; cytosol [GO:0005829]; inclusion body [GO:0016234]; isoamylase complex [GO:0043033]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.Q9Y3A2UTP115Probable U3 small nucleolar RNA-associated protein 11|nervous system development [GO:0007399]; positive regulation of apoptotic process [GO:0043065]; rRNA processing [GO:0006364]wcytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]SFUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000250}.Q9NPJ3ACO13Acyl-coenzyme A thioesterase 13BSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin (By similarity). {ECO:0000250}.(protein homotetramerization [GO:0051289](acyl-CoA hydrolase activity [GO:0047617]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; spindle [GO:0005819] FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity). {ECO:0000250}.Q71U36TBA1ATubulin alpha-1A chainde novo' posttranslational protein folding [GO:0051084]; cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cytoskeleton-dependent intracellular transport [GO:0030705]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; protein folding [GO:0006457]; protein polymerization [GO:0051258]cytoplasmic microtubule [GO:0005881]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; recycling endosome [GO:0055037]Q9BPZ7SIN1-Target of rapamycin complex 2 subunit MAPKAP1_SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasmic vesicle. Nucleus.)epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; negative regulation of Ras protein signal transduction [GO:0046580]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; substantia nigra development [GO:0021762]; T cell costimulation [GO:0031295]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]_phosphatidic acid binding [GO:0070300]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase binding [GO:0019901]; Ras GTPase binding [GO:0017016]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]GFUNCTION: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. {ECO:0000269|PubMed:15988011, ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:17043309, ECO:0000269|PubMed:17054722, ECO:0000269|PubMed:17303383, ECO:0000269|PubMed:23727834}.Q9Y5P4C43BP(Collagen type IV alpha-3-binding proteinkSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Golgi apparatus {ECO:0000269|PubMed:14685229, ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Endoplasmic reticulum {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Note=Preferentially localized to the Golgi apparatus. {ECO:0000305|PubMed:16895911}.cell morphogenesis [GO:0000902]; cell proliferation [GO:0008283< ]; ceramide metabolic process [GO:0006672]; endoplasmic reticulum organization [GO:0007029]; ER to Golgi ceramide transport [GO:0035621]; heart morphogenesis [GO:0003007]; immune response [GO:0006955]; in utero embryonic development [GO:0001701]; lipid homeostasis [GO:0055088]; mitochondrion morphogenesis [GO:0070584]; muscle contraction [GO:0006936]; protein phosphorylation [GO:0006468]; response to endoplasmic reticulum stress [GO:0034976]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]ceramide binding [GO:0097001]; ceramide transporter activity [GO:0035620]; phosphatidylinositol-4-phosphate binding [GO:0070273]; protein kinase activity [GO:0004672]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]1FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. {ECO:0000269|PubMed:14685229, ECO:0000269|PubMed:17591919, ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:20036255}.Q16832DDR2&Discoidin domain-containing receptor 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}; Single-pass type I membrane protein {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}.biomineral tissue development [GO:0031214]; cell adhesion [GO:0007155]; chondrocyte proliferation [GO:0035988]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; collagen fibril organization [GO:0030199]; endochondral bone growth [GO:0003416]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of extracellular matrix disassembly [GO:0090091]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein autophosphorylation [GO:0046777]; regulation of bone mineralization [GO:0030500]; regulation of extracellular matrix disassembly [GO:0010715]; signal transduction [GO:0007165]ATP binding [GO:0005524]; collagen binding [GO:0005518]; protein tyrosine kinase collagen receptor activity [GO:0038062]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. {ECO:0000269|PubMed:16186104, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:17665456, ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20004161, ECO:0000269|PubMed:20564243, ECO:0000269|PubMed:20734453, ECO:0000269|PubMed:9659899}.Q9UKA4AKA11A-kinase anchor protein 118SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in premeiotic pachytene spermatocytes and in the centrosome of developing postmeiotic germ cells, while a midpiece/centrosome localization was found in elongating spermatocytes and mature sperm.eintracellular signal transduction [GO:0035556]; regulation of protein kinase A signaling [GO:0010738]Qprotein kinase A binding [GO:0051018]; protein phosphatase 1 binding [GO:0008157]ycytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; peroxisome [GO:0005777]; protein complex [GO:0043234]\FUNCTION: Binds to type II regulatory subunits of protein kinase A and anchors/targets them.Q9NW97TMM51Transmembrane protein 51Q8N183MIMITMimitin, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15774466}.negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; reactive oxygen species metabolic process [GO:0072593]; respiratory electron transport chain [GO:0022904]lFUNCTION: Acts as a molecular chaperone for mitochondrial complex I assembly. {ECO:0000269|PubMed:16200211}.Q4G0F5VP26B/Vacuolar protein sorting-associated protein 26BISUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C0E2}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C0E2}. Early endosome {ECO:0000250|UniProtKB:Q8C0E2}. Late endosome {ECO:0000250|UniProtKB:Q8C0E2}. Note=Localizes to early and late endosomal structures (By similarity). {ECO:0000250|UniProtKB:Q8C0E2}.bintracellular protein transport [GO:0006886]; retrograde transport, endosome to Golgi [GO:0042147]cytosol [GO:0005829]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; retromer complex [GO:0030904]yFUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity). {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}.Q9NVC6MED176Mediator of RNA polymerase II transcription subunit 17androgen receptor signaling pathway [GO:0030521]; gene expression [GO:0010467]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; stem cell maintenance [GO:0019827]; transcription initiation from RNA polymerase II promoter [GO:0006367]ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; receptor activity [GO:0004872]; RNA polymerase II transcription cofactor activity [GO:0001104]; thyroid hormone receptor binding [GO:0046966]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; ubiquitin protein ligase activity [GO:0061630]; vitamin D receptor binding [GO:0042809]mediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]; ubiquitin ligase complex [GO:0000151]Q9UNL2SSRG+Translocon-associated protein subunit gammahintegral component of endoplasmic reticulum membrane [GO:0030176]; Sec61 translocon complex [G< O:0005784]Q93062RBPMS*RNA-binding protein with multiple splicingeSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17099224}. Cytoplasm {ECO:0000269|PubMed:17099224}.positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of SMAD protein import into nucleus [GO:0060391]; regulation of transcription, DNA-templated [GO:0006355]; RNA processing [GO:0006396]; transcription, DNA-templated [GO:0006351]nucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]FUNCTION: Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. Binds to poly(A) RNA. {ECO:0000269|PubMed:17099224}.Q9NX46ARHL2$Poly(ADP-ribose) glycohydrolase ARH3?SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion matrix. Nucleus.,cellular response to superoxide [GO:0071451]Umetal ion binding [GO:0046872]; poly(ADP-ribose) glycohydrolase activity [GO:0004649];mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria. {ECO:0000269|PubMed:16278211}.O95985TOP3BDNA topoisomerase 3-beta-1Homologous recombination(23)Hchromosome segregation [GO:0007059]; DNA topological change [GO:0006265]DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type I activity [GO:0003917]; poly(A) RNA binding [GO:0044822]Qcondensed chromosome [GO:0000793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]6FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity. {ECO:0000250}.P20290BTF3Transcription factor BTF3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10982809}. Nucleus {ECO:0000269|PubMed:10982809}. Note=The heterodimer with NACA is cytoplasmic.in utero embryonic development [GO:0001701]; protein transport [GO:0015031]; regulation of transcription, DNA-templated [GO:0006355]; transcription from RNA polymerase II promoter [GO:0006366]FUNCTION: When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription. {ECO:0000269|PubMed:10982809}.P08243ASNS-Asparagine synthetase [glutamine-hydrolyzing]asparagine biosynthetic process [GO:0006529]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; cellular protein metabolic process [GO:0044267]; cellular response to glucose starvation [GO:0042149]; cellular response to hormone stimulus [GO:0032870]; endoplasmic reticulum unfolded protein response [GO:0030968]; glutamine metabolic process [GO:0006541]; L-asparagine biosynthetic process [GO:0070981]; liver development [GO:0001889]; negative regulation of apoptotic process [GO:0043066]; PERK-mediated unfolded protein response [GO:0036499]; positive regulation of mitotic cell cycle [GO:0045931]; response to amino acid [GO:0043200]; response to follicle-stimulating hormone [GO:0032354]; response to light stimulus [GO:0009416]; response to mechanical stimulus [GO:0009612]; response to methotrexate [GO:0031427]; response to toxic substance [GO:0009636]; small molecule metabolic process [GO:0044281]zasparagine synthase (glutamine-hydrolyzing) activity [GO:0004066]; ATP binding [GO:0005524]; cofactor binding [GO:0048037]Q6DKJ4NXN NucleoredoxinNSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.cardiovascular system development [GO:0072358]; cell differentiation [GO:0030154]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of Wnt signaling pathway [GO:0030178]; Wnt signaling pathway [GO:0016055]hprotein-disulfide reductase activity [GO:0047134]; thioredoxin-disulfide reductase activity [GO:0004791](FUNCTION: Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A) (By similarity). {ECO:0000250}.Q15695U2AFLTU2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1Ymetal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]<nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]Q7LBR1CHM1B&Charged multivesicular body protein 1bSUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body.cell division [GO:0051301]; cell separation after cytokinesis [GO:0000920]; establishment of protein localization [GO:0045184]; mitotic metaphase plate congression [GO:0007080]; nucleus organization [GO:0006997]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702],protein domain specific binding [GO:0019904]cytosol [GO:0005829]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane coat [GO:0030117]FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPa< se VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells. Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:19129479}.Q5JU85IQEC2-IQ motif and SEC7 domain-containing protein 2actin cytoskeleton organization [GO:0030036]; positive regulation of GTPase activity [GO:0043547]; regulation of ARF protein signal transduction [GO:0032012]Q96K58ZN668Zinc finger protein 668GFUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.Q6IPU0CENPPCentromere protein PSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16622420}. Chromosome, centromere {ECO:0000269|PubMed:16622420}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.CENP-A containing nucleosome assembly [GO:0034080]; mitotic cell cycle [GO:0000278]; nucleosome assembly [GO:0006334]; small GTPase mediated signal transduction [GO:0007264][chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]gFUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16622420}.O00154BACH-Cytosolic acyl coenzyme A thioester hydrolaseSUBCELLULAR LOCATION: Isoform 4: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 5: Mitochondrion.9coenzyme A biosynthetic process [GO:0015937]; fatty acid catabolic process [GO:0009062]; long-chain fatty-acyl-CoA catabolic process [GO:0036116]; medium-chain fatty acid biosynthetic process [GO:0051792]; medium-chain fatty-acyl-CoA catabolic process [GO:0036114]; palmitic acid biosynthetic process [GO:1900535]carboxylic ester hydrolase activity [GO:0052689]; fatty-acyl-CoA binding [GO:0000062]; long-chain fatty acyl-CoA binding [GO:0036042]; palmitoyl-CoA hydrolase activity [GO:0016290]; protein homodimerization activity [GO:0042803]cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.Q9NV70EXOC1Exocyst complex component 1rcellular protein metabolic process [GO:0044267]; exocyst localization [GO:0051601]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of protein secretion [GO:0050714]; protein transport [GO:0015031]XGTP-Rho binding [GO:0017049]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]cytoplasm [GO:0005737]; cytoplasmic side of apical plasma membrane [GO:0098592]; cytosol [GO:0005829]; exocyst [GO:0000145]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q9Y4G8RPGF2(Rap guanine nucleotide exchange factor 2Activation RasSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Late endosome. Cell junction {ECO:0000250}. Note=Associated with the synaptic plasma membrane. Colocalizes with ADRB1 at the plasma membrane. Synaptosome. Enriched in synaptic plasma membrane and neuronal cell body. Colocalized with CTNNB1 at cell-cell contacts (By similarity). Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with the high affinity nerve growth factor receptor NTRK1 at late endosomes. Translocated to the perinuclear region in a RAP1A-dependent manner. Translocated to the cell membrane. {ECO:0000250}.adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; blood vessel development [GO:0001568]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; cAMP-mediated signaling [GO:0019933]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to nerve growth factor stimulus [GO:1990090]; establishment of endothelial barrier [GO:0061028]; establishment of endothelial intestinal barrier [GO:0090557]; forebrain neuron development [GO:0021884]; G-protein coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; microvillus assembly [GO:0030033]; negative regulation of cell proliferation [GO:0008285]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of melanin biosynthetic process [GO:0048022]; nerve growth factor signaling pathway [GO:0038180]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron migration [GO:2001224]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein binding [GO:0032092]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of vasculogenesis [GO:2001214]; protein localization to plasma membrane [GO:0072659]; Rap protein signal transduction [GO:0032486]; regulation of cell junction assembly [GO:1901888]; regulation of synaptic plasticity [GO:0048167]; small GTPase mediated signal transduction [GO:0007264]; ventricular system development [GO:0021591]beta-1 adrenergic receptor binding [GO:0031697]; calcium ion binding [GO:0005509]; cAMP binding [GO:0030552]; diacylglycerol binding [GO:0019992]; GTPase activator activity [GO:0005096]; PDZ domain binding [GO:0030165]; phosphatidic acid binding [GO:0070300]; Rap guanyl-nucleotide exchange factor activity [GO:0017034]; Ras guanyl-nucleotide exchange factor activity [GO:0005088]; signal transducer activity [GO:0004871]; WW domain binding [GO:0050699]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; synapse [GO:0045202]FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10608844, PubMed:10548487, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through th< e G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions. {ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:10608883, ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:10934204, ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:23800469}.P31943HNRH1)Heterogeneous nuclear ribonucleoprotein Hgene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; regulation of RNA splicing [GO:0043484]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]}nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG). {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:16946708}.Q8N5I4DHRSX9Dehydrogenase/reductase SDR family member on chromosome XO75525KHDR3KKH domain-containing, RNA-binding, signal transduction-associated protein 3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15901763}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. May play a role as a negative regulator of cell growth. Inhibits cell proliferation. Involved in splice site selection of vascular endothelial growth factor. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. RNA-binding abilities are down-regulated by tyrosine kinase PTK6. Involved in post-transcriptional regulation of HIV-1 gene expression. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. {ECO:0000269|PubMed:10564820, ECO:0000269|PubMed:11741900, ECO:0000269|PubMed:15901763}.O75368SH3L12SH3 domain-binding glutamic acid-rich-like protein7positive regulation of signal transduction [GO:0009967]rcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634]Q9Y6A1POMT1 Protein O-mannosyl-transferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14699049}; Multi-pass membrane protein {ECO:0000269|PubMed:14699049}.carbohydrate metabolic process [GO:0005975]; extracellular matrix organization [GO:0030198]; mannosylation [GO:0097502]; multicellular organismal development [GO:0007275]; protein O-linked glycosylation [GO:0006493]dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannosyltransferase activity [GO:0000030]; metal ion binding [GO:0046872]acrosomal vesicle [GO:0001669]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. {ECO:0000269|PubMed:12369018, ECO:0000269|PubMed:14699049}.Q5HYK7SH319 SH3 domain-containing protein 19SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14551139}. Nucleus {ECO:0000269|PubMed:14551139}. Note=Is recruited to the nucleus by the KMT2A/MLL1-EEN fusion protein.cytoskeleton organization [GO:0007010]; membrane organization [GO:0061024]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of cell morphogenesis [GO:0022604](proline-rich region binding [GO:0070064]jcytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:14551139, ECO:0000269|PubMed:15280379, ECO:0000269|PubMed:21834987}.Q9C0J8WDR33(pre-mRNA 3' end processing protein WDR33YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11162572, ECO:0000269|PubMed:19217410}.mRNA cleavage [GO:0006379]; mRNA polyadenylation [GO:0006378]; postreplication repair [GO:0006301]; spermatogenesis [GO:0007283]collagen trimer [GO:0005581]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]mFUNCTION: Essential for both cleavage and polyadenylation of pre-mRNA 3' ends. {ECO:0000269|PubMed:19217410}.P21810PGS1Biglycan Proteoglycansblood vessel remodeling [GO:0001974]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; extracellular matrix organization [GO:0030198]; glycosaminoglycan metabolic process [GO:0030203]; peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan [GO:0019800]; small molecule metabolic process [GO:0044281]extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent [GO:0005201]; glycosaminoglycan binding [GO:0005539]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; proteinaceous extracellular matrix [GO:0005578]; sarcolemma [GO:0042383]; transport vesicle [GO:0030133]DFUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}.Q02556IRF8Interferon regulatory factor 8<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23166356}.*cellular response to lipopolysaccharide [GO:0071222]; cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; defense response to protozoan [GO:0042832]; immune response [GO:0006955]; interferon-gamma-mediated signaling pathway [GO:0060333]; myeloid cell differentiation [GO:0030099]; negative regulation of growth of symbiont in host [GO:0044130]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; phagocytosis [GO:0006909]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of transcription initiation from RNA polymerase II < promoter [GO:0060261]; transcription, DNA-templated [GO:0006351]; type I interferon signaling pathway [GO:0060337]regulatory region DNA binding [GO:0000975]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705] FUNCTION: Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)). Plays a negative regulatory role in cells of the immune system. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF8 and activation of genes (By similarity). {ECO:0000250}.Q9BRS8LARP6La-related protein 6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17383118}. Nucleus {ECO:0000269|PubMed:17383118}. Note=Shuttles between the nucleus and the cytoplasm.Cregulation of translation [GO:0006417]; RNA processing [GO:0006396]9nucleotide binding [GO:0000166]; RNA binding [GO:0003723]Tcytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]iFUNCTION: Regulates the coordinated translation of type I collagen alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through high-affinity binding of a stem-loop structure in their 5' UTR. This regulation requires VIM and MYH10 filaments, and the helicase DHX9. {ECO:0000269|PubMed:20603131, ECO:0000269|PubMed:21746880, ECO:0000269|PubMed:22190748}.Q5VW38GP107Protein GPR107SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:25031321}; Multi-pass membrane protein.FUNCTION: Involved in Golgi-to-ER retrograde transport. Functions as a host factor required for infection by Pseudomonas aeruginosa exotoxin A and Campylobacter jejuni CDT toxins. {ECO:0000269|PubMed:25031321}.O75792RNH2ARibonuclease H2 subunit ADNA replication [GO:0006260]; DNA replication, removal of RNA primer [GO:0043137]; mismatch repair [GO:0006298]; RNA catabolic process [GO:0006401]; RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]metal ion binding [GO:0046872]; ribonuclease activity [GO:0004540]; RNA binding [GO:0003723]; RNA-DNA hybrid ribonuclease activity [GO:0004523]:nucleus [GO:0005634]; ribonuclease H2 complex [GO:0032299]}FUNCTION: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.Q6IN85P4R3A<Serine/threonine-protein phosphatase 4 regulatory subunit 3ARSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18487071}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18487071}. Nucleus {ECO:0000269|PubMed:18487071}. Note=In interphase localized in the cytoplasm and in the nucleus (with higher levels). During metaphase located in pericentriolar regions.Xcytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]mFUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair. {ECO:0000269|PubMed:18614045}.Q8TD55PKHO27Pleckstrin homology domain-containing family O member 2Q969Z0TBRG4 Protein TBRG4ycell cycle arrest [GO:0007050]; cellular respiration [GO:0045333]; positive regulation of cell proliferation [GO:0008284]RFUNCTION: May play a role in cell cycle progression. {ECO:0000269|PubMed:9383053}.P25098ARBK1!Beta-adrenergic receptor kinase 1mSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21146}. Cell membrane {ECO:0000250|UniProtKB:P21146}.Hactivation of phospholipase C activity [GO:0007202]; cardiac muscle contraction [GO:0060048]; desensitization of G-protein coupled receptor protein signaling pathway [GO:0002029]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; heart development [GO:0007507]; innate immune response [GO:0045087]; negative regulation of striated muscle contraction [GO:0045988]; negative regulation of the force of heart contraction by chemical signal [GO:0003108]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of catecholamine secretion [GO:0033605]; receptor internalization [GO:0031623]; signal transduction [GO:0007165]; tachykinin receptor signaling pathway [GO:0007217]; termination of G-protein coupled receptor signaling pathway [GO:0038032]; viral entry into host cell [GO:0046718]; viral genome replication [GO:0019079]alpha-2A adrenergic receptor binding [GO:0031694]; ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; Edg-2 lysophosphatidic acid receptor binding [GO:0031755]; G-protein coupled receptor kinase activity [GO:0004703]; protein kinase activity [GO:0004672]~cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]; primary cilium [GO:0072372]FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner. {ECO:0000269|PubMed:19306925}.P35998PRS7!26S protease regulatory subunit 7anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; osteoblast differentiation [GO:0001649]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0045899]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cyto< sol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; membrane [GO:0016020]; nuclear proteasome complex [GO:0031595]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, base subcomplex [GO:0008540]8FUNCTION: The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. {ECO:0000269|PubMed:9295362}.O43516WIPF1,WAS/WASL-interacting protein family member 1SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL (By similarity). {ECO:0000250}.,actin cortical patch assembly [GO:0000147]; actin cortical patch localization [GO:0051666]; actin filament-based movement [GO:0030048]; actin polymerization or depolymerization [GO:0008154]; endocytosis [GO:0006897]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; positive regulation of actin nucleation [GO:0051127]; protein complex assembly [GO:0006461]; regulation of cell shape [GO:0008360]; response to other organism [GO:0051707]; small GTPase mediated signal transduction [GO:0007264]^actin binding [GO:0003779]; actin filament binding [GO:0051015]; profilin binding [GO:0005522]actin cortical patch [GO:0030479]; actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; ruffle [GO:0001726]TFUNCTION: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus. {ECO:0000250, ECO:0000269|PubMed:10878810, ECO:0000269|PubMed:19910490, ECO:0000269|PubMed:9405671}.Q9UDY2ZO2Tight junction protein ZO-2xSUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus {ECO:0000250}. Note=Also nuclear under environmental stress conditions and in migratory endothelial cells and subconfluent epithelial cell cultures. {ECO:0000250}.apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; establishment of endothelial intestinal barrier [GO:0090557]; hippo signaling [GO:0035329]; intestinal absorption [GO:0050892]; nucleotide phosphorylation [GO:0046939]; programmed cell death [GO:0012501]; regulation of membrane permeability [GO:0090559]; response to organic substance [GO:0010033]|guanylate kinase activity [GO:0004385]; protein binding, bridging [GO:0030674]; protein domain specific binding [GO:0019904]adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]AFUNCTION: Plays a role in tight junctions and adherens junctions.Q9UPY8MARE34Microtubule-associated protein RP/EB family member 3SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:19255245}. Note=Associated with the microtubule network. Detected at the plus end of microtubules.$cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of microtubule plus-end binding [GO:1903033]; positive regulation of transcription, DNA-templated [GO:0045893]cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:0048471]-FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). {ECO:0000250}.Q9Y3L33BP1SH3 domain-binding protein 1cFUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. This protein binds preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP activity for Rac-related proteins but not for Rho- or Ras-related proteins. It inhibits PDGF-induced membrane ruffling mediated by Rac (By similarity). {ECO:0000250}.O14863ZNT4Zinc transporter 4regulation of sequestering of zinc ion [GO:0061088]; response to toxic substance [GO:0009636]; zinc II ion transmembrane transport [GO:0071577]; zinc ion homeostasis [GO:0055069]cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]}FUNCTION: Probably involved in zinc transport out of the cytoplasm, maybe by sequestration into an intracellular compartment.Q9ULK4MED236Mediator of RNA polymerase II transcription subunit 23gene expression [GO:0010467]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription initiation from RNA polymerase II promoter [GO:0006367]_transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; transcription factor complex [GO:0005667]; ubiquitin ligase complex [GO:0000151]FUNCTION: Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling. {ECO:0000250, ECO:0000269|PubMed:10353252, ECO:0000269|PubMed:14759369, ECO:0000269|PubMed:16595664}.O95340PAPS2=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 23'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; blood coagulation [GO:0007596]; bone development [GO:0060348]; carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]; sulfate assimilation [GO:0000103]; xenobiotic metabolic process [GO:0006805]uFUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. May h< ave a important role in skeletogenesis during postnatal growth (By similarity). {ECO:0000250}.O60610DIAP1Protein diaphanous homolog 1SUBCELLULAR LOCATION: Cell membrane. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells.actin filament polymerization [GO:0030041]; cellular response to histamine [GO:0071420]; cytoskeleton organization [GO:0007010]; protein localization to microtubule [GO:0035372]; regulation of cell shape [GO:0008360]; regulation of microtubule-based process [GO:0032886]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; sensory perception of sound [GO:0007605]; small GTPase mediated signal transduction [GO:0007264]aion channel binding [GO:0044325]; poly(A) RNA binding [GO:0044822]; receptor binding [GO:0005102]Pcytosol [GO:0005829]; mitotic spindle [GO:0072686]; ruffle membrane [GO:0032587]6FUNCTION: Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000250, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21834987}.Q99570PI3R4.Phosphoinositide 3-kinase regulatory subunit 4SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:14617358}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes. Localizes also to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q8VD65, ECO:0000305}.cellular response to glucose starvation [GO:0042149]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; late endosome to vacuole transport [GO:0045324]; macroautophagy [GO:0016236]; peroxisome degradation [GO:0030242]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; protein phosphorylation [GO:0006468]; protein targeting to vacuole [GO:0006623]; receptor catabolic process [GO:0032801]; regulation of cytokinesis [GO:0032465]; small molecule metabolic process [GO:0044281]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]autophagosome [GO:0005776]; axoneme [GO:0005930]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; late endosome [GO:0005770]; membrane [GO:0016020]; nuclear pore [GO:0005643]; nucleus-vacuole junction [GO:0071561]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]FUNCTION: Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123). {ECO:0000269|PubMed:20643123}.Q96T76MMS190MMS19 nucleotide excision repair protein homolog@SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.cellular response to DNA damage stimulus [GO:0006974]; chromosome segregation [GO:0007059]; DNA metabolic process [GO:0006259]; DNA repair [GO:0006281]; iron-sulfur cluster assembly [GO:0016226]; nucleotide-excision repair [GO:0006289]; phosphorelay signal transduction system [GO:0000160]; positive regulation of transcription, DNA-templated [GO:0045893]; response to hormone [GO:0009725]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]estrogen receptor binding [GO:0030331]; protein binding, bridging [GO:0030674]; receptor signaling complex scaffold activity [GO:0030159]; transcription coactivator activity [GO:0003713]CIA complex [GO:0097361]; cytoplasm [GO:0005737]; holo TFIIH complex [GO:0005675]; membrane [GO:0016020]; MMXD complex [GO:0071817]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription. As part of the mitotic spindle-associated MMXD complex, plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD. Indirectly acts as a transcriptional coactivator of estrogen receptor (ER), via its role in iron-sulfur insertion into some component of the TFIIH-machinery. {ECO:0000269|PubMed:11071939, ECO:0000269|PubMed:11328871, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:22678361, ECO:0000269|PubMed:22678362}.Q13813SPTN1(Spectrin alpha chain, non-erythrocytic 1Tight junction(134)SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells. {ECO:0000250}.actin filament capping [GO:0051693]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; programmed cell death [GO:0012501]qactin binding [GO:0003779]; calcium ion binding [GO:0005509]; structural constituent of cytoskeleton [GO:0005200]_cuticular plate [GO:0032437]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; fascia adherens [GO:0005916]; intracellular membrane-bounded organelle [GO:0043231]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; spectrin [GO:0008091]; Z disc [GO:0030018]FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.P46821MAP1B!Microtubule-associated protein 1B%SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18195017}. Cytoplasm {ECO:0000269|PubMed:18195017}. Cell junction, synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DAPK1 in the microtubules and cortical actin fibers. {ECO:0000250}.haxon extension [GO:0048675]; cellular process [GO:0009987]; dendrite development [GO:0016358]; establishment of monopolar cell polarity [GO:0061162]; microtubule bundle formation [GO:0001578]; mitochondrion transport al< ong microtubule [GO:0047497]; negative regulation of intracellular transport [GO:0032387]; positive regulation of axon extension [GO:0045773]!cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; neuronal postsynaptic density [GO:0097481]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]FUNCTION: Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. {ECO:0000250, ECO:0000269|PubMed:18195017}.Q8TBB5KLDC4!Kelch domain-containing protein 4Q9P2G1AKIB12Ankyrin repeat and IBR domain-containing protein 1Rubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. {ECO:0000250}.Q92841DDX17)Probable ATP-dependent RNA helicase DDX17nSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.apositive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of skeletal muscle cell differentiation [GO:2001014]; RNA processing [GO:0006396]; RNA secondary structure unwinding [GO:0010501]; transcription, DNA-templated [GO:0006351]/ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; estrogen receptor binding [GO:0030331]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA-dependent ATPase activity [GO:0008186]; RNA helicase activity [GO:0003724]; transcription coactivator activity [GO:0003713]BFUNCTION: RNA-dependent ATPase activity. Involved in transcriptional regulation. Transcriptional coactivator for estrogen receptor ESR1. Increases ESR1 AF-1 domain-mediated transactivation. Synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and probably involved in skeletal muscle differentiation. Required for zinc-finger antiviral protein ZC3HAV1-mediated mRNA degradation. {ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:18334637, ECO:0000269|PubMed:19718048}.O60830TI17B?Mitochondrial import inner membrane translocase subunit Tim17-BRP-P-bond-hydrolysis-driven protein transmembrane transporter activity [GO:0015450]integral component of mitochondrial inner membrane [GO:0031305]; mitochondrial inner membrane [GO:0005743]; mitochondrial inner membrane presequence translocase complex [GO:0005744]P0CG40SP9Transcription factor Sp9embryonic limb morphogenesis [GO:0030326]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]FUNCTION: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity). {ECO:0000250}.Q96J88ESIP1(Epithelial-stromal interaction protein 1P35754GLRX1Glutaredoxin-1cell redox homeostasis [GO:0045454]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of membrane potential [GO:0045838]; positive regulation of sodium ion transmembrane transporter activity [GO:2000651]; protein deglutathionylation [GO:0080058]; small molecule metabolic process [GO:0044281]electron carrier activity [GO:0009055]; glutathione disulfide oxidoreductase activity [GO:0015038]; glutathione oxidoreductase activity [GO:0097573]; protein N-terminus binding [GO:0047485]jcytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.Q2TAA8TXIP12Translin-associated factor X-interacting protein 1SSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99P25}.,perinuclear region of cytoplasm [GO:0048471]KFUNCTION: Possible role in spermatogenesis. {ECO:0000250|UniProtKB:Q99P25}.Q7Z333SETXProbable helicase senataxinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:24105744}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17562789}. Nucleus, nucleolus {ECO:0000269|PubMed:17562789}. Cytoplasm {ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21576111}. Chromosome {ECO:0000269|PubMed:23149945}. Chromosome, telomere {ECO:0000269|PubMed:21112256}. Cell projection, axon {ECO:0000269|PubMed:21576111}. Cell projection, growth cone {ECO:0000269|PubMed:21576111}. Note=May be detected in the nucleolus only in cycling cells. At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (By similarity). Localizes with telomeric DNA in a transcription-dependent manner (PubMed:21112256). Under replication stress, colocalizes with a variety of DNA damage signaling and repair response proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells in a transcription- and RNA/DNA hybrid-dependent manner (PubMed:23149945). Localizes at limited number of nuclear foci (PubMed:24105744). Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744). Most abundant in the nucleus. Detected in granules. Colocalized in cycling cells with FBL in the nucleolus. {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:23149945, ECO:0000269|PubMed:24105744}.cellular response to DNA damage stimulus [GO:0006974]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; circadian rhythm [GO:0007623]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; double-strand break repair [GO:0006302]; fibroblast growth factor receptor signaling pathway [GO:0008543]; MAPK cascade [GO:0000165]; mRNA splice site selection [GO:0006376]; negative regulation of apoptotic process [GO:0043066]; positive regulation of DNA-templated transcription, initiation [GO:2000144]; positive regulation of DNA-templated transcription, termination [GO:0060566]; positive regulation of neuron projection development [GO:0010976]; positive regulation of RNA splicing [GO:0033120]; positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled [GO:2000806]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein kinase B signaling [GO:0043491]; RNA processing [GO:0006396]; spermatogenesis [GO:0007283]; termination of RNA polymerase II transcription [GO:0006369]ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; identical protein binding [GO:0042802]; transcription termination site sequence-specific DNA binding [GO:0001147]axon [GO:0030424]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]OFUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymeras< e II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111). {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:19515850, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:24105744}.Q9P273TEN3 Teneurin-3~SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250}.camera-type eye morphogenesis [GO:0048593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; positive regulation of neuron projection development [GO:0010976]; self proteolysis [GO:0097264]; signal transduction [GO:0007165]Uaxon [GO:0030424]; integral component of membrane [GO:0016021]; membrane [GO:0016020]PFUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes axon guidance and homophilic cell adhesion. Plays a role in the development of the visual pathway; regulates the formation in ipsilateral retinal mapping to both the dorsal lateral geniculate nucleus (dLGN) and the superior colliculus (SC). May be involved in the differentiation of the fibroblast-like cells in the superficial layer of mandibular condylar cartilage into chondrocytes. May function as a cellular signal transducer (By similarity). {ECO:0000250}.Q9NZJ9NUDT42Diphosphoinositol polyphosphate phosphohydrolase 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12121577}.xcalcium-mediated signaling [GO:0019722]; cyclic-nucleotide-mediated signaling [GO:0019935]; cyclic nucleotide metabolic process [GO:0009187]; inositol phosphate metabolic process [GO:0043647]; intracellular signal transduction [GO:0035556]; intracellular transport [GO:0046907]; regulation of RNA export from nucleus [GO:0046831]; small molecule metabolic process [GO:0044281]diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity [GO:0052846]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052847]; inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity [GO:0052843]; inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052848]; inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity [GO:0052844]; inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity [GO:0052845]; inositol diphosphate tetrakisphosphate diphosphatase activity [GO:0052840]; metal ion binding [GO:0046872]; snoRNA binding [GO:0030515]FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000269|PubMed:10777568}.Q13617CUL2Cullin-2cell cycle arrest [GO:0007050]; cellular response to hypoxia [GO:0071456]; G1/S transition of mitotic cell cycle [GO:0000082]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of cell proliferation [GO:0008285]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; viral process [GO:0016032]_Cul2-RING ubiquitin ligase complex [GO:0031462]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF). {ECO:0000250}.Q07021C1QBPDComplement component 1 Q subcomponent-binding protein, mitochondrial transporterSUBCELLULAR LOCATION: Mitochondrion matrix. Nucleus. Cell membrane; Peripheral membrane protein; Extracellular side. Secreted. Cytoplasm. Nucleus, nucleolus. Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes.apoptotic process [GO:0006915]; blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; innate immune response [GO:0045087]; mature ribosome assembly [GO:0042256]; mRNA processing [GO:0006397]; negative regulation of defense response to virus [GO:0050687]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of MDA-5 signaling pathway [GO:0039534]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of RIG-I signaling pathway [GO:0039536]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; phosphatidylinositol 3-kinase signaling [GO:0014065]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell adhesion [GO:0045785]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of mitochondrial translation [GO:0070131]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of trophoblast cell migration [GO:1901165]; regulation of complement activation [GO:0030449]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]Aadrenergic receptor binding [GO:0031690]; complement component C1q binding [GO:0001849]; hyaluronic acid binding [GO:0005540]; kininogen binding [GO:0030984]; mitochondrial ribosome binding [GO:0097177]; mRNA binding [GO:0003729]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134] cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; mitochondrial matrix [GO:000575< 9]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. Involved in replication of Rubella virus. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppresion of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection. Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. {ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:11859136, ECO:0000269|PubMed:12833064, ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16140380, ECO:0000269|PubMed:16177118, ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19004836, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:20810993, ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.O14920IKKB7Inhibitor of nuclear factor kappa-B kinase subunit betafSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane raft. Note=Colocalized with DPP4 in membrane rafts. B cell homeostasis [GO:0001782]; cellular response to tumor necrosis factor [GO:0071356]; Fc-epsilon receptor signaling pathway [GO:0038095]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; I-kappaB phosphorylation [GO:0007252]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; neuron projection development [GO:0031175]; neurotrophin TRK receptor signaling pathway [GO:0048011]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of cation channel activity [GO:2001259]; positive regulation of cell proliferation [GO:0008284]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of neuron death [GO:1901216]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sodium ion transport [GO:0010765]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; protein phosphorylation [GO:0006468]; response to drug [GO:0042493]; response to fatty acid [GO:0070542]; response to toxic substance [GO:0009636]; response to virus [GO:0009615]; serine phosphorylation of STAT protein [GO:0042501]; skeletal muscle contraction [GO:0003009]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]IATP binding [GO:0005524]; IkappaB kinase activity [GO:0008384]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; membrane raft [GO:0045121]; nucleus [GO:0005634]FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. {ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:17213322, ECO:0000269|PubMed:19716809, ECO:0000269|PubMed:20410276, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20797629, ECO:0000269|PubMed:21138416}.Q6PIU2NCEH1%Neutral cholesterol ester hydrolase 1< SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:12149457}; Single-pass type II membrane protein {ECO:0000305|PubMed:12149457}. Microsome {ECO:0000250}.0carboxylic ester hydrolase activity [GO:0052689]fendoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration. {ECO:0000269|PubMed:17052608}.Q8IVP5FUND1!FUN14 domain-containing protein 1SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:22267086}; Multi-pass membrane protein {ECO:0000269|PubMed:22267086}.Hmitochondrion degradation [GO:0000422]; response to hypoxia [GO:0001666]jintegral component of mitochondrial outer membrane [GO:0031307]; mitochondrial outer membrane [GO:0005741]FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an important mechanism for mitochondrial quality control. {ECO:0000269|PubMed:22267086}.O95400CD2B2.CD2 antigen cytoplasmic tail-binding protein 2ESUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of phosphatase activity [GO:0010923]; RNA splicing [GO:0008380]; spliceosomal tri-snRNP complex assembly [GO:0000244].ribonucleoprotein complex binding [GO:0043021]]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U5 snRNP [GO:0005682]FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. {ECO:0000269|PubMed:15840814}.P49662CASP4 Caspase-4DSUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion.,apoptotic process [GO:0006915]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of inflammatory response [GO:0050727]1cysteine-type endopeptidase activity [GO:0004197]AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; IPAF inflammasome complex [GO:0072557]; mitochondrion [GO:0005739]; NLRP3 inflammasome complex [GO:0072559]FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Involved in ER-stress induced apoptosis. Cleaves caspase-1. {ECO:0000269|PubMed:15123740, ECO:0000269|Ref.14}.P09651ROA1*Heterogeneous nuclear ribonucleoprotein A1_SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner.Talternative mRNA splicing, via spliceosome [GO:0000380]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; nuclear export [GO:0051168]; nuclear import [GO:0051170]; RNA export from nucleus [GO:0006405]; RNA splicing [GO:0008380]; viral process [GO:0016032]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]; spliceosomal complex [GO:0005681]FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681}.P61970NTF2Nuclear transport factor 2positive regulation of protein import into nucleus [GO:0042307]; protein export from nucleus [GO:0006611]; protein import into nucleus, translocation [GO:0000060]; regulation of vascular endothelial growth factor production [GO:0010574]BRan GTPase binding [GO:0008536]; transporter activity [GO:0005215]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear outer membrane [GO:0005640]; nuclear pore [GO:0005643]; nuclear pore central transport channel [GO:0044613]pFUNCTION: Facilitates protein transport into the nucleus. Interacts with the nucleoporin p62 and with Ran. Acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import.O60645EXOC3Exocyst complex component 3cellular protein metabolic process [GO:0044267]; exocyst localization [GO:0051601]; exocytosis [GO:0006887]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]Scytosol [GO:0005829]; exocyst [GO:0000145]; secretory granule membrane [GO:0030667]O75821EIF3G4Eukaryotic translation initiation factor 3 subunit G+SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.vnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; translation initiation factor activity [GO:0003743]cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit can bind 18S rRNA.O95819M4K47Mitogen-activated protein kinase kinase kinase kinase 4>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14966141}.activation of protein kinase activity [GO:0032147]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; neuron projection morphogenesis [GO:0048812]; protein phosphorylation [GO:0006468]; regulation of JNK cascade [GO:0046328]; regulation of mitotic cell cycle [GO:0007346]; stress-activated protein kinase signaling cascade [GO:0031098]vATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Serine/threonine kinase that may play a role in the response to environmental stress and cytokines such as TNF-alpha. Appears to act upstream of the JUN N-terminal pathway. Phosphorylates SMAD1 on Thr-322. {ECO:0000269|PubMed:21690388, ECO:0000269|PubMed:9890973}.Q9UN70PCDGKProtocadherin gamma-C3calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; synapse < organization [GO:0050808]Q14156EFR3AProtein EFR3 homolog AdSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Localizes to plasma membrane. {ECO:0000250}.P08134RHOC$Rho-related GTP-binding protein RhoCSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000269|PubMed:16236794}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.apical junction assembly [GO:0043297]; axon guidance [GO:0007411]; cytokinesis [GO:0000910]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of lipase activity [GO:0060193]; regulation of small GTPase mediated signal transduction [GO:0051056]; skeletal muscle satellite cell migration [GO:1902766]; small GTPase mediated signal transduction [GO:0007264]; wound healing, spreading of cells [GO:0044319]AGTP binding [GO:0005525]; signal transducer activity [GO:0004871]cleavage furrow [GO:0032154]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:20974804}.Q9C0B7TNG62Transport and Golgi organization protein 6 homologO43301HS12AHeat shock 70 kDa protein 12AP85037FOXK1Forkhead box protein K19SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; muscle organ development [GO:0007517]; negative regulation of cell growth [GO:0030308]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription from RNA polymerase II promoter [GO:0006366]RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]!FUNCTION: Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene. Has a role in myogenic differentiation and in remodeling processes of adult muscles that occur in response to physiological stimuli (By similarity). {ECO:0000250|UniProtKB:P42128}.Q5RHP9ERIC3Glutamate-rich protein 3Q8TDY8IGDC40Immunoglobulin superfamily DCC subclass member 4eSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.O75616ERAL1GTPase Era, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion inner membrane; Peripheral membrane protein. Note=Localizes on the matrix side on the mitochondrial inner membrane.-ribosomal small subunit assembly [GO:0000028]GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]; rRNA binding [GO:0019843]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly. {ECO:0000269|PubMed:20430825, ECO:0000269|PubMed:20604745}.Q9Y2J2E41L3Band 4.1-like protein 3`SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction {ECO:0000269|PubMed:9892180}. Cell membrane {ECO:0000269|PubMed:9892180}; Peripheral membrane protein {ECO:0000269|PubMed:9892180}; Cytoplasmic side {ECO:0000269|PubMed:9892180}. Cytoplasm {ECO:0000269|PubMed:9892180}. Note=Detected in the cytoplasm of actively dividing cells.=apoptotic process [GO:0006915]; cortical actin cytoskeleton organization [GO:0030866]; cortical cytoskeleton organization [GO:0030865]; cytoskeletal anchoring at plasma membrane [GO:0007016]; myelin maintenance [GO:0043217]; neuron projection morphogenesis [GO:0048812]; paranodal junction assembly [GO:0030913]; protein localization to juxtaparanode region of axon [GO:0071205]; protein localization to paranode region of axon [GO:0002175]; protein localization to plasma membrane [GO:0072659]; regulation of cell growth [GO:0001558]; regulation of cell shape [GO:0008360]2axolemma [GO:0030673]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extrinsic component of membrane [GO:0019898]; juxtaparanode region of axon [GO:0044224]; neuronal postsynaptic density [GO:0097481]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]$FUNCTION: Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5. {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}.Q08378GOGA3Golgin subfamily A member 3dSUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein..cytosol [GO:0005829]; extrinsic component of Golgi membrane [GO:0090498]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]OFUNCTION: Golgi auto-antigen; probably involved in maintaining Golgi structure.Q96Q35AL2SBLAmyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein*regulation of GTPase activity [GO:0043087]_outer dense fiber [GO:0001520]; sperm fibrous sheath [GO:0035686]; sperm flagellum [GO:0036126]Q96FN4CPNE2Copine-2P07951TPM2Tropomyosin beta chainqmuscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; regulation of ATPase activity [GO:0043462]Iactin binding [GO:0003779]; structural constituent of muscle [GO:0008307]Ccytosol [GO:0005829]; muscle thin filament tropomyosin [GO:0005862]FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity). {ECO:0000250}.Q5SWX8ODR4Protein odr-4 homologCoxidoreductase activity [GO:0016491]; zinc ion binding [GO:0008270]gFUNCTION: May play a role in the trafficking of a subset of G-protein coupled receptors. {ECO:0000250}.Q9UNI6DUS12'Dual specificity protein phosphatase 12cellular protein modification process [GO:0006464]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of glucokinase activity [GO:0033133]protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]; zinc ion binding [GO:0008270]P04216THY1Thy-1 membrane glycoproteinangiogenesis [GO:0001525]; cytoskeleton organization [GO:0007010]; focal adhesion assembly [GO:0048041]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell migration [GO:0030336]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of GTPase activity [GO:0043547]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of T c< ell activation [GO:0050870]; protein autophosphorylation [GO:0046777]; retinal cone cell development [GO:0046549]; single organismal cell-cell adhesion [GO:0016337]; T cell receptor signaling pathway [GO:0050852]fGPI anchor binding [GO:0034235]; GTPase activator activity [GO:0005096]; integrin binding [GO:0005178]anchored component of external side of plasma membrane [GO:0031362]; apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]wFUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.P57729RAB38Ras-related protein Rab-38QSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Melanosome. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.endosome to melanosome transport [GO:0035646]; intracellular protein transport [GO:0006886]; melanosome assembly [GO:1903232]; phagosome acidification [GO:0090383]; platelet dense granule organization [GO:0060155]; protein localization to membrane [GO:0072657]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; small GTPase mediated signal transduction [GO:0007264]cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; melanosome [GO:0042470]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: May be involved in melanosomal transport and docking. Involved in the proper sorting of TYRP1. Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with ANKRD27 and VAMP7 (By similarity). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. {ECO:0000250|UniProtKB:Q8QZZ8, ECO:0000269|PubMed:21255211}.A6NCW0U17L37Ubiquitin carboxyl-terminal hydrolase 17-like protein 3QSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.Zapoptotic process [GO:0006915]; ubiquitin-dependent protein catabolic process [GO:0006511]Zcysteine-type peptidase activity [GO:0008234]; ubiquitinyl hydrolase activity [GO:0036459]8endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]$FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. {ECO:0000250}.P35251RFC1Replication factor C subunit 1base-excision repair [GO:0006284]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; positive regulation of catalytic activity [GO:0043085]; regulation of transcription, DNA-templated [GO:0006355]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; telomere maintenance via telomerase [GO:0007004]; transcription, DNA-templated [GO:0006351]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; enzyme activator activity [GO:0008047]cell junction [GO:0030054]; DNA replication factor C complex [GO:0005663]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA. {ECO:0000269|PubMed:8999859}.; FUNCTION: Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair. {ECO:0000269|PubMed:8999859}.Q9NYU1UGGG2.UDP-glucose:glycoprotein glucosyltransferase 2SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12913004}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12913004}.cellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-glucosylation [GO:0097359]BUDP-glucose:glycoprotein glucosyltransferase activity [GO:0003980]kendoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]vFUNCTION: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity). {ECO:0000250}.Q96BJ3AIDA1Axin interactor, dorsalization-associated proteindorsal/ventral pattern formation [GO:0009953]; negative regulation of JNK cascade [GO:0046329]; negative regulation of JUN kinase activity [GO:0043508]; regulation of protein homodimerization activity [GO:0043496]'FUNCTION: Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling (By similarity). {ECO:0000250}.O95104SFR15(Splicing factor, arginine/serine-rich 15kFUNCTION: May act to physically and functionally link transcription and pre-mRNA processing. {ECO:0000250}.Q9NUL3STAU25Double-stranded RNA-binding protein Staufen homolog 2SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Endoplasmic reticulum. Note=Shuttles between the nucleolus, nucleus and the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1 and requires the exportin XPO5. Nuclear export of isoform 2 and isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-independent pathways. Found in large cytoplasmic ribonucleoprotein (RNP) granules which are present in the actin rich regions of myelinating processes and associated with microtubules, polysomes and the endoplasmic reticulum. Also recruited to stress granules (SGs) upon inhibition of translation or oxidative stress. These structures are thought to harbor housekeeping mRNAs when translation is aborted (By similarity). {ECO:0000250}.Jdouble-stranded RNA binding [GO:0003725]; poly(A) RNA binding [GO:0044822]kendoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleolus [GO:0005730]bFUNCTION: RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of sp< ecific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). {ECO:0000250}.Q9NZQ3SPN90'NCK-interacting protein with SH3 domainSUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes.icytoskeleton organization [GO:0007010]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of neuron projection development [GO:0010976]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264])cytoskeletal protein binding [GO:0008092]Ncytosol [GO:0005829]; intermediate filament [GO:0005882]; nucleus [GO:0005634]FUNCTION: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis. {ECO:0000250, ECO:0000269|PubMed:22419821}.Q9HAS0NJMUProtein Njmu-R1-FUNCTION: May have a role in spermatogenesis.Q96J42TXD15(Thioredoxin domain-containing protein 15P58004SESN2 Sestrin-2 DNA repair and damage prevention^autophagy [GO:0006914]; fatty acid beta-oxidation [GO:0006635]; gene expression [GO:0010467]; glucose import [GO:0046323]; mitochondrial DNA metabolic process [GO:0032042]; protein kinase B signaling [GO:0043491]; regulation of cAMP-dependent protein kinase activity [GO:2000479]; regulation of gluconeogenesis involved in cellular glucose homeostasis [GO:0090526]; regulation of response to reactive oxygen species [GO:1901031]; response to glucose [GO:0009749]; response to insulin [GO:0032868]; transcription initiation from RNA polymerase II promoter [GO:0006367]; triglyceride homeostasis [GO:0070328]^cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]UFUNCTION: Involved in the reduction of peroxiredoxins. {ECO:0000269|PubMed:15105503}.P55010IF5*Eukaryotic translation initiation factor 5GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]wFUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).Q6IQ26DEN5A!DENN domain-containing protein 5Acalcium ion transmembrane transport [GO:0070588]; detection of mechanical stimulus [GO:0050982]; positive regulation of GTPase activity [GO:0043547]; retrograde transport, endosome to Golgi [GO:0042147]bcalcium channel activity [GO:0005262]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]7membrane [GO:0016020]; trans-Golgi network [GO:0005802]FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB6A and RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.Q8WV92MITD1MIT domain-containing protein 1%SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Midbody. Membrane; Peripheral membrane protein; Cytoplasmic side. Note=During cytokinesis, recruited to the midbody via interaction with CHMP1A. Interacts with membranes enriched in phosphoinositides.cell separation after cytokinesis [GO:0000920]; mitotic cytokinesis [GO:0000281]; negative regulation of protein binding [GO:0032091]; transport [GO:0006810]phosphatidylinositol binding [GO:0035091]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; midbody [GO:0030496]FUNCTION: Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT-III complex. {ECO:0000269|PubMed:23015756, ECO:0000269|PubMed:23045692}.P43307SSRA+Translocon-associated protein subunit alphacellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; IRE1-mediated unfolded protein response [GO:0036498]; positive regulation of cell proliferation [GO:0008284]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]iFUNCTION: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.Q86UL8MAGI2LMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruted to late endosomes after NGF stimulation. Membrane-associated in synaptosomes (By similarity). {ECO:0000250}.cellular response to nerve growth factor stimulus [GO:1990090]; cytoplasmic transport [GO:0016482]; glomerular visceral epithelial cell development [GO:0072015]; mitotic cell cycle arrest [GO:0071850]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of protein kinase B signaling [GO:0051898]; nerve growth factor signaling pathway [GO:0038180]; neuroligin clustering involved in postsynaptic membrane assembly [GO:0097118]; planar cell polarity pathway involved in axis elongation [GO:0003402]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of receptor internalization [GO:0002092]; positive regulation of synaptic vesicle clustering [GO:2000809]; protein heterooligomerization [GO:0051291]; receptor clustering [GO:0043113]; SMAD protein signal transduction [GO:0060395]beta-1 adrenergic receptor binding [GO:0031697]; phosphatase binding [GO:0019902]; receptor signaling complex scaffold activity [GO:0030159]; signal transducer activity [GO:0004871]; SMAD binding [GO:0046332]; type II activin receptor binding [GO:0070699]Gbicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; late endosome [GO:0005770]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein complex [GO:0043234]; slit diaphragm [GO:0036057]; synapse [GO:0045202]FUNCTION: Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. {ECO:0000269|PubMed:10760291}.Q9H000MKRN2.Probable E3 ubiquitin-protein ligase makorin-2#protein ubiquitination [GO:0016567]]ligase activity [GO:0016874]; poly(A) R< NA binding [GO:0044822]; zinc ion binding [GO:0008270]~FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. {ECO:0000250}.Q8IX12CCAR15Cell division cycle and apoptosis regulator protein 1RSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12816952}.apoptotic process [GO:0006915]; cell cycle [GO:0007049]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of nucleic acid-templated transcription [GO:1903507]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]core promoter binding [GO:0001047]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]Fnucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (PubMed:12816952). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells (PubMed:23887938). {ECO:0000250|UniProtKB:Q8CH18, ECO:0000269|PubMed:12816952, ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.P22626ROA2.Heterogeneous nuclear ribonucleoproteins A2/B1`SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Predominantly nucleoplasmic, however isoform A2 is also found in the cytoplasm of cells in some tissues. Not found in the nucleolus.5gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; RNA splicing [GO:0008380]; RNA transport [GO:0050658]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; pre-mRNA intronic binding [GO:0097157]; RNA binding [GO:0003723]; single-stranded telomeric DNA binding [GO:0043047]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; spliceosomal complex [GO:0005681]FUNCTION: Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus.P40121CAPGMacrophage-capping proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.|barbed-end actin filament capping [GO:0051016]; cell projection assembly [GO:0030031]; protein complex assembly [GO:0006461]Rprotein complex binding [GO:0032403]; protein domain specific binding [GO:0019904]centriole [GO:0005814]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; F-actin capping protein complex [GO:0008290]; Flemming body [GO:0090543]; melanosome [GO:0042470]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]<FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA.Q5VZ89DEN4C!DENN domain-containing protein 4CSUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Cell membrane. Cytoplasm, cytosol. Note=Associates with SLC2A4/GLUT4 storage vesicles.cellular response to insulin stimulus [GO:0032869]; positive regulation of GTPase activity [GO:0043547]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; insulin-responsive compartment [GO:0032593]; plasma membrane [GO:0005886]KFUNCTION: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin. {ECO:0000269|PubMed:20937701}.P35270SPRESepiapterin reductasecell morphogenesis involved in neuron differentiation [GO:0048667]; death [GO:0016265]; dopamine metabolic process [GO:0042417]; L-phenylalanine metabolic process [GO:0006558]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide metabolic process [GO:0046209]; norepinephrine metabolic process [GO:0042415]; oxidation-reduction process [GO:0055114]; pteridine metabolic process [GO:0019889]; regulation of multicellular organism growth [GO:0040014]; regulation of nitric-oxide synthase activity [GO:0050999]; serotonin metabolic process [GO:0042428]; small molecule metabolic process [GO:0044281]; tetrahydrobiopterin biosynthetic process [GO:0006729]; voluntary musculoskeletal movement [GO:0050882]xaldo-keto reductase (NADP) activity [GO:0004033]; NADP binding [GO:0050661]; sepiapterin reductase activity [GO:0004757]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]}FUNCTION: Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.O14681EI24%Etoposide-induced protein 2.4 homologSUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:21154811}; Multi-pass membrane protein {ECO:0000269|PubMed:21154811}. Cytoplasm {ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.gapoptotic process [GO:0006915]; autophagy [GO:0006914]; negative regulation of cell growth [GO:0030308]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear membrane [GO:0031965]FUNCTION: Acts as a negative growth regulator via p53-mediated apoptosis pathway. Regulates formation of degradative autolysosomes during autophagy (By similarity). {ECO:0000250}.P19838NFKB1&Nuclear factor NF-kappa-B p105 subunitSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). apoptotic process [GO:0006915]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; cellular response to lipopolysaccharide [GO:0< 071222]; cellular response to mechanical stimulus [GO:0071260]; cellular response to nicotine [GO:0071316]; cellular response to peptide hormone stimulus [GO:0071375]; Fc-epsilon receptor signaling pathway [GO:0038095]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; membrane protein intracellular domain proteolysis [GO:0031293]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcidiol 1-monooxygenase activity [GO:0010956]; negative regulation of cellular protein metabolic process [GO:0032269]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-12 biosynthetic process [GO:0045083]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of vitamin D biosynthetic process [GO:0010957]; neurotrophin TRK receptor signaling pathway [GO:0048011]; NIK/NF-kappaB signaling [GO:0038061]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of hyaluronan biosynthetic process [GO:1900127]; positive regulation of lipid storage [GO:0010884]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of miRNA metabolic process [GO:2000630]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; response to copper ion [GO:0046688]; response to muscle stretch [GO:0035994]; response to oxidative stress [GO:0006979]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]actinin binding [GO:0042805]; chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; regulatory region DNA binding [GO:0000975]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]; transcription regulatory region sequence-specific DNA binding [GO:0000976]cytoplasm [GO:0005737]; cytosol [GO:0005829]; I-kappaB/NF-kappaB complex [GO:0033256]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. {ECO:0000269|PubMed:15485931}.P30044PRDX5Peroxiredoxin-5, mitochondrialSUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.; SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm. Peroxisome.apoptotic process [GO:0006915]; cellular response to reactive oxygen species [GO:0034614]; gene expression [GO:0010467]; hydrogen peroxide catabolic process [GO:0042744]; inflammatory response [GO:0006954]; NADPH oxidation [GO:0070995]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of oxidoreductase activity [GO:0051354]; negative regulation of transcription from RNA polymerase III promoter [GO:0016480]; positive regulation of collagen biosynthetic process [GO:0032967]; reactive nitrogen species metabolic process [GO:2001057]; regulation of apoptosis involved in tissue homeostasis [GO:0060785]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; transcription initiation from RNA polymerase II promoter [GO:0006367]|antioxidant activity [GO:0016209]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; peroxynitrite reductase activity [GO:0072541]; protein dimerization activity [GO:0046983]; receptor binding [GO:0005102]; RNA polymerase III regulatory region DNA binding [GO:0001016]cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.Q9UK59DBR1Lariat debranching enzyme< mRNA splicing, via spliceosome [GO:0000398]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; RNA splicing, via transesterification reactions [GO:0000375]umetal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA lariat debranching enzyme activity [GO:0008419]FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis. {ECO:0000269|PubMed:10982890, ECO:0000269|PubMed:16232320}.Q7L2H7EIF3M4Eukaryotic translation initiation factor 3 subunit MBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.cytoplasmic translational initiation [GO:0002183]; formation of translation preinitiation complex [GO:0001731]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413]eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]dFUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2). {ECO:0000255|HAMAP-Rule:MF_03012, ECO:0000269|PubMed:15919898, ECO:0000269|PubMed:17403899}.P21980TGM2-Protein-glutamine gamma-glutamyltransferase 2apoptotic cell clearance [GO:0043277]; branching involved in salivary gland morphogenesis [GO:0060445]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; peptide cross-linking [GO:0018149]; phospholipase C-activating G-protein coupled receptor signaling pathway [GO:0007200]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell adhesion [GO:0045785]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; salivary gland cavitation [GO:0060662]ametal ion binding [GO:0046872]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intrinsic component of plasma membrane [GO:0031226]; mitochondrion [GO:0005739]`FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.Q9BY43CHM4A&Charged multivesicular body protein 4a:SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated. Localizes to large vesicle-like structures. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; membrane budding [GO:0006900]; membrane invagination [GO:0010324]; membrane organization [GO:0061024]; membrane tubulation [GO:0097320]; mitotic metaphase plate congression [GO:0007080]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of neuron death [GO:1901215]; nucleus organization [GO:0006997]; posttranslational protein targeting to membrane [GO:0006620]; protein homooligomerization [GO:0051260]; protein polymerization [GO:0051258]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]:cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane coat [GO:0030117]; midbody [GO:0030496]; nucleus [GO:0005634]FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:18209100}.Q9NXZ1SAGE1Sarcoma antigen 1Q68DQ2CRBG3"Very large A-kinase anchor proteinFUNCTION: Isoform vlAKAP: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). {ECO:0000269|PubMed:25097019}.P39060COIA1Collagen alpha-1(XVIII) chainfangiogenesis [GO:0001525]; cell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; endothelial cell morphogenesis [GO:0001886]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of cell proliferation [GO:0008285]; organ morphogenesis [GO:0009887]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of endothelial cell apoptotic process [GO:2000353]; response to drug [GO:0042493]; response to hydrostatic pressure [GO:0051599]; visual perception [GO:0007601]qidentical protein binding [GO:0042802]; metal ion binding [GO:0046872]; structural molecule activity [GO:0005198]basement membrane [GO:0005604]; collagen trimer [GO:0005581]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]GFUNCTION: COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.; FUNCTION: Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.Q9BRP4PAAF1&Proteasomal ATPase-associated factor 1viral process [GO:0016032]proteasome complex [GO:0000502]FUNCTION: Inhibits proteasome 26S assembly and proteolytic activity by impairing the association of the 19S regulatory complex with the 20S core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 promoter, where it promotes the recruitment of 19S regulatory complex through dissociation of the proteasome 26S. This presumably promotes provirus transcription efficie< ncy. Protects SUPT6H from proteasomal degradation. {ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:17289585, ECO:0000269|PubMed:22316138}.Q9UNY4TTF2"Transcription termination factor 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15125840}. Nucleus {ECO:0000269|PubMed:15125840}. Note=Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis.DNA-templated transcription, termination [GO:0006353]; mRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]ATP binding [GO:0005524]; ATP-dependent helicase activity [GO:0008026]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; zinc ion binding [GO:0008270]ocytoplasm [GO:0005737]; spliceosomal complex [GO:0005681]; transcription elongation factor complex [GO:0008023]yFUNCTION: DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing. {ECO:0000269|PubMed:10455150, ECO:0000269|PubMed:12927788, ECO:0000269|PubMed:15125840, ECO:0000269|PubMed:9748214}.Q96NC0ZMAT2!Zinc finger matrin-type protein 2U4/U6Q9H8H2DDX31)Probable ATP-dependent RNA helicase DDX31kGolgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]=FUNCTION: Probable ATP-dependent RNA helicase. {ECO:0000250}.P42771CD2A14Cyclin-dependent kinase inhibitor 2A, isoforms 1/2/3eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17658461}. Nucleus {ECO:0000269|PubMed:17658461}.cell cycle arrest [GO:0007050]; cellular senescence [GO:0090398]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; negative regulation of cell growth [GO:0030308]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of phosphorylation [GO:0042326]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cellular senescence [GO:2000774]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; Ras protein signal transduction [GO:0007265]; replicative senescence [GO:0090399]; senescence-associated heterochromatin focus assembly [GO:0035986]cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; NF-kappaB binding [GO:0051059]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]|cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; senescence-associated heterochromatin focus [GO:0035985]FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein. {ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:7972006}.Q16222UAP1(UDP-N-acetylhexosamine pyrophosphorylaseSUBCELLULAR LOCATION: Cytoplasm. Note=In spermatozoa, localized to the principal piece of the tail, the neck region of the head and to a lesser extent, the midpiece of the tail.cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; UDP-N-acetylglucosamine diphosphorylase activity [GO:0003977]FUNCTION: Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.Q9UBK8MTRRMethionine synthase reductaseSUBCELLULAR LOCATION: Isoform B: Cytoplasm.; SUBCELLULAR LOCATION: Isoform C: Cytoplasm.; SUBCELLULAR LOCATION: Isoform A: Cytoplasm {ECO:0000269|PubMed:18221906}.cellular nitrogen compound metabolic process [GO:0034641]; cobalamin metabolic process [GO:0009235]; DNA methylation [GO:0006306]; folic acid metabolic process [GO:0046655]; homocysteine catabolic process [GO:0043418]; methionine biosynthetic process [GO:0009086]; methionine metabolic process [GO:0006555]; methylation [GO:0032259]; negative regulation of cystathionine beta-synthase activity [GO:1904042]; oxidation-reduction process [GO:0055114]; S-adenosylmethionine cycle [GO:0033353]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]; xenobiotic metabolic process [GO:0006805]c[methionine synthase] reductase activity [GO:0030586]; aquacobalamin reductase (NADPH) activity [GO:0050444]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; iron ion binding [GO:0005506]; NADP binding [GO:0050661]; NADPH binding [GO:0070402]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor [GO:0016723]wcytoplasm [GO:0005737]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]FUNCTION: Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects. {ECO:0000269|PubMed:17892308}.Q9NW64RBM22Pre-mRNA-splicing factor RBM22SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol.4cellular response to drug [GO:0035690]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of RNA splicing [GO:0033120]; protein import into nucleus, translocation [GO:0000060]calcium-dependent protein binding [GO:0048306]; metal ion binding [GO:0046872]; nucleocytoplasmic transporter activity [GO:0005487]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; pre-mRNA binding [GO:0036002]; snRNA binding [GO:0017069]qcatalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses. {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:22246180}.O15056SYNJ2Synaptojanin-2zSUBCELLULAR LOCATION: Membrane {ECO:0000250}. Note=Predominantly associated with the particulate fractions. {ECO:0000250}.nucleotide binding [GO:0000166]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; RNA binding [GO:0003723]FUNCTION: Inositol 5-phosphatase which may be involved in distinct membra< ne trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis.Q8NHM4TRY6Putative trypsin-6'endothelial cell migration [GO:0043542]Ometal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]EFUNCTION: May regulate cell migration. {ECO:0000269|PubMed:15313892}.P50443S26A2Sulfate transporter3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; ion transport [GO:0006811]; ossification [GO:0001503]; small molecule metabolic process [GO:0044281]; sulfate transport [GO:0008272]; transmembrane transport [GO:0055085]; xenobiotic metabolic process [GO:0006805]secondary active sulfate transmembrane transporter activity [GO:0008271]; sulfate transmembrane transporter activity [GO:0015116]extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]NFUNCTION: Sulfate transporter. May play a role in endochondral bone formation.P26196DDX6(Probable ATP-dependent RNA helicase DDX6SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22915799}.cytoplasmic mRNA processing body assembly [GO:0033962]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; negative regulation of neuron differentiation [GO:0045665]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; regulation of translation [GO:0006417]; RNA secondary structure unwinding [GO:0010501]; stem cell maintenance [GO:0019827]; viral RNA genome packaging [GO:0019074]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; RNA helicase activity [GO:0003724]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; RISC complex [GO:0016442]PFUNCTION: In the process of mRNA degradation, may play a role in mRNA decapping.P55884EIF3B4Eukaryotic translation initiation factor 3 subunit BBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.{nucleotide binding [GO:0000166]; protein complex scaffold [GO:0032947]; translation initiation factor activity [GO:0003743]Ycytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. {ECO:0000269|PubMed:9388245}.Q8WYB5KAT6BHistone acetyltransferase KAT6BK-acetyltransferaseschromatin organization [GO:0006325]; histone acetylation [GO:0016573]; histone H3 acetylation [GO:0043966]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleosome assembly [GO:0006334]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]acetyltransferase activity [GO:0016407]; DNA binding [GO:0003677]; histone acetyltransferase activity [GO:0004402]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]FUNCTION: Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:10497217, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:16387653}.Q8NDH3PEPL1Probable aminopeptidase NPEPL1gFUNCTION: Probably catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.Q00653NFKB2&Nuclear factor NF-kappa-B p100 subunitTranscriptional factorvaging [GO:0007568]; extracellular matrix organization [GO:0030198]; follicular dendritic cell differentiation [GO:0002268]; germinal center formation [GO:0002467]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; NIK/NF-kappaB signaling [GO:0038061]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of transcription, DNA-templated [GO:0006355]; response to cytokine [GO:0034097]; response to lipopolysaccharide [GO:0032496]; rhythmic process [GO:0048511]; spleen development [GO:0048536]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]chromatin binding [GO:0003682]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]Bcl3/NF-kappaB2 complex [GO:0033257]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcrip< tional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000269|PubMed:7925301}.Q9P253VPS186Vacuolar protein sorting-associated protein 18 homolog:SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:11382755}; Peripheral membrane protein {ECO:0000269|PubMed:11382755}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:11382755}; Peripheral membrane protein {ECO:0000269|PubMed:11382755}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:18552835}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}. Note=Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes.2endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; lysosome organization [GO:0007040]; regulation of SNARE complex assembly [GO:0035542]; vesicle docking involved in exocytosis [GO:0006904]; viral entry into host cell [GO:0046718]emetal ion binding [GO:0046872]; protein binding, bridging [GO:0030674]; syntaxin binding [GO:0019905]actin filament [GO:0005884]; early endosome [GO:0005769]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25783203). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). Involved in dendrite development of Pukinje cells (By similarity). {ECO:0000250|UniProtKB:Q8R307, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25783203}.P48729KC1ACasein kinase I isoform alphaSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Nucleus speckle. Note=Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis.cell division [GO:0051301]; cell surface receptor signaling pathway [GO:0007166]; mitotic nuclear division [GO:0007067]; peptidyl-serine phosphorylation [GO:0018105]; phagocytosis [GO:0006909]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear speck [GO:0016607]; primary cilium [GO:0072372]FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. {ECO:0000269|PubMed:11955436, ECO:0000269|PubMed:1409656, ECO:0000269|PubMed:18305108}.H0YM25GG6LV+Golgin subfamily A member 6-like protein 22P57087JAM2Junctional adhesion molecule BSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Localized at tight junctions of both epithelial and endothelial cells. {ECO:0000250}.blood coagulation [GO:0007596]; extracellular matrix organization [GO:0030198]; leukocyte migration [GO:0050900]; negative regulation of cell adhesion [GO:0007162]; single organismal cell-cell adhesion [GO:0016337]xbicellular tight junction [GO:0005923]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]]FUNCTION: May play a role in the processes of lymphocyte homing to secondary lymphoid organs.Q96BH1RNF25!E3 ubiquitin-protein ligase RNF25ppositive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein ubiquitination [GO:0016567]ligase activity [GO:0016874]; NF-kappaB binding [GO:0051059]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B. {ECO:0000250, ECO:0000269|PubMed:12748188}.Q01082SPTB2'Spectrin beta chain, non-erythrocytic 1kSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}. Note=Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.Oactin filament capping [GO:0051693]; axon guidance [GO:0007411]; common-partner SMAD protein phosphorylation [GO:0007182]; Golgi to plasma membrane protein transport [GO:0043001]; membrane assembly [GO:0071709]; mitotic cytokinesis [GO:0000281]; plasma membrane organization [GO:0007009]; positive regulation of interleukin-2 secretion [GO:1900042]; positive regulation of protein localization to plasma membrane [GO:1903078]; protein targeting to plasma membrane [GO:0072661]; regulation of protein localization to plasma membrane [GO:1903076]; SMAD protein import into nucleus [GO:0007184]actin binding [GO:0003779]; ankyrin binding [GO:0030506]; GTPase binding [GO:0051020]; phospholipid binding [GO:0005543]; poly(A) RNA binding [GO:0044822]; structural constituent of cytoskeleton [GO:0005200]$axolemma [GO:0030673]; cuticular plate < [GO:0032437]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; M band [GO:0031430]; neuronal postsynaptic density [GO:0097481]; nucleolus [GO:0005730]; spectrin [GO:0008091]; spectrin-associated cytoskeleton [GO:0014731]Q9UJY1HSPB8Heat shock protein beta-8sHSPSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Translocates to nuclear foci during heat shock.cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]<FUNCTION: Displays temperature-dependent chaperone activity.Q9Y6N7ROBO1Roundabout homolog 1immunoglobulin receptor superfamily(PC00124);immunoglobulin superfamily cell adhesion molecule(PC00125);protein phosphatase(PC00195)<activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; cell adhesion [GO:0007155]; cell migration involved in sprouting angiogenesis [GO:0002042]; chemorepulsion involved in postnatal olfactory bulb interneuron migration [GO:0021836]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; mammary duct terminal end bud growth [GO:0060763]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of mammary gland epithelial cell proliferation [GO:0033600]; negative regulation of negative chemotaxis [GO:0050925]; nervous system development [GO:0007399]; positive regulation of axonogenesis [GO:0050772]; Roundabout signaling pathway [GO:0035385]uaxon guidance receptor activity [GO:0008046]; identical protein binding [GO:0042802]; LRR domain binding [GO:0030275]axolemma [GO:0030673]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development. {ECO:0000269|PubMed:10102268}.Q9BT17MTG1*Mitochondrial ribosome-associated GTPase 1mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial ribosome [GO:0005761]; mitochondrion [GO:0005739]FUNCTION: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity. {ECO:0000269|PubMed:23396448}.Q15742NAB2NGFI-A-binding protein 2kSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Isoform 2 is not localized to the nucleus. {ECO:0000250}.fcell proliferation [GO:0008283]; endochondral ossification [GO:0001958]; myelination [GO:0042552]; negative regulation of transcription from RNA polymerase III promoter [GO:0016480]; nervous system development [GO:0007399]; regulation of epidermis development [GO:0045682]; Schwann cell differentiation [GO:0014037]; transcription, DNA-templated [GO:0006351]FUNCTION: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity). {ECO:0000250}.Q96Q05TPPC9.Trafficking protein particle complex subunit 9SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Processes and cell bodies of neurons. {ECO:0000250}.FUNCTION: Functions as an activator of NF-kappa-B through increased phosphorylation of the IKK complex. May function in neuronal cells differentiation. May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:15951441}.Q14254FLOT2 Flotillin-2?SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20682791}; Peripheral membrane protein {ECO:0000269|PubMed:20682791}. Membrane, caveola {ECO:0000269|PubMed:20682791}; Peripheral membrane protein {ECO:0000269|PubMed:20682791}. Endosome {ECO:0000269|PubMed:20682791}. Note=Membrane-associated protein of caveolae. cell adhesion [GO:0007155]; epidermis development [GO:0008544]; establishment of protein localization to plasma membrane [GO:0090002]; membrane raft assembly [GO:0001765]; negative regulation of amyloid precursor protein catabolic process [GO:1902992]; negative regulation of gene expression [GO:0010629]; positive regulation of establishment of T cell polarity [GO:1903905]; protein localization to plasma membrane raft [GO:0044860]; protein stabilization [GO:0050821]; regulation of myoblast differentiation [GO:0045661]0protein heterodimerization activity [GO:0046982]acrosomal membrane [GO:0002080]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell adherens junction [GO:0005913]; cell-cell contact zone [GO:0044291]; cytoplasmic vesicle [GO:0031410]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; flotillin complex [GO:0016600]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; uropod [GO:0001931]; vesicle [GO:0031982]FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. May be involved in epidermal cell adhesion and epidermal structure and function.Q9NZN8CNOT2(CCR4-NOT transcription complex subunit 2eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21299754}. Nucleus {ECO:0000305|PubMed:21299754}.gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606]; regulation of stem cell maintenance [GO:2000036]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of translation [GO:0006417]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; transcription, DNA-templated [GO:0006351]; trophectodermal cell differentiation [GO:0001829]RNA polymerase II transcription cofactor activity [GO:0001104]; RNA polymerase II transcription corepressor binding [GO:0001226]xCCR4-NOT complex [GO:0030014]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]6FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specificly involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:16712523, ECO:0000269|PubMed:21299754, ECO:0000269|PubMed:22367759}.Q14112NID2 Nidogen-2basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; extracellular matrix organization [GO:0030198]?calcium ion binding [GO:0005509]; collagen binding [GO:0005518]basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]FUNCTION: Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV,< to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell-extracellular matrix interactions.Q9BYJ9YTHD1&YTH domain-containing family protein 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:26046440}.<positive regulation of translational initiation [GO:0045948]wN6-methyladenosine-containing RNA binding [GO:1990247]; poly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]xFUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and promotes mRNA translation efficiency (PubMed:24284625, PubMed:26046440). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:24284625). Acts as a regulator of mRNA translation efficiency: promotes ribosome loading to m6A-containing mRNAs and interacts with translation initiation factors eIF3 (EIF3A or EIF3B) to facilitate translation initiation (PubMed:26046440). {ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:26046440}.Q9Y2P8RCL1.RNA 3'-terminal phosphate cyclase-like proteineendonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000479]@endoribonuclease activity [GO:0004521]; RNA binding [GO:0003723]FUNCTION: Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA (By similarity). {ECO:0000250}.Q9BZE9ASPC1&Tether containing UBX domain for GLUT4-SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:22207755}; Peripheral membrane protein. Cytoplasm {ECO:0000269|PubMed:23349634}. Nucleus {ECO:0000269|PubMed:23349634}.glucose homeostasis [GO:0042593]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; regulation of glucose import [GO:0046324]cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; extrinsic component of membrane [GO:0019898]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506] FUNCTION: Tethering protein that sequesters GLUT4-containing vesicles in the cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that is available at the cell surface (By similarity). Enhances VCP methylation catalyzed by VCPKMT. {ECO:0000250, ECO:0000269|PubMed:23349634}.O14613BORG1Cdc42 effector protein 2SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:11035016}; Peripheral membrane protein {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11035016}.actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein complex assembly [GO:0031334]; positive regulation of pseudopodium assembly [GO:0031274]; regulation of cell shape [GO:0008360]; Rho protein signal transduction [GO:0007266]DGTPase activator activity [GO:0005096]; GTP-Rho binding [GO:0017049]cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]-FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}.Q16584M3K111Mitogen-activated protein kinase kinase kinase 11SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12529434}. Note=Location is cell cycle dependent.activation of JUN kinase activity [GO:0007257]; activation of MAPK activity [GO:0000187]; cell death [GO:0008219]; cell proliferation [GO:0008283]; JNK cascade [GO:0007254]; microtubule-based process [GO:0007017]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of neuron apoptotic process [GO:0043525]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]qATP binding [GO:0005524]; identical protein binding [GO:0042802]; JUN kinase kinase kinase activity [GO:0004706]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]`centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule [GO:0005874]!FUNCTION: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle. {ECO:0000269|PubMed:12529434, ECO:0000269|PubMed:15258589, ECO:0000269|PubMed:8195146, ECO:0000269|PubMed:9003778}.Q7L592NDUF7<NADH dehydrogenase [ubiquinone] complex I, assembly factor 7BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20406883}.Ymethylation [GO:0032259]; mitochondrial respiratory chain complex I assembly [GO:0032981]Denzyme binding [GO:0019899]; methyltransferase activity [GO:0008168]<extracellular space [GO:0005615]; mitochondrion [GO:0005739]FUNCTION: Involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). {ECO:0000269|PubMed:20406883}.Q86V81THOC4THO complex subunit 4kSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur..gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; regulation of DNA recombination [GO:0000018]; replication fork processing [GO:0031297]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]; viral mRNA export from host cell nucleus [GO:0046784](catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription export complex [GO:0000346]FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX com< plex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability. {ECO:0000269|PubMed:25662211}.; FUNCTION: Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation.P78332RBM6RNA-binding protein 6uDNA binding [GO:0003677]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]?FUNCTION: Specifically binds poly(G) RNA homopolymers in vitro.Q9UGR2Z3H7B-Zinc finger CCCH domain-containing protein 7BSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18799579}. Note=Nuclear localization seems to be depleted upon rotavirus A infection.Q5SQS7SH24B SH2 domain-containing protein 4BQ9Y6K8KAD5Adenylate kinase isoenzyme 5>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19647735}.ADP biosynthetic process [GO:0006172]; ATP metabolic process [GO:0046034]; dADP biosynthetic process [GO:0006173]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside diphosphate phosphorylation [GO:0006165]; nucleoside triphosphate biosynthetic process [GO:0009142]; pyrimidine ribonucleotide biosynthetic process [GO:0009220]; small molecule metabolic process [GO:0044281]adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside kinase activity [GO:0019206]Xcytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:19647735, ECO:0000269|PubMed:23416111}.Q9Y4L5RN115"E3 ubiquitin-protein ligase RNF115SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D0C1}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes. {ECO:0000250|UniProtKB:Q9D0C1}.Gnegative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]FUNCTION: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4. {ECO:0000269|PubMed:16288031, ECO:0000269|PubMed:18819927, ECO:0000303|PubMed:23418353}.Q16352AINXAlpha-internexincell differentiation [GO:0030154]; neurofilament cytoskeleton organization [GO:0060052]; substantia nigra development [GO:0021762]cytoplasmic ribonucleoprotein granule [GO:0036464]; extracellular space [GO:0005615]; intermediate filament cytoskeleton [GO:0045111]; myelin sheath [GO:0043209]; neurofilament [GO:0005883]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]VFUNCTION: Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges.P49419AL7A1,Alpha-aminoadipic semialdehyde dehydrogenaseSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20207735}. Nucleus {ECO:0000269|PubMed:20207735}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol.+cellular aldehyde metabolic process [GO:0006081]; cellular nitrogen compound metabolic process [GO:0034641]; glycine betaine biosynthetic process from choline [GO:0019285]; lysine catabolic process [GO:0006554]; sensory perception of sound [GO:0007605]; small molecule metabolic process [GO:0044281]aldehyde dehydrogenase (NAD) activity [GO:0004029]; betaine-aldehyde dehydrogenase activity [GO:0008802]; L-aminoadipate-semialdehyde dehydrogenase activity [GO:0004043]dFUNCTION: Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism. {ECO:0000269|PubMed:16491085, ECO:0000269|PubMed:20207735}.Q5T5C0STXB5Syntaxin-binding protein 5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Cytoplasmic, and associated with vesicular membranes and the plasma membrane. Detected at synapses and on synaptic vesicles (By similarity). {ECO:0000250}.exocytosis [GO:0006887]; positive regulation of exocytosis [GO:0045921]; protein transport [GO:0015031]; regulation of blood coagulation [GO:0030193]; regulation of exocytosis [GO:0017157]; regulation of gene expression [GO:0010468]syntaxin-1 binding [GO:0017075]acetylcholine-gated channel complex [GO:0005892]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; synaptic vesicle [GO:0008021]FUNCTION: Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane. Competes with STXBP1 for STX1 binding (By similarity). {ECO:0000250}.Q6KC79NIPBLNipped-B-like proteinbrain development [GO:0007420]; cellular protein localization [GO:0034613]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to X-ray [GO:0071481]; cognition [GO:0050890]; developmental growth [GO:0048589]; ear morphogenesis [GO:0042471]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic forelimb morphogenesis [GO:0035115]; embryonic viscerocranium morphogenesis [GO:0048703]; external genitalia morphogenesis [GO:0035261]; eye morphogenesis [GO:0048592]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; forelimb morphogenesis [GO:0035136]; gall bladder development [GO:0061010]; heart morphogenesis [GO:0003007]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; metanephros development [GO:0001656]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; outflow tract morphogenesis [GO:0003151]; positive regulation of histone deacetylation [GO:0031065]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of ossification [GO:0045778]; positive regulation of transcription from RNA polymera< se II promoter [GO:0045944]; regulation of developmental growth [GO:0048638]; regulation of embryonic development [GO:0045995]; regulation of hair cycle [GO:0042634]; sensory perception of sound [GO:0007605]; stem cell maintenance [GO:0019827]; uterus morphogenesis [GO:0061038]chromatin binding [GO:0003682]; chromo shadow domain binding [GO:0070087]; histone deacetylase binding [GO:0042826]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]chromatin [GO:0000785]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMC loading complex [GO:0032116]FUNCTION: Probably plays a structural role in chromatin. Involved in sister chromatid cohesion, possibly by interacting with the cohesin complex (By similarity). {ECO:0000250}.O43172PRP4*U4/U6 small nuclear ribonucleoprotein Prp4nSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Colocalizes with spliceosomal snRNPs. {ECO:0000250}.<U4 snRNA binding [GO:0030621]; U6 snRNA binding [GO:0017070]Cajal body [GO:0015030]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]FUNCTION: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.Q8TBC3SHKB1SH3KBP1-binding protein 1Q9HB19PKHA27Pleckstrin homology domain-containing family A member 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2. {ECO:0000250}.8positive regulation of cell-matrix adhesion [GO:0001954]Zfibronectin binding [GO:0001968]; laminin binding [GO:0043236]; lipid binding [GO:0008289]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity). {ECO:0000250}.P02768ALBU Serum albuminbile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; blood coagulation [GO:0007596]; cellular response to starvation [GO:0009267]; hemolysis by symbiont of host erythrocytes [GO:0019836]; lipoprotein metabolic process [GO:0042157]; maintenance of mitochondrion location [GO:0051659]; negative regulation of apoptotic process [GO:0043066]; negative regulation of programmed cell death [GO:0043069]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; receptor-mediated endocytosis [GO:0006898]; retina homeostasis [GO:0001895]; small molecule metabolic process [GO:0044281]; sodium-independent organic anion transport [GO:0043252]; transmembrane transport [GO:0055085]; transport [GO:0006810]antioxidant activity [GO:0016209]; chaperone binding [GO:0051087]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; drug binding [GO:0008144]; fatty acid binding [GO:0005504]; pyridoxal phosphate binding [GO:0030170]; toxic substance binding [GO:0015643]blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; platelet alpha granule lumen [GO:0031093]; protein complex [GO:0043234][FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. {ECO:0000269|PubMed:19021548}.P20020AT2B1-Plasma membrane calcium-transporting ATPase 1aging [GO:0007568]; blood coagulation [GO:0007596]; brain development [GO:0007420]; calcium ion export [GO:1901660]; cellular response to corticosterone stimulus [GO:0071386]; cellular response to vitamin D [GO:0071305]; ion transmembrane transport [GO:0034220]; neural retina development [GO:0003407]; response to cold [GO:0009409]; transmembrane transport [GO:0055085]; transport [GO:0006810]kATP binding [GO:0005524]; calcium-transporting ATPase activity [GO:0005388]; metal ion binding [GO:0046872]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; dendrite membrane [GO:0032590]; dendritic spine membrane [GO:0032591]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuronal cell body membrane [GO:0032809]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.Q9NPJ6MED45Mediator of RNA polymerase II transcription subunit 4Zandrogen receptor signaling pathway [GO:0030521]; gene expression [GO:0010467]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]7ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; receptor activity [GO:0004872]; RNA polymerase II transcription cofactor activity [GO:0001104]; thyroid hormone receptor binding [GO:0046966]; transcription cofactor activity [GO:0003712]; vitamin D receptor binding [GO:0042809]O00541PESCPescadillo homologSUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. {ECO:0000255|HAMAP-Rule:MF_03028}.cell proliferation [GO:0008283]; maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000466]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; nucleolus organization [GO:0007000]; protein localization to organelle [GO:0033365]; regulation of cell cycle [GO:0051726]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PeBoW complex [GO:0070545]; preribosome, large subunit precursor [GO:0030687]FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269}.Q8IUW5RELL1RELT-like protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16389068}; Single-pass type I membrane protein {ECO:0000269|PubMed:16389068}.pintegral component of membrane [GO:0016021]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]Q5VT25MRCKA*Serine/threonine-protein kinase MRCK alpha SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). {ECO:0000250}.%actin cytoskeleton reorganization [GO:0031532]; actomyosin structure organization [GO:0031032]; cell migration [GO:0016477]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; nuclear migration [GO:0007097]; protein phosphorylation [GO:0006468]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein serine/threonine kinase activity [GO:0004674]actomyosin [GO:0042641]; cell-cell junction [GO:0005911]; cell leading edge [GO:0031252]; cytoplasm [GO:000< 5737]; extracellular exosome [GO:0070062]FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. {ECO:0000269|PubMed:11340065, ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:15723050, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:20188707, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:9092543, ECO:0000269|PubMed:9418861}.Q8N2M8CLASR-CLK4-associating serine/arginine rich proteinFUNCTION: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity). {ECO:0000250}.Q9Y2K7KDM2ALysine-specific demethylase 2A)SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:20417597}. Note=Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2.chromatin organization [GO:0006325]; double-strand break repair via nonhomologous end joining [GO:0006303]; histone H3-K36 demethylation [GO:0070544]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]histone demethylase activity (H3-K36 specific) [GO:0051864]; unmethylated CpG binding [GO:0045322]; zinc ion binding [GO:0008270]fnuclear chromatin [GO:0000790]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:19001877}.O14545TRAD11TRAF-type zinc finger domain-containing protein 1:negative regulation of innate immune response [GO:0045824]FUNCTION: Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity). {ECO:0000250}.P29466CASP1 Caspase-1$activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; cellular response to organic substance [GO:0071310]; innate immune response [GO:0045087]; interleukin-1 beta production [GO:0032611]; membrane hyperpolarization [GO:0060081]; mitochondrial depolarization [GO:0051882]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-1 alpha secretion [GO:0050717]; positive regulation of interleukin-1 beta secretion [GO:0050718]; programmed necrotic cell death [GO:0097300]; proteolysis [GO:0006508]; pyroptosis [GO:0070269]; regulation of autophagy [GO:0010506]; regulation of inflammatory response [GO:0050727]; response to ATP [GO:0033198]; response to hypoxia [GO:0001666]; response to lipopolysaccharide [GO:0032496]; signal transduction [GO:0007165]; toxin transport [GO:1901998]cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activity [GO:0004175] AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; IPAF inflammasome complex [GO:0072557]; mitochondrion [GO:0005739]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]mFUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. {ECO:0000269|PubMed:15498465, ECO:0000269|PubMed:7876192}.Q96FZ7CHMP6%Charged multivesicular body protein 6SUBCELLULAR LOCATION: Endomembrane system. Endosome membrane; Lipid-anchor. Late endosome membrane {ECO:0000305}. Note=Localizes to endosomal membranes.xcell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; nucleus organization [GO:0006997]; protein transport [GO:0015031]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]cytosol [GO:0005829]; endosome membrane [GO:0010008]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; membrane [GO:0016020]FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.O95980RECK:Reversion-inducing cysteine-rich protein with Kazal motifsblood vessel maturation [GO:0001955]; embryo implantation [GO:0007566]; extracellular matrix organization [GO:0030198]; negative regulation of endopeptidase activity [GO:0010951]endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867]`anchored component of membrane [GO:0031225]; membrane [GO:0016020]; plasma membrane [GO:0005886]BFUNCTION: Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.Q9NUQ7UFSP2Ufm1-specific protease 2jSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}.fproteolysis [GO:0006508]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]Pthiolester hydrolase activity [GO:0016790]; UFM1 hydrolase activity [GO:0071567]< FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins. Through TRIP4 deufmylation may regulate intracellular nuclear receptors transactivation and thereby regulate cell proliferation and differentiation. {ECO:0000269|PubMed:25219498}.Q5UCC4EMC10&ER membrane protein complex subunit 10{SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Secreted.xER membrane protein complex [GO:0072546]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]Q8WXF7ATLA1 Atlastin-1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell projection, axon {ECO:0000250}.taxonogenesis [GO:0007409]; endoplasmic reticulum organization [GO:0007029]; protein homooligomerization [GO:0051260]axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi cis cisterna [GO:0000137]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development. {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:25751282}.Q7Z3D4LYSM3CLysM and putative peptidoglycan-binding domain-containing protein 3Q6P4F2ADXL'Adrenodoxin-like protein, mitochondrialfSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20547883}. Mitochondrion matrix {ECO:0000250}.C21-steroid hormone biosynthetic process [GO:0006700]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]; sterol metabolic process [GO:0016125]; xenobiotic metabolic process [GO:0006805]\FUNCTION: Essential for heme A and Fe/S protein biosynthesis. {ECO:0000269|PubMed:20547883}.Q9Y240CLC11'C-type lectin domain family 11 member AfSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11803813}. Secreted {ECO:0000269|PubMed:11803813}.Fcarbohydrate binding [GO:0030246]; growth factor activity [GO:0008083][cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]aFUNCTION: Stimulates the proliferation and differentiation of hematopoietic precursor cells from various lineages, including erythrocytes, lymphocytes, granulocytes and macrophages. Acts synergistically with other cytokines, including IL-3, GCSF, GMCSF and FLT3 ligand. Suppresses SCF-stimulated erythrocyte proliferation. {ECO:0000269|PubMed:11920266}.Q99541PLIN2 Perilipin-2cellular lipid metabolic process [GO:0044255]; lipid storage [GO:0019915]; long-chain fatty acid transport [GO:0015909]; response to drug [GO:0042493]; response to organic cyclic compound [GO:0014070]; small molecule metabolic process [GO:0044281]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; lipid particle [GO:0005811]; nucleus [GO:0005634]; plasma membrane [GO:0005886]ZFUNCTION: May be involved in development and maintenance of adipose tissue. {ECO:0000250}.Q9NUL5CS066UPF0515 protein C19orf66Q5VT06CE350!Centrosome-associated protein 350SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus. Note=Associated with mitotic spindles. Nuclear, in discrete foci. Associated with intermediate filaments. Also present in the pericentrosomal area."microtubule anchoring [GO:0034453]vcentrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; spindle [GO:0005819]FUNCTION: Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity. {ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:18412956, ECO:0000269|PubMed:19052644}.Q9UBC3DNM3B%DNA (cytosine-5)-methyltransferase 3BYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11735126, ECO:0000269|PubMed:12145218}.C-5 methylation of cytosine [GO:0090116]; cellular response to amino acid stimulus [GO:0071230]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hyperoxia [GO:0071455]; DNA methylation [GO:0006306]; DNA methylation on cytosine [GO:0032776]; DNA methylation on cytosine within a CG sequence [GO:0010424]; gene expression [GO:0010467]; inactivation of X chromosome by DNA methylation [GO:0060821]; methylation-dependent chromatin silencing [GO:0006346]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of histone H3-K9 methylation [GO:0051573]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of gene expression [GO:0010628]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of neuron differentiation [GO:0045666]; protein complex localization [GO:0031503]; regulation of gene expression, epigenetic [GO:0040029]; regulation of gene expression by genetic imprinting [GO:0006349]; response to activity [GO:0014823]; response to caffeine [GO:0031000]; response to cocaine [GO:0042220]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to ionizing radiation [GO:0010212]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; S-adenosylhomocysteine metabolic process [GO:0046498]; S-adenosylmethioninamine metabolic process [GO:0046499]Schromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates [GO:0051718]; DNA-methyltransferase activity [GO:0009008]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; unmethylated CpG binding [GO:0045322]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear heterochromatin [GO:0005720]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity). In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. {ECO:0000250, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:17303076, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18567530}.Q9ULG6CCPG1 Cell cycle progression protein 1uSUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.cell cycle [GO:0007049]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of Rho guanyl-nucleotide exchange factor activity [GO:2001106]FUNCTION: Acts as an assembly platform for Rho protein sign< aling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42 (By similarity). May be involved in cell cycle regulation. {ECO:0000250, ECO:0000269|PubMed:9383053}.Q5TGL8PXDC1PX domain-containing protein 1Q9P2E2KIF17Kinesin-like protein KIF17cell projection organization [GO:0030030]; microtubule-based movement [GO:0007018]; organelle organization [GO:0006996]; protein complex localization [GO:0031503]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]bATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]-axoneme [GO:0005930]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; intraciliary transport particle B [GO:0030992]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; periciliary membrane compartment [GO:1990075]; photoreceptor connecting cilium [GO:0032391]; primary cilium [GO:0072372]sFUNCTION: Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. {ECO:0000250}.Q9C0E2XPO4 Exportin-4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16449645}. Nucleus {ECO:0000269|PubMed:16449645}. Note=Shuttles between the nucleus and the cytoplasm._positive regulation of protein export from nucleus [GO:0046827]; protein transport [GO:0015031]JFUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO4 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645}.Q3KR37GRM1B!GRAM domain-containing protein 1BQ99832TCPHT-complex protein 1 subunit eta?ATP binding [GO:0005524]; unfolded protein binding [GO:0051082]cell body [GO:0044297]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; zona pellucida receptor complex [GO:0002199]FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). {ECO:0000250}.Q16512PKN1"Serine/threonine-protein kinase N1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome. Cell membrane; Peripheral membrane protein. Cleavage furrow. Midbody. Note=Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-374 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis.5activation of JUN kinase activity [GO:0007257]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; histone H3-T11 phosphorylation [GO:0035407]; hyperosmotic response [GO:0006972]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein kinase activity [GO:0006469]; protein phosphorylation [GO:0006468]; regulation of cell motility [GO:2000145]; regulation of germinal center formation [GO:0002634]; regulation of immunoglobulin production [GO:0002637]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; renal system process [GO:0003014]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; spleen development [GO:0048536]; transcription, DNA-templated [GO:0006351]androgen receptor binding [GO:0050681]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; GTP-Rho binding [GO:0017049]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone kinase activity (H3-T11 specific) [GO:0035402]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; Rac GTPase binding [GO:0048365]cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endosome [GO:0005768]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]dFUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269|PubMed:11104762, ECO:0000269|PubMed:12514133, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:24248594, ECO:0000269|PubMed:8557118, ECO:0000269|PubMed:8621664, ECO:0000269|PubMed:9175763}.Q5BJD5TM41BTransmembrane protein 41B'nervous system development [GO:0007399]FFUNCTION: Required for normal motor neuron development. {ECO:0000250}.P54687BCAT15Branched-chain-amino-acid aminotransferase, cytosolic4branched-chain amino acid biosynthetic process [GO:0009082]; branched-chain amino acid catabolic process [GO:0009083]; cell proliferation [GO:0008283]; cellular nitrogen compound metabolic process [GO:0034641]; G1/S transition of mitotic cell cycle [GO:0000082]; small molecule metabolic process [GO:0044281]branched-chain-amino-acid transaminase activity [GO:0004084]; L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-valine transaminase activity [GO:0052655]FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.O95232LC7L3Luc7-like protein 3SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:12565863}. Note=The subnuclear localization is affected by cisplatin.BmRNA splice site selection [GO:0006376]; RNA splicing [GO:0008380]anuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U1 snRNP [GO:0005685]uFUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. {ECO:0000269|PubMed:16462885}.Q9BY49PECR'Peroxisomal trans-2-enoyl-CoA reductase?SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11669066}.}fatty acid biosynthetic process [GO:0006633]; oxidation-reduction process [GO:0055114]; phytol metabolic process [GO:0033306]Xreceptor binding [GO:0005102]; trans-2-enoyl-CoA reductase (NADPH) activity [GO:0019166]< intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]eFUNCTION: Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.Q9UIG0BAZ1BTyrosine-protein kinase BAZ1B<SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475, ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136}. Note=Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA.cellular response to DNA damage stimulus [GO:0006974]; chromatin assembly or disassembly [GO:0006333]; chromatin-mediated maintenance of transcription [GO:0048096]; double-strand break repair [GO:0006302]; heart morphogenesis [GO:0003007]; histone phosphorylation [GO:0016572]; peptidyl-tyrosine phosphorylation [GO:0018108]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]UATP binding [GO:0005524]; chromatin binding [GO:0003682]; histone kinase activity [GO:0035173]; lysine-acetylated histone binding [GO:0070577]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; vitamin D receptor activator activity [GO:0071884]; zinc ion binding [GO:0008270]acondensed chromosome [GO:0000793]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]8FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. {ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:19092802, ECO:0000269|PubMed:19234442}.O43707ACTN4Alpha-actinin-4sSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cytoplasm {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cell junction {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers. Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU-7). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:9508771}.'actin filament bundle assembly [GO:0051017]; bicellular tight junction assembly [GO:0070830]; blood coagulation [GO:0007596]; negative regulation of cellular component movement [GO:0051271]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of cell migration [GO:0030335]; positive regulation of cellular component movement [GO:0051272]; positive regulation of NIK/NF-kappaB signaling [GO:1901224]; positive regulation of pinocytosis [GO:0048549]; positive regulation of sodium:proton antiporter activity [GO:0032417]; protein localization to bicellular tight junction [GO:1902396]; protein transport [GO:0015031]; regulation of apoptotic process [GO:0042981]; regulation of nucleic acid-templated transcription [GO:1903506]; response to hypoxia [GO:0001666]; retinoic acid receptor signaling pathway [GO:0048384]; vesicle transport along actin filament [GO:0030050]8actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; chromatin DNA binding [GO:0031490]; integrin binding [GO:0005178]; ion channel binding [GO:0044325]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; nuclear hormone receptor binding [GO:0035257]; nucleoside binding [GO:0001882]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; retinoic acid receptor binding [GO:0042974]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]cell-cell junction [GO:0005911]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; intracellular [GO:0005622]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; platelet alpha granule lumen [GO:0031093]; protein complex [GO:0043234]; pseudopodium [GO:0031143]; ribonucleoprotein complex [GO:0030529]; stress fiber [GO:0001725]; Z disc [GO:0030018]=FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000305|PubMed:9508771}.O14776TCRG1$Transcription elongation regulator 1uSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10908677, ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:9315662}.negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription from RNA polymerase II promoter [GO:0006366]poly(A) RNA binding [GO:0044822]; RNA polymerase II repressing transcription factor binding [GO:0001103]; RNA polymerase II transcription corepressor activity [GO:0001106]; transcription coactivator activity [GO:0003713]Mactin cytoskeleton [GO:0015629]; nucleolus [GO:0005730]; nucleus [GO:0005634]_FUNCTION: Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter. {ECO:0000269|PubMed:11604498, ECO:0000269|PubMed:9315662}.Q6ZRP7QSOX2Sulfhydryl oxidase 2SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14633699}; Single-pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Seems to be predominantly targeted to the nuclear and outer plasma membrane.Acell redox homeostasis [GO:0045454]; protein folding [GO:0006457]extracellular space [GO:0005615]; integral component of Golgi membrane [GO:0030173]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]{FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins. Also seems to play a role in regulating the sensitization of neuroblastoma cells for interferon-gamma-induced apoptosi< s. {ECO:0000269|PubMed:14633699}.Q8TD16BICD2Protein bicaudal D homolog 2SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity). Its localization is dependent on microtubule morphology. {ECO:0000250}.microtubule anchoring at microtubule organizing center [GO:0072393]; minus-end-directed organelle transport along microtubule [GO:0072385]cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]>FUNCTION: May play a role in the dynein-dynactin interactions on the surface of membranous organelles, by associating with these complexes. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex (By similarity). {ECO:0000250}.Q01130SRSF2&Serine/arginine-rich splicing factor 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21157427}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21157427}. Nucleus speckle {ECO:0000269|PubMed:21157427}. Note=Phosphorylation by SRPK2 provokes its redistribution from the nuclear specke to nucleoplasm.gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of nucleic acid-templated transcription [GO:1903507]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; pre-mRNA binding [GO:0036002]; transcription corepressor activity [GO:0003714]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]+FUNCTION: Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment. {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21157427}.Q92973TNPO1 Transportin-1gene expression [GO:0010467]; organelle organization [GO:0006996]; protein import into nucleus, translocation [GO:0000060]; viral process [GO:0016032]Tnuclear localization sequence binding [GO:0008139]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; primary cilium [GO:0072372]FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner. {ECO:0000250, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:8986607, ECO:0000269|PubMed:9687515}.P26358DNMT1$DNA (cytosine-5)-methyltransferase 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145218}.cellular response to amino acid stimulus [GO:0071230]; chromatin modification [GO:0016568]; DNA methylation [GO:0006306]; DNA methylation on cytosine [GO:0032776]; gene expression [GO:0010467]; gene silencing [GO:0016458]; maintenance of DNA methylation [GO:0010216]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of histone H3-K9 methylation [GO:0051573]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of gene expression [GO:0010628]; positive regulation of histone H3-K4 methylation [GO:0051571]; regulation of cell proliferation [GO:0042127]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]; DNA-methyltransferase activity [GO:0009008]; methyl-CpG binding [GO:0008327]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]wnucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; replication fork [GO:0005657]?FUNCTION: Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. {ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18754681}.Q96KP1EXOC2Exocyst complex component 2&cellular protein metabolic process [GO:0044267]; exocyst assembly [GO:0001927]; Golgi to plasma membrane transport [GO:0006893]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]; regulation of entry of bacterium into host cell [GO:2000535]Dprotein kinase binding [GO:0019901]; Ral GTPase binding [GO:0017160]cytosol [GO:0005829]; exocyst [GO:0000145]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q9H4G4GAPR15Golgi-associated plant pathogenesis-related protein 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11865038}; Lipid-anchor {ECO:0000269|PubMed:11865038}. Note=Binds lipid-enriched microdomains of Golgi membranes not only by ionic interactions but also through the myristate.positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]Q14103HNRPD*Heterogeneous nuclear ribonucleoprotein D0SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasm< ic localization oscillates diurnally.circadian regulation of translation [GO:0097167]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; mRNA stabilization [GO:0048255]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of translation [GO:0045727]; regulation of circadian rhythm [GO:0042752]; regulation of transcription, DNA-templated [GO:0006355]; RNA catabolic process [GO:0006401]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; telomeric DNA binding [GO:0042162]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529] FUNCTION: Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation. {ECO:0000269|PubMed:10080887, ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:24423872}.P56211ARP19 cAMP-regulated phosphoprotein 19cell division [GO:0051301]; dopamine receptor signaling pathway [GO:0007212]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of catalytic activity [GO:0043086]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of glucose import [GO:0046326]; positive regulation of Ras protein signal transduction [GO:0046579]; regulation of protein phosphatase type 2A activity [GO:0034047]phosphatase inhibitor activity [GO:0019212]; potassium channel regulator activity [GO:0015459]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase inhibitor activity [GO:0004864]; protein phosphatase type 2A regulator activity [GO:0008601]; receptor binding [GO:0005102]FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression. {ECO:0000269|PubMed:21164014}.Q9H0R3TM222Transmembrane protein 222O43739CYH3 Cytohesin-3SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.*establishment of epithelial cell polarity [GO:0090162]; Golgi vesicle transport [GO:0048193]; positive regulation of cell adhesion [GO:0045785]; positive regulation of GTPase activity [GO:0043547]; regulation of ARF protein signal transduction [GO:0032012]; regulation of cell adhesion [GO:0030155]zARF guanyl-nucleotide exchange factor activity [GO:0005086]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. {ECO:0000269|PubMed:23940353, ECO:0000269|PubMed:9707577}.Q68CZ1FTMProtein fantomSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21685204}. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell junction, tight junction. Note=In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions.camera-type eye development [GO:0043010]; cerebellum development [GO:0021549]; cilium assembly [GO:0042384]; cochlea development [GO:0090102]; corpus callosum development [GO:0022038]; determination of left/right symmetry [GO:0007368]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; establishment of planar polarity [GO:0001736]; establishment or maintenance of cell polarity [GO:0007163]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; lateral ventricle development [GO:0021670]; liver development [GO:0001889]; negative regulation of G-protein coupled receptor protein signaling pathway [GO:0045744]; neural tube patterning [GO:0021532]; nose development [GO:0043584]; olfactory bulb development [GO:0021772]; organelle organization [GO:0006996]; pericardium development [GO:0060039]; regulation of smoothened signaling pathway [GO:0008589],thromboxane A2 receptor binding [GO:0031870]axoneme [GO:0005930]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]FUNCTION: Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP1 and NPHP4 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). {ECO:0000250}.P32856STX2 Syntaxin-2ESUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.Kacrosome reaction [GO:0007340]; cornified envelope assembly [GO:1903575]; digestive tract morphogenesis [GO:0048546]; ectoderm development [GO:0007398]; epithelial cell differentiation [GO:0030855]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; microvillus assembly [GO:0030033]; organ morphogenesis [GO:0009887]; protein oligomerization [GO:0051259]; regulation of blood coagulation [GO:0030193]; response to hydroperoxide [GO:0033194]; signal transduction [GO:0007165]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; vesicle docking [GO:0048278]calcium-dependent protein binding [GO:0048306]; protein dimerization activity [GO:0046983]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; midbody [GO:0030496]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; transport vesicle [GO:0030133]zFUNCTION: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.Q58WW2DCAF6"DDB1- and CUL4-associated factor 6<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15784617}.vpositive regulation of transcription from RNA polymerase II promoter [GO:004< 5944]; protein ubiquitination [GO:0016567]Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]5FUNCTION: Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:15784617, ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.Q13283G3BP1/Ras GTPase-activating protein-binding protein 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cytoplasmic granule. Cell membrane. Nucleus. Note=Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells (By similarity). Cytosolic and partially nuclear in resting cells. Recruited to stress granules (SGs) upon either arsenite or high temperature treatment. Recruitment to SGs is influenced by HRAS. {ECO:0000250}.DNA duplex unwinding [GO:0032508]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; Ras protein signal transduction [GO:0007265]; transport [GO:0006810]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; ATP-dependent RNA helicase activity [GO:0004004]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:9889278}.Q13232NDK3Nucleoside diphosphate kinase 3dapoptotic process [GO:0006915]; CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; nucleoside triphosphate biosynthetic process [GO:0009142]; purine nucleotide metabolic process [GO:0006163]; pyrimidine nucleotide metabolic process [GO:0006220]; regulation of apoptotic process [GO:0042981]; UTP biosynthetic process [GO:0006228]pcytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; mitochondrion [GO:0005739]SFUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis.Q15397K0020*Pumilio domain-containing protein KIAA0020ZSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|Ref.6}.&regulation of translation [GO:0006417]:endoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]Q5SRE7PHYD15Phytanoyl-CoA dioxygenase domain-containing protein 1Adioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]FUNCTION: Isoform 1 has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA. Isoform 2 and isoform 3 probably lack enzyme activity. {ECO:0000269|PubMed:21530488}.P46087NOP29Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferaseTpositive regulation of cell proliferation [GO:0008284]; rRNA processing [GO:0006364]hpoly(A) RNA binding [GO:0044822]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]-FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA (Probable). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation. {ECO:0000305}.Q7L5Y1ENOF1*Mitochondrial enolase superfamily member 1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16162288}.hcellular amino acid catabolic process [GO:0009063]; cellular carbohydrate catabolic process [GO:0044275]qisomerase activity [GO:0016853]; L-fuconate dehydratase activity [GO:0050023]; magnesium ion binding [GO:0000287]uFUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion (PubMed:24697329). {ECO:0000269|PubMed:24697329}.O43293DAPK3!Death-associated protein kinase 3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15910542, ECO:0000269|PubMed:20854903}. Cytoplasm {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903}. Note=Predominantly localizes to the cytoplasm but can shuttle between the nucleus and cytoplasm; cytoplasmic localization is promoted by phosphorylation at Thr-299 and involves Rho/Rock signaling. {ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:17126281}. Cytoplasm {ECO:0000269|PubMed:17126281}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:17126281}. Cytoplasm {ECO:0000269|PubMed:17126281}.apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to interferon-gamma [GO:0071346]; chromatin modification [GO:0016568]; cytokinesis [GO:0000910]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; neuron differentiation [GO:0030182]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of apoptotic process [GO:0042981]; regulation of autophagy [GO:0010506]; regulation of cell motility [GO:2000145]; regulation of cell shape [GO:0008360]; regulation of focal adhesion assembly [GO:0051893]; regulation of mitotic cell cycle [GO:0007346]; regulation of mitotic nuclear division [GO:0007088]; regulation of myosin II filament organization [GO:0043519]; regulation of smooth muscle contraction [GO:0006940]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]kATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; cAMP response element binding protein binding [GO:0008140]; identical protein binding [GO:0042802]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]; Rho GTPase binding [GO:0017048]|actin filament [GO:0005884]; cytoplasm [GO:0005737]; membrane raft [GO:0045121]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphor< ylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor. {ECO:0000269|PubMed:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18995835, ECO:0000269|PubMed:21169990, ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:21487036, ECO:0000269|PubMed:23454120}.P05106ITB3Integrin beta-3{SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-pass type I membrane protein {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:20702409}. Cell junction, focal adhesion {ECO:0000269|PubMed:20702409}.@activation of protein kinase activity [GO:0032147]; angiogenesis involved in wound healing [GO:0060055]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell growth [GO:0016049]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cell-substrate adhesion [GO:0031589]; cell-substrate junction assembly [GO:0007044]; extracellular matrix organization [GO:0030198]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; mesodermal cell differentiation [GO:0048333]; negative chemotaxis [GO:0050919]; negative regulation of lipid storage [GO:0010888]; negative regulation of lipid transport [GO:0032369]; negative regulation of lipoprotein metabolic process [GO:0050748]; negative regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045715]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; protein folding [GO:0006457]; regulation of bone resorption [GO:0045124]; smooth muscle cell migration [GO:0014909]; substrate adhesion-dependent cell spreading [GO:0034446]; tube development [GO:0035295]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral entry into host cell [GO:0046718]; wound healing [GO:0042060]cell adhesion molecule binding [GO:0050839]; extracellular matrix binding [GO:0050840]; fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; platelet-derived growth factor receptor binding [GO:0005161]; protease binding [GO:0002020]; protein disulfide isomerase activity [GO:0003756]; receptor activity [GO:0004872]; vascular endothelial growth factor receptor 2 binding [GO:0043184]3alphav-beta3 integrin-vitronectin complex [GO:0071062]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; integrin alphav-beta3 complex [GO:0034683]; integrin complex [GO:0008305]; lamellipodium membrane [GO:0031258]; melanosome [GO:0042470]; microvillus membrane [GO:0031528]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets (By similarity). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000250|UniProtKB:O54890, ECO:0000269|PubMed:10397733, ECO:0000269|PubMed:18045938, ECO:0000269|PubMed:9195946, ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.O60256KPRB:Phosphoribosyl pyrophosphate synthase-associated protein 2bone development [GO:0060348]; negative regulation of catalytic activity [GO:0043086]; nucleobase-containing compound metabolic process [GO:0006139]; nucleotide biosynthetic process [GO:0009165]Q9NTZ6RBM12RNA-binding protein 12Q9NR56MBNL1Muscleblind-like protein 1>SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule. Note=Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress. Localized in the cytoplasm of multinucleated myotubes. Colocalizes with nuclear foci of retained expanded-repeat transcripts in myotubes from patients affected by myotonic dystrophy.embryonic limb morphogenesis [GO:0030326]; in utero embryonic development [GO:0001701]; mRNA splice site selection [GO:0006376]; myoblast differentiation [GO:0045445]; nervous system development [GO:0007399]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]; skeletal muscle tissue development [GO:0007519]double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U< residues. {ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:15257297, ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:19470458}.Q9NQZ5STAR74StAR-related lipid transfer protein 7, mitochondrialQ16555DPYL2%Dihydropyrimidinase-related protein 2SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20801876}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20801876}. Membrane {ECO:0000269|PubMed:20801876}. Note=Tightly but non-covalently associated with membranes.)axon guidance [GO:0007411]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; nervous system development [GO:0007399]; nucleobase-containing compound metabolic process [GO:0006139]; olfactory bulb development [GO:0021772]; positive regulation of glutamate secretion [GO:0014049]; regulation of axon extension [GO:0030516]; response to amphetamine [GO:0001975]; response to cocaine [GO:0042220]; response to drug [GO:0042493]; signal transduction [GO:0007165]; spinal cord development [GO:0021510]; synaptic vesicle transport [GO:0048489])dihydropyrimidinase activity [GO:0004157]0cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; membrane [GO:0016020]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; protein complex [GO:0043234]; terminal bouton [GO:0043195]mFUNCTION: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis. {ECO:0000269|PubMed:11477421, ECO:0000269|PubMed:15466863, ECO:0000269|PubMed:20801876}.Q96JY6PDLI2PDZ and LIM domain protein 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659642}. Nucleus {ECO:0000269|PubMed:15659642}. Note=May be partially nuclear.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton. Note=Colocalizes with beta-1 integrin (ITGB1) and alpha-actinin but not with paxillin (PXN).; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: Isoform 3: Nucleus.actin cytoskeleton [GO:0015629]; cortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; stress fiber [GO:0001725]\FUNCTION: Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity. {ECO:0000269|PubMed:15659642}.O60879DIAP2Protein diaphanous homolog 2SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol. Early endosome. Note=Isoform 3 is cytosolic but when coexpressed with RHOD, the 2 proteins colocalize to early endosomes.actin filament polymerization [GO:0030041]; cytokinesis [GO:0000910]; female gamete generation [GO:0007292]; multicellular organismal development [GO:0007275]; oogenesis [GO:0048477]; small GTPase mediated signal transduction [GO:0007264]cytosol [GO:0005829]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]HFUNCTION: Could be involved in oogenesis. Involved in the regulation of endosome dynamics. Implicated in a novel signal transduction pathway, in which isoform 3 and CSK are sequentially activated by RHOD to regulate the motility of early endosomes through interactions with the actin cytoskeleton. {ECO:0000269|PubMed:12577064}.P50990TCPQ!T-complex protein 1 subunit thetaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20080638}.de novo' posttranslational protein folding [GO:0051084]; binding of sperm to zona pellucida [GO:0007339]; cellular protein metabolic process [GO:0044267]; pore complex assembly [GO:0046931]; protein folding [GO:0006457]; toxin transport [GO:1901998]?ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]@aggresome [GO:0016235]; cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; microtubule [GO:0005874]; zona pellucida receptor complex [GO:0002199]Q9BRK3MXRA8&Matrix-remodeling-associated protein 87establishment of glial blood-brain barrier [GO:0060857]jcell surface [GO:0009986]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]bFUNCTION: May play a role in the maturation and maintenance of blood-brain barrier. {ECO:0000250}.P08240SRPR2Signal recognition particle receptor subunit alphaSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain.acellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; IRE1-mediated unfolded protein response [GO:0036498]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; signal recognition particle binding [GO:0005047]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; signal recognition particle receptor complex [GO:0005785]FUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system.O14668TMG12Transmembrane gamma-carboxyglutamic acid protein 1O75909CCNKCyclin-K<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22012619}.cell division [GO:0051301]; cellular response to DNA damage stimulus [GO:0006974]; in utero embryonic development [GO:0001701]; mitotic nuclear division [GO:0007067]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation of cell cycle arrest [GO:0071157]; positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues [GO:2001165]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of transcription, DNA-templated [GO:0006355]; transcription from RNA polymerase II promoter [GO:0006366]cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]^cyclin K-CDK12 complex [GO:0002944]; cyclin K-CDK13 complex [GO:0002945]; nucleus [GO:0005634]iFUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:9632813}.Q8TEX9IPO4 Importin-4DNA replication-dependent nucleosome assembly [GO:0006335]; DNA replication-independent nucleosome assembly [GO:0006336]; intracellular protein transport [GO:0006886]; protein transport [GO:0015031]kcytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; protein complex [GO:0043234]FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear p< ore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of RPS3A. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. {ECO:0000250, ECO:0000269|PubMed:11823430}.P84022SMAD3)Mothers against decapentaplegic homolog 3SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1. Co-localizes with LEMD3 at the nucleus inner membrane. MAPK-mediated phosphorylation appears to have no effect on nuclear import. PDPK1 prevents its nuclear translocation in response to TGF-beta.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activin receptor signaling pathway [GO:0032924]; cell-cell junction organization [GO:0045216]; cell cycle arrest [GO:0007050]; developmental growth [GO:0048589]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic foregut morphogenesis [GO:0048617]; embryonic pattern specification [GO:0009880]; endoderm development [GO:0007492]; evasion or tolerance of host defenses by virus [GO:0019049]; extrinsic apoptotic signaling pathway [GO:0097191]; gene expression [GO:0010467]; heart looping [GO:0001947]; immune response [GO:0006955]; immune system development [GO:0002520]; intracellular signal transduction [GO:0035556]; in utero embryonic development [GO:0001701]; lens fiber cell differentiation [GO:0070306]; liver development [GO:0001889]; mesoderm formation [GO:0001707]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of inflammatory response [GO:0050728]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of wound healing [GO:0061045]; nodal signaling pathway [GO:0038092]; osteoblast development [GO:0002076]; paraxial mesoderm morphogenesis [GO:0048340]; pericardium development [GO:0060039]; positive regulation of alkaline phosphatase activity [GO:0010694]; positive regulation of bone mineralization [GO:0030501]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of catenin import into nucleus [GO:0035413]; positive regulation of cell migration [GO:0030335]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta3 production [GO:0032916]; primary miRNA processing [GO:0031053]; protein stabilization [GO:0050821]; regulation of binding [GO:0051098]; regulation of epithelial cell proliferation [GO:0050678]; regulation of immune response [GO:0050776]; regulation of striated muscle tissue development [GO:0016202]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of transforming growth factor beta2 production [GO:0032909]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to hypoxia [GO:0001666]; signal transduction involved in regulation of gene expression [GO:0023019]; SMAD protein complex assembly [GO:0007183]; SMAD protein signal transduction [GO:0060395]; somitogenesis [GO:0001756]; T cell activation [GO:0042110]; thyroid gland development [GO:0030878]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transdifferentiation [GO:0060290]; transforming growth factor beta receptor signaling pathway [GO:0007179]; transport [GO:0006810]; ureteric bud development [GO:0001657]; wound healing [GO:0042060]beta-catenin binding [GO:0008013]; bHLH transcription factor binding [GO:0043425]; chromatin DNA binding [GO:0031490]; core promoter proximal region sequence-specific DNA binding [GO:0000987]; co-SMAD binding [GO:0070410]; double-stranded DNA binding [GO:0003690]; enhancer binding [GO:0035326]; identical protein binding [GO:0042802]; phosphatase binding [GO:0019902]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity [GO:0000983]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]; transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity [GO:0030618]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]Vcytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear chromatin [GO:0000790]; nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; SMAD2-SMAD3 protein complex [GO:0071144]; SMAD protein complex [GO:0071141]; transcription factor complex [GO:0005667]FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000269|PubMed:10995748, ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:15588252, ECO:0000269|PubMed:16156666, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:16862174, ECO:0000269|PubMed:17327236, ECO:0000269|PubMed:19218245, ECO:0000269|PubMed:19289081, ECO:0000269|Pub< Med:9732876, ECO:0000269|PubMed:9892009}.Q8N138ORML3ORM1-like protein 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12093374, ECO:0000269|PubMed:19819884}; Multi-pass membrane protein {ECO:0000269|PubMed:12093374, ECO:0000269|PubMed:19819884}.Wcellular sphingolipid homeostasis [GO:0090156]; ceramide metabolic process [GO:0006672]kendoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; SPOTS complex [GO:0035339]FUNCTION: Negative regulator of sphingolipid synthesis. May indirectly regulate endoplasmic reticulum-mediated Ca(+2) signaling. {ECO:0000269|PubMed:20182505}.O43379WDR62WD repeat-containing protein 62SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle pole. Note=Shows cell cycle-dependent localization. Accumulates to the spindle pole during mitosis.ncerebral cortex development [GO:0021987]; mitotic spindle organization [GO:0007052]; neurogenesis [GO:0022008]acytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Required for cerebral cortical development. Plays a role in neuronal proliferation and migration. {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278}.Q13425SNTB2Beta-2-syntrophinaSUBCELLULAR LOCATION: Membrane. Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton. Note=Membrane-associated. In muscle, it is exclusively localized at the neuromuscular junction (By similarity). In insulinoma cell line, it is enriched in secretory granules. {ECO:0000250}.cytoplasm [GO:0005737]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; microtubule [GO:0005874]; protein complex [GO:0043234]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658]4FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.Q9Y4P8WIPI27WD repeat domain phosphoinositide-interacting protein 2SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:20505359, ECO:0000269|PubMed:21564513, ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:23916833}; Peripheral membrane protein {ECO:0000269|PubMed:20505359, ECO:0000269|PubMed:21564513, ECO:0000269|PubMed:22456507}; Cytoplasmic side {ECO:0000269|PubMed:20505359, ECO:0000269|PubMed:21564513, ECO:0000269|PubMed:22456507}. Note=Localizes to omegasomes membranes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Enriched at preautophagosomal structure membranes in response to PtdIns3P. {ECO:0000269|PubMed:24954904}.cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; nucleoplasm [GO:0005654]; pre-autophagosomal structure [GO:0000407]; pre-autophagosomal structure membrane [GO:0034045]; protein complex [GO:0043234]FUNCTION: Early component of the autophagy machinery being involved in formation of preautophagosomal structures and their maturation into mature phagosomes in response to phosphatidylinositol 3-phosphate (PtdIns3P). May bind PtdIns3P. {ECO:0000269|PubMed:20505359}.; FUNCTION: Isoform 4: Recruits the ATG12-ATG5-ATG16L1 complex to omegasomes and preautophagosomal structures, resulting in ATG8 family proteins lipidation and starvation-induced autophagy. Isoform 4 is also required for autophagic clearance of pathogenic bacteria. Isoform 4 binds the membrane surrounding Salmonella and recruits the ATG12-5-16L1 complex, initiating LC3 conjugation, autophagosomal membrane formation, and engulfment of Salmonella. {ECO:0000269|PubMed:24954904}.O43325LYRM1LYR motif-containing protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19022914}.Wintercellular bridge [GO:0045171]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]uFUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. {ECO:0000269|PubMed:19022914}.O75828CBR3Carbonyl reductase [NADPH] 3>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18493841}.Dcognition [GO:0050890]; phylloquinone catabolic process [GO:0042376]{3-keto sterol reductase activity [GO:0000253]; carbonyl reductase (NADPH) activity [GO:0004090]; NADPH binding [GO:0070402]hcytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]FUNCTION: Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro). {ECO:0000269|PubMed:18493841}.O43148MCES%mRNA cap guanine-N7 methyltransferaseYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:15767670}.7-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; RNA (guanine-N7)-methylation [GO:0036265]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]TmRNA (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA binding [GO:0003723]mRNA cap binding complex [GO:0005845]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; receptor complex [GO:0043235]FUNCTION: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC. {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902}.P49903SPS1Selenide, water dikinase 1SUBCELLULAR LOCATION: Isoform 1: Cell membrane. Nucleus membrane.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.ATP binding [GO:0005524]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; selenide, water dikinase activity [GO:0004756]Scytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]ZFUNCTION: Synthesizes selenophosphate from selenide and ATP. {ECO:0000269|PubMed:7665581}.O95777LSM8(U6 snRNA-associated Sm-like protein LSm8?poly(A) RNA binding [GO:0044822]; U6 snRNA binding [GO:0017070]Lspliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]sFUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome.P04181OAT)Ornithine aminotransferase, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:23076989}.cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; L-proline biosynthetic process [GO:0055129]; protein hexamerization [GO:0034214]; small molecule metabolic process [GO:0044281]; visual perception [GO:0007601]_ornithine-oxo-acid transaminase activity [GO:0004587]; pyridoxal phosphate binding [GO:0030170]Q9UBU6FA8A1Protein FAM8A1Q96QB1RHG07Rho GTPase-activating protein 7SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Membrane; Peripheral membrane protein. Note=Colocalizes with EF1A1 at actin-rich regions in the cell periphery.actin cytoskeleton organization [GO:0030036]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; focal adhesion assembly [GO:0048041]; forebrain development [GO:0030900]; heart morphogenesis [GO:0003007]; hindbrain morphogenesis [GO:0021575]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of stress fiber assembly [GO:0051497]; neural tube closure [GO:0001843]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of GTPase activit< y [GO:0043547]; positive regulation of protein dephosphorylation [GO:0035307]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]cGTPase activator activity [GO:0005096]; lipid binding [GO:0008289]; SH2 domain binding [GO:0042169]caveola [GO:0005901]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; ruffle membrane [GO:0032587]#FUNCTION: Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality. {ECO:0000269|PubMed:18786931, ECO:0000269|PubMed:19170769, ECO:0000269|PubMed:19710422}.P46937YAP1 Transcriptional coactivator YAP1YAPSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:22525271}. Nucleus {ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:22525271}. Note=Both phosphorylation and cell density can regulate its subcellular localization. Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus. At low density, predominantly nuclear and is translocated to the cytoplasm at high density (PubMed:18158288, PubMed:20048001). PTPN14 induces translocation from the nucleus to the cytoplasm (PubMed:22525271). {ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:22525271}.Kbud elongation involved in lung branching [GO:0060449]; cell morphogenesis [GO:0000902]; cell proliferation [GO:0008283]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to gamma radiation [GO:0071480]; cellular response to retinoic acid [GO:0071300]; contact inhibition [GO:0060242]; embryonic heart tube morphogenesis [GO:0003143]; gene expression [GO:0010467]; hippo signaling [GO:0035329]; keratinocyte differentiation [GO:0030216]; lateral mesoderm development [GO:0048368]; lung epithelial cell differentiation [GO:0060487]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of stem cell differentiation [GO:2000737]; notochord development [GO:0030903]; paraxial mesoderm development [GO:0048339]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell proliferation [GO:0008284]; positive regulation of organ growth [GO:0046622]; positive regulation of stem cell maintenance [GO:1902459]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of keratinocyte proliferation [GO:0010837]; regulation of metanephric nephron tubule epithelial cell differentiation [GO:0072307]; regulation of neurogenesis [GO:0050767]; regulation of stem cell proliferation [GO:0072091]; somatic stem cell maintenance [GO:0035019]; transcription initiation from RNA polymerase II promoter [GO:0006367]; vasculogenesis [GO:0001570]achromatin binding [GO:0003682]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II transcription factor binding transcription factor activity [GO:0001076]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; transcription regulatory region DNA binding [GO:0044212]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288). The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction (PubMed:18579750). {ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:21364637, ECO:0000269|PubMed:25778702}.; FUNCTION: Isoform 2: Isoform 2 and isoform 3 can activate the C-terminal fragment (CTF) of ERBB4 (isoform 3). {ECO:0000269|PubMed:12807903}.P49848TAF6/Transcription initiation factor TFIID subunit 61DNA-templated transcription, initiation [GO:0006352]; gene expression [GO:0010467]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell proliferation [GO:0008285]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of transcription, DNA-templated [GO:0006355]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]bDNA binding [GO:0003677]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytoplasm [GO:0005737]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276]FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.P46459NSFVesicle-fusing ATPase exocytosis [GO:0006887]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi vesicle docking [GO:0048211]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; plasma membrane fusion [GO:0045026]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of receptor recycling [GO:0001921]; potassium ion transport [GO:0006813]; regulation of exocytosis [GO:0017157]; synaptic transmission [GO:0007268]; vesicle-mediated transport [GO:0016192]+ATPase activity [GO:0016887]; ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; protein complex binding [GO:0032403]; protein kinase binding [GO:0019901]; Rab GTPase binding [GO:0017137]; syntaxin-1 binding [GO:0017075]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; extracellular exosome [GO:0070062]; Golgi stack [GO:0005795]; lysosomal membrane [GO:0005765]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]FUNCTION: Required for vesicle-mediated tr< ansport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling (By similarity). {ECO:0000250}.Q96SQ9CP2S1Cytochrome P450 2S1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11181079}; Peripheral membrane protein {ECO:0000269|PubMed:11181079}. Microsome membrane {ECO:0000269|PubMed:11181079}; Peripheral membrane protein {ECO:0000269|PubMed:11181079}.epoxygenase P450 pathway [GO:0019373]; exogenous drug catabolic process [GO:0042738]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; oxygen binding [GO:0019825]; steroid hydroxylase activity [GO:0008395]LFUNCTION: Has a potential importance for extrahepatic xenobiotic metabolism.Q9UJA5TRM6DtRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6tRNA methylation [GO:0030488]Gnucleus [GO:0005634]; tRNA (m1A) methyltransferase complex [GO:0031515]FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. {ECO:0000269|PubMed:16043508}.Q9H269VPS166Vacuolar protein sorting-associated protein 16 homologSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:17897319}; Peripheral membrane protein {ECO:0000269|PubMed:17897319}; Cytoplasmic side {ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Peripheral membrane protein {ECO:0000269|PubMed:17897319}; Cytoplasmic side {ECO:0000269|PubMed:17897319}. Early endosome {ECO:0000269|PubMed:18552835}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q920Q4}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24554770}. Note=Colocalizes with AP-3, clathrin, Rab5 and Rab7b (By similarity). Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes. {ECO:0000250|UniProtKB:Q920Q4, ECO:0000305}.5autophagosome fusion [GO:0000046]; endosomal transport [GO:0016197]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of SNARE complex assembly [GO:0035542]; regulation of vacuole fusion, non-autophagic [GO:0032889]; viral entry into host cell [GO:0046718]!actin filament [GO:0005884]; axon [GO:0030424]; early endosome [GO:0005769]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; recycling endosome [GO:0055037]FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:11382755, PubMed:23351085, PubMed:24554770, PubMed:25266290, PubMed:25783203). Required for recruitment of VPS33A to the HOPS complex (PubMed:23901104). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS33A but not VPS33B (PubMed:25783203). The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG (PubMed:24554770). {ECO:0000269|PubMed:23901104, ECO:0000269|PubMed:24554770, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:25266290, ECO:0000305|PubMed:25783203}.Q9NVR2INT10Integrator complex subunit 10<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16239144}.integrator complex [GO:0032039]Q6ZPD9D19L3&Probable C-mannosyltransferase DPY19L3Q8IWB7WDFY1.WD repeat and FYVE domain-containing protein 1CSUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:11739631}.J1-phosphatidylinositol binding [GO:0005545]; zinc ion binding [GO:0008270]Gcytosol [GO:0005829]; early endosome [GO:0005769]; nucleus [GO:0005634]O94766B3GA3CGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:21763480}; Single-pass type II membrane protein {ECO:0000269|PubMed:21763480}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:21763480}.[carbohydrate metabolic process [GO:0005975]; chondroitin sulfate metabolic process [GO:0030204]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; dermatan sulfate proteoglycan biosynthetic process [GO:0050651]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; positive regulation of catalytic activity [GO:0043085]; positive regulation of intracellular protein transport [GO:0090316]; protein glycosylation [GO:0006486]; small molecule metabolic process [GO:0044281]galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity [GO:0015018]; glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; protein phosphatase activator activity [GO:0072542]cis-Golgi network [GO:0005801]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation. {ECO:0000269|PubMed:24425863}.O43189PHF1PHD finger protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome.cellular response to DNA damage stimulus [GO:0006974]; chromatin modification [GO:0016568]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of histone H3-K27 methylation [GO:0061086]; positive regulation of histone H3-K27 methylation [GO:0061087]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]methylated histone binding [GO:0035064]; sequence-specific DNA binding transcription < factor activity [GO:0003700]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]XFUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18285464 and PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. {ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:18385154, ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23150668, ECO:0000269|PubMed:23273982}.O76094SRP72)Signal recognition particle subunit SRP72sSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22541560}. Endoplasmic reticulum {ECO:0000269|PubMed:22541560}.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]o7S RNA binding [GO:0008312]; poly(A) RNA binding [GO:0044822]; signal recognition particle binding [GO:0005047]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]YFUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.Q9NUQ9FA49BProtein FAM49B7cilium [GO:0005929]; extracellular exosome [GO:0070062]Q8N8S7ENAHProtein enabled homologSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell junction, focal adhesion. Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses (By similarity). {ECO:0000250}.actin polymerization or depolymerization [GO:0008154]; axon guidance [GO:0007411]; intracellular transport [GO:0046907]; neural tube closure [GO:0001843]; T cell receptor signaling pathway [GO:0050852]WW domain binding [GO:0050699]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; synapse [GO:0045202]FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity). {ECO:0000250}.P35659DEK Protein DEKSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17524367, ECO:0000269|PubMed:19695025}. Note=Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei.~chromatin modification [GO:0016568]; regulation of double-strand break repair [GO:2000779]; regulation of double-strand break repair via nonhomologous end joining [GO:2001032]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; transcription from RNA polymerase II promoter [GO:0006366]; viral genome replication [GO:0019079]XDNA binding [GO:0003677]; histone binding [GO:0042393]; poly(A) RNA binding [GO:0044822]4contractile fiber [GO:0043292]; nucleus [GO:0005634]LFUNCTION: Involved in chromatin organization. {ECO:0000269|PubMed:17524367}.Q13685AAMP'Angio-associated migratory cell protein/SUBCELLULAR LOCATION: Cell membrane. Cytoplasm.angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; positive regulation of endothelial cell migration [GO:0010595]; smooth muscle cell migration [GO:0014909]Ocell surface [GO:0009986]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]FUNCTION: Plays a role in angiogenesis and cell migration. In smooth muscle cell migration, may act through the RhoA pathway. {ECO:0000269|PubMed:10329261, ECO:0000269|PubMed:18634987}.Q13601KRR1/KRR1 small subunit processome component homologSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Translocates from cytoplasm to nucleus after exposure to HIV-1 virus or HIV-1 protein VPR or induction by hydrocortisone and dexamethasone in the absence of HIV-1 protein VPR.cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity). {ECO:0000250}.Q9H5K3SG196Protein O-mannose kinasewSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.brain development [GO:0007420]; carbohydrate phosphorylation [GO:0046835]; learning or memory [GO:0007611]; neuromuscular process [GO:0050905]; neuron migration [GO:0001764]; protein O-linked glycosylation [GO:0006493]; sensory perception of pain [GO:0019233]ATP binding [GO:0005524]; carbohydrate kinase activity [GO:0019200]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; protein kinase activity [GO:0004672]3FUNCTION: Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif. {ECO:0000269|PubMed:23519211, ECO:0000269|PubMed:23929950}.Q9Y496KIF3AKinesin-like protein KIF3AcSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250}.uantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cilium assembly [GO:0042384]; cilium morphogenesis [GO:0060271]; membrane organization [GO:0061024]; microtubule-based movement [GO:0007018]; organelle organization [GO:0006996]; plus-end-directed vesicle transport along microtubule [GO:0072383]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; spectrin binding [GO:0030507]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; kinesin II complex [GO:0016939]; microtubule [GO:0005874]; mic< rotubule cytoskeleton [GO:0015630]; primary cilium [GO:0072372]FUNCTION: Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation (By similarity). {ECO:0000250}.O95084PRS23Serine protease 23/serine-type endopeptidase activity [GO:0004252]O60936NOL3Nucleolar protein 3ASUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus {ECO:0000269|PubMed:10196175}. Note=The SR-rich C-terminus mediates nuclear localization. {ECO:0000269|PubMed:10196175}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:10196175}. Mitochondrion {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q62881}. Note=Phosphorylation at Thr-149 results in translocation to mithochondria. Colocalized with mitochondria in response to oxidative stress. {ECO:0000250|UniProtKB:Q62881}.#blood vessel remodeling [GO:0001974]; cardiac muscle cell apoptotic process [GO:0010659]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; intrinsic apoptotic signaling pathway [GO:0097193]; mRNA splice site selection [GO:0006376]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902109]; negative regulation of muscle atrophy [GO:0014736]; negative regulation of necrotic cell death [GO:0060547]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; protein oligomerization [GO:0051259]; regulation of NF-kappaB import into nucleus [GO:0042345]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to hypoxia [GO:0001666]; response to injury involved in regulation of muscle adaptation [GO:0014876]; response to ischemia [GO:0002931]; RNA splicing [GO:0008380]calcium ion binding [GO:0005509]; caspase binding [GO:0089720]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Isoform 1: May be involved in RNA splicing. {ECO:0000269|PubMed:10196175}.; FUNCTION: Isoform 2: Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors (PubMed:15004034). Inhibits calcium-mediated cell death by functionning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (PubMed:15509781). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (By similarity). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (By similarity). Inhibits too myoblast differentiation through caspase inhibition (By similarity). {ECO:0000250|UniProtKB:Q62881, ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:15004034, ECO:0000269|PubMed:15509781}.Q9H9C1SPE39,Spermatogenesis-defective protein 39 homologQSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000269|PubMed:19109425}. Recycling endosome {ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:22753090}. Late endosome {ECO:0000269|PubMed:19109425}. Note=Colocalizes in clusters with VPS33B at cytoplasmic organelles (PubMed:19109425).cell differentiation [GO:0030154]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of transcription, DNA-templated [GO:0006355]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; early endosome [GO:0005769]; late endosome [GO:0005770]; recycling endosome [GO:0055037]FUNCTION: Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be indepenedent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity). {ECO:0000250|UniProtKB:Q23288, ECO:0000269|PubMed:19109425, ECO:0000269|PubMed:20190753}.Q96EV2RBM33RNA-binding protein 33Q6IA69NADE%Glutamine-dependent NAD(+) synthetasexATP binding [GO:0005524]; glutaminase activity [GO:0004359]; NAD+ synthase (glutamine-hydrolyzing) activity [GO:0003952]Q14865ARI5B0AT-rich interactive domain-containing protein 5BESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.adipose tissue development [GO:0060612]; adrenal gland development [GO:0030325]; cell development [GO:0048468]; chromatin organization [GO:0006325]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; fat pad development [GO:0060613]; female gonad development [GO:0008585]; fibroblast migration [GO:0010761]; kidney development [GO:0001822]; liver development [GO:0001889]; male gonad development [GO:0008584]; multicellular organism growth [GO:0035264]; muscle organ morphogenesis [GO:0048644]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; palate development [GO:0060021]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; post-embryonic development [GO:0009791]; skeletal system morphogenesis [GO:0048705]; transcription, DNA-templated [GO:0006351]ODNA binding [GO:0003677]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; transcription regulatory region DNA binding [GO:0044212]]FUNCTION: Transcription coactivator that binds to the 5'-AATA[CT]-3' core sequence and plays a key role in adipogenesis and liver development. Acts by forming a complex with phosphorylated PHF2, which mediates demethylation at Lys-336, leading to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histon< e H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. Required for adipogenesis: regulates triglyceride metabolism in adipocytes by regulating expression of adipogenic genes. Overexpression leads to induction of smooth muscle marker genes, suggesting that it may also act as a regulator of smooth muscle cell differentiation and proliferation. Represses the cytomegalovirus enhancer. {ECO:0000269|PubMed:21532585}.Q96RU3FNBP1Formin-binding protein 1<SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes.cell cortex [GO:0005938]; coated pit [GO:0005905]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoskeleton [GO:0005856]; lysosome [GO:0005764]; plasma membrane [GO:0005886]>FUNCTION: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:15252009, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17512409}.Q86UY6NAA40N-alpha-acetyltransferase 40)N-acetyltransferase activity [GO:0008080]{FUNCTION: Responsible for the acetylation of the N-terminal residues of histones H4 and H2A. {ECO:0000269|PubMed:21935442}.P42166LAP2A.Lamina-associated polypeptide 2, isoform alpha[SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Expressed diffusely throughout the nucleus.4DNA binding [GO:0003677]; lamin binding [GO:0005521]pchromatin [GO:0000785]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634]2FUNCTION: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.Q9Y2W1TR150-Thyroid hormone receptor-associated protein 3YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:23525231}.androgen receptor signaling pathway [GO:0030521]; circadian rhythm [GO:0007623]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; nuclear-transcribed mRNA catabolic process [GO:0000956]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]; transcription initiation from RNA polymerase II promoter [GO:0006367]ATP binding [GO:0005524]; core promoter sequence-specific DNA binding [GO:0001046]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; phosphoprotein binding [GO:0051219]; poly(A) RNA binding [GO:0044822]; receptor activity [GO:0004872]; RNA polymerase II transcription cofactor activity [GO:0001104]; thyroid hormone receptor binding [GO:0046966]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; vitamin D receptor binding [GO:0042809]qextracellular exosome [GO:0070062]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]mFUNCTION: Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:22424773, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}.Q9BRV8SIKE1Suppressor of IKBKE 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16281057}.#innate immune response [GO:0045087]FUNCTION: Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation pathways. {ECO:0000269|PubMed:16281057}.Q9HCL0PCD18Protocadherin-18Q9UKN7MYO15Unconventional myosin-XVSUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to stereocilium tips in cochlear and vestibular hair cells. {ECO:0000250}.pinner ear morphogenesis [GO:0042472]; locomotory behavior [GO:0007626]; sensory perception of sound [GO:0007605]5ATP binding [GO:0005524]; motor activity [GO:0003774]rcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; myosin complex [GO:0016459]; stereocilium [GO:0032420]cFUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Required for the arrangement of stereocilia in mature hair bundles (By similarity). {ECO:0000250}.P11717MPRI/Cation-independent mannose-6-phosphate receptorM6P receptor(2)SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:10900005}; Single-pass type I membrane protein {ECO:0000269|PubMed:10900005}. Note=Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.insulin-like growth factor receptor signaling pathway [GO:0048009]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165]glycoprotein binding [GO:0001948]; identical protein binding [GO:0042802]; insulin-like growth factor-activated receptor activity [GO:0005010]; mannose binding [GO:0005537]; phosphoprotein binding [GO:0051219]; receptor activity [GO:0004872]; transporter activity [GO:0005215]cell surface [GO:0009986]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; e< xtracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; nuclear envelope lumen [GO:0005641]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140] FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4. {ECO:0000269|PubMed:10900005}.Q8N4Q0ZADH2>Zinc-binding alcohol dehydrogenase domain-containing protein 23mitochondrion [GO:0005739]; peroxisome [GO:0005777]P33992MCM5%DNA replication licensing factor MCM5DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA helicase activity [GO:0003678]; DNA replication origin binding [GO:0003688]_MCM complex [GO:0042555]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Interacts with MCMBP. {ECO:0000250}.Q01844EWSRNA-binding protein EWSSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16965792}. Cytoplasm {ECO:0000269|PubMed:16965792}. Cell membrane {ECO:0000269|PubMed:16965792}. Note=Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation.identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]|cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]qFUNCTION: Might normally function as a transcriptionnal repressor. EWS-fusion-proteins (EFPS) may play a role in the tumorigenic process. They may disturb gene expression by mimicking, or interfering with the normal function of CTD-POLII within the transcription initiation complex. They may also contribute to an aberrant activation of the fusion protein target genes.Q15878CAC1E9Voltage-dependent R-type calcium channel subunit alpha-1Exbehavioral fear response [GO:0001662]; behavioral response to pain [GO:0048266]; calcium ion import [GO:0070509]; calcium ion transport [GO:0006816]; energy reserve metabolic process [GO:0006112]; glucose homeostasis [GO:0042593]; ion transmembrane transport [GO:0034220]; locomotory behavior [GO:0007626]; membrane depolarization [GO:0051899]; membrane depolarization during action potential [GO:0086010]; regulation of heart rate [GO:0002027]; regulation of insulin secretion [GO:0050796]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of somatostatin secretion [GO:0090273]; sensory perception of pain [GO:0019233]; small molecule metabolic process [GO:0044281]; sperm motility [GO:0030317]; synaptic transmission [GO:0007268]; transmission of nerve impulse [GO:0019226]; transport [GO:0006810]; visual learning [GO:0008542]calcium ion binding [GO:0005509]; high voltage-gated calcium channel activity [GO:0008331]; voltage-gated calcium channel activity [GO:0005245]Pplasma membrane [GO:0005886]; voltage-gated calcium channel complex [GO:0005891],FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), omega-conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing.P78552I13R1'Interleukin-13 receptor subunit alpha-1Receptor(CytokineR)4cell surface receptor signaling pathway [GO:0007166]'cytokine receptor activity [GO:0004896]Jinterleukin-13 receptor complex [GO:0005898]; plasma membrane [GO:0005886]YFUNCTION: Binds with low affinity to interleukin-13 (IL13). Together with IL4RA can form a functional receptor for IL13. Also serves as an alternate accessory protein to the common cytokine receptor gamma chain for interleukin-4 (IL4) signaling, but cannot replace the function of IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.Q06587RING1!E3 ubiquitin-protein ligase RING1kSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Nucleus speckle {ECO:0000269|PubMed:21282530}.anterior/posterior pattern specification [GO:0009952]; camera-type eye morphogenesis [GO:0048593]; cellular protein metabolic process [GO:0044267]; histone H2A monoubiquitination [GO:0035518]; negative regulation of transcription, DNA-templated [GO:0045892]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; ligase activity [GO:0016874]; ubiquitin-protein transferase activator activity [GO:0097027]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]; sex chromatin [GO:0001739]vFUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity. {ECO:0000269|PubMed:16359901}.Q15012LAP4A-Lysosomal-associated transmembrane protein 4ASUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=May reside in an intracellular membrane-bound compartment. {ECO:0000305}.FUNCTION: May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. {ECO:0000250}.A5YKK6CNOT1(CCR4-NOT transcription complex subunit 1SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:21976065}. Nucleus {ECO:0000305|PubMed:21976065}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.#gene expression [GO:0010467]; gene silencing by miRNA [GO:0035195]; mul< ticellular organismal development [GO:0007275]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; regulation of stem cell maintenance [GO:2000036]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; transcription, DNA-templated [GO:0006351]armadillo repeat domain binding [GO:0070016]; estrogen receptor binding [GO:0030331]; poly(A) RNA binding [GO:0044822]; protein complex scaffold [GO:0032947]; protein domain specific binding [GO:0019904]; retinoic acid receptor binding [GO:0042974]CCR4-NOT complex [GO:0030014]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; peroxisomal membrane [GO:0005778]FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:16778766, ECO:0000269|PubMed:21278420, ECO:0000269|PubMed:21976065, ECO:0000269|PubMed:21984185, ECO:0000269|PubMed:22367759, ECO:0000269|PubMed:23644599}.Q96HH6TMM19Transmembrane protein 19P49368TCPG!T-complex protein 1 subunit gamma3cell body [GO:0044297]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; zona pellucida receptor complex [GO:0002199]Q9NW68BSDC1BSD domain-containing protein 1Q8ND94LRN4LLRRN4 C-terminal-like proteinQ99807COQ7,Ubiquinone biosynthesis protein COQ7 homologSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}.age-dependent response to oxidative stress [GO:0001306]; cellular response to oxidative stress [GO:0034599]; determination of adult lifespan [GO:0008340]; in utero embryonic development [GO:0001701]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; mitochondrion morphogenesis [GO:0070584]; neural tube formation [GO:0001841]; neurogenesis [GO:0022008]; small molecule metabolic process [GO:0044281]; ubiquinone biosynthetic process [GO:0006744]Cmetal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]DFUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner. {ECO:0000255|HAMAP-Rule:MF_03194}.Q9Y5J6T10B?Mitochondrial import inner membrane translocase subunit Tim10 BSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral membrane protein {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.cell-matrix adhesion [GO:0007160]; cellular protein metabolic process [GO:0044267]; protein targeting to mitochondrion [GO:0006626]mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. {ECO:0000269|PubMed:14726512}.Q9BT40INP5K&Inositol polyphosphate 5-phosphatase KSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12536145}. Note=Following stimulation with EGF, translocates to membrane ruffles.actin cytoskeleton organization [GO:0030036]; cellular response to cAMP [GO:0071320]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to hormone stimulus [GO:0032870]; cellular response to insulin stimulus [GO:0032869]; cellular response to tumor necrosis factor [GO:0071356]; dephosphorylation [GO:0016311]; glucose homeostasis [GO:0042593]; G-protein coupled receptor signaling pathway [GO:0007186]; inositol phosphate dephosphorylation [GO:0046855]; in utero embryonic development [GO:0001701]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of dephosphorylation [GO:0035305]; negative regulation of glucose transport [GO:0010829]; negative regulation of glycogen (starch) synthase activity [GO:2000466]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein targeting to membrane [GO:0090315]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869]; negative regulation of stress fiber assembly [GO:0051497]; negative regulation of transcription, DNA-templated [GO:0045892]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phospholipid metabolic process [GO:0006644]; positive regulation of renal water transport [GO:2001153]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of urine volume [GO:0035810]; protein targeting to plasma membrane [GO:0072661]; regulation of glycogen biosynthetic process [GO:0005979]; ruffle assembly [GO:0097178]; small molecule metabolic process [GO:0044281]dinositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; inositol trisphosphate phosphatase activity [GO:0046030]; lipid phosphatase activity [GO:0042577]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; phosphatidylinositol phosphat< e 5-phosphatase activity [GO:0034595]; phosphatidylinositol trisphosphate phosphatase activity [GO:0034594]; vasopressin receptor activity [GO:0005000]>cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; trans-Golgi network [GO:0005802]FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. May negatively regulate assembly of the actin cytoskeleton. {ECO:0000269|PubMed:10753883}.Q9NVE5UBP40(Ubiquitin carboxyl-terminal hydrolase 40Q7L8J43BP5L!SH3 domain-binding protein 5-likeintracellular signal transduction [GO:0035556]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of protein tyrosine kinase activity [GO:0061099]Oprotein kinase inhibitor activity [GO:0004860]; SH3 domain binding [GO:0017124]P07477TRY1 Trypsin-1Fcobalamin metabolic process [GO:0009235]; digestion [GO:0007586]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] FUNCTION: Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. {ECO:0000269|PubMed:7945238}.Q86W33TPRA1,Transmembrane protein adipocyte-associated 1saging [GO:0007568]; G-protein coupled receptor signaling pathway [GO:0007186]; lipid metabolic process [GO:0006629]Q6AWC2WWC2 Protein WWC2negative regulation of hippo signaling [GO:0035331]; negative regulation of organ growth [GO:0046621]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]Bkinase binding [GO:0019900]; protein complex scaffold [GO:0032947]Q6GMV3PTRD1'Putative peptidyl-tRNA hydrolase PTRHD1Q08209PP2BAGSerine/threonine-protein phosphatase 2B catalytic subunit alpha isoformSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle. {ECO:0000250}.calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion transport [GO:0006816]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to drug [GO:0035690]; cellular response to glucose stimulus [GO:0071333]; dephosphorylation [GO:0016311]; Fc-epsilon receptor signaling pathway [GO:0038095]; G1/S transition of mitotic cell cycle [GO:0000082]; innate immune response [GO:0045087]; multicellular organismal response to stress [GO:0033555]; negative regulation of chromatin binding [GO:0035562]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of insulin secretion [GO:0046676]; positive regulation of cardiac muscle hypertrophy in response to stress [GO:1903244]; positive regulation of NFAT protein import into nucleus [GO:0051533]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein dephosphorylation [GO:0006470]; protein import into nucleus [GO:0006606]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of synaptic transmission [GO:0050804]; response to amphetamine [GO:0001975]; response to calcium ion [GO:0051592]; skeletal muscle fiber development [GO:0048741]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell activation [GO:0042110]; transition between fast and slow fiber [GO:0014883]!calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; drug binding [GO:0008144]; enzyme binding [GO:0019899]; protein dimerization activity [GO:0046983]; protein serine/threonine phosphatase activity [GO:0004722]calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; sarcolemma [GO:0042383]; Z disc [GO:0030018]AFUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. {ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:18838687}.P46199IF2M1Translation initiation factor IF-2, mitochondrialmitochondrial translation [GO:0032543]; mitochondrial translational initiation [GO:0070124]; organelle organization [GO:0006996]; regulation of translational initiation [GO:0006446]; ribosome disassembly [GO:0032790]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; poly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.Q8WUJ3CEMIP6Cell migration-inducing and hyaluronan-binding proteinSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Cell membrane. Membrane, clathrin-coated pit. Secreted. Note=Retained in the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Colocalized with clathrin heavy chain/CLTC in clathrin-coated vesicles. Strongly detected in the cytoplasm of breast carcinoma cells, whereas poorly detected in adjacent normal epithelial cells, stromal cells, or benign breast tissues. Localized in the nucleus and cytoplasm of colon adenocarcinomas.hyaluronan catabolic process [GO:0030214]; positive regulation of cell migration [GO:0030335]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of protein kinase C activity [GO:1900020]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; sensory perception of sound [GO:0007605]clathrin heavy chain binding [GO:0032050]; ER retention sequence binding [GO:0046923]; hyaluronic acid binding [GO:0005540]; hyalurononglucosaminidase activity [GO:0004415]clathrin-coated vesicle membrane [GO:0030665]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886]0FUNCTION: Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing. {ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:24269685}.P83111LACTB7Serine beta-lactamase-like protein LACTB, mitocho< ndrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:19858488}.Q8NCW5NNRENAD(P)H-hydrate epimeraseSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:11991719}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}.rNADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; protein homotetramerization [GO:0051289]metal ion binding [GO:0046872]; NADHX epimerase activity [GO:0052856]; NADPHX epimerase activity [GO:0052857]; nucleotide binding [GO:0000166]cell body [GO:0044297]; cilium [GO:0005929]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]7FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. {ECO:0000255|HAMAP-Rule:MF_03159}.Q9BVC5ASHWNAshwin$embryonic morphogenesis [GO:0048598]Q9BWJ5SF3B5Splicing factor 3B subunit 5Znucleoplasm [GO:0005654]; nucleus [GO:0005634]; U12-type spliceosomal complex [GO:0005689]Q70IA6MOB2MOB kinase activator 2ySUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15067004}.actin cytoskeleton organization [GO:0030036]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein phosphorylation [GO:0001934]cytoplasm [GO:0005737]; neuron projection terminus [GO:0044306]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]tFUNCTION: Stimulates the autophosphorylation and kinase activity of STK38 and STK38L. {ECO:0000269|PubMed:15067004}.Q5SVS4KMCP1&Kidney mitochondrial carrier protein 1$mitochondrial transport [GO:0006839].FUNCTION: Probable transporter. {ECO:0000250}.Q9Y287ITM2BIntegral membrane protein 2BSUBCELLULAR LOCATION: Integral membrane protein 2B: Golgi apparatus membrane; Single-pass type II membrane protein. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted.; SUBCELLULAR LOCATION: BRI2, membrane form: Cell membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Note=Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing.; SUBCELLULAR LOCATION: Bri23 peptide: Secreted. Note=Detected in the cerebral spinal fluid (CSF).; SUBCELLULAR LOCATION: BRI2C, soluble form: Secreted.{negative regulation of amyloid precursor protein biosynthetic process [GO:0042985]; nervous system development [GO:0007399]xendosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle membrane [GO:0030660]; integral component of organelle membrane [GO:0031301]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Plays a regulatory role in the processing of the beta-amyloid A4 precursor protein (APP) and acts as an inhibitor of the beta-amyloid peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.; FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the beta-amyloid A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed beta-amyloid protein 40 and beta-amyloid protein 42.; FUNCTION: Bri23 peptide prevents aggregation of APP beta-amyloid protein 42 peptide into toxic oligomers.Q02318CP27A$Sterol 26-hydroxylase, mitochondrialPrimary bile acid biosynthesis Hormone biosynthesis-SUBCELLULAR LOCATION: Mitochondrion membrane.bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; cholesterol metabolic process [GO:0008203]; small molecule metabolic process [GO:0044281]; sterol metabolic process [GO:0016125]; xenobiotic metabolic process [GO:0006805]cholestanetriol 26-monooxygenase activity [GO:0047749]; cholesterol 26-hydroxylase activity [GO:0031073]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395]; vitamin D3 25-hydroxylase activity [GO:0030343]FUNCTION: Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3-25-hydroxylase activity.Q14997PSME4&Proteasome activator complex subunit 4SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000269|PubMed:12093752}. Nucleus speckle {ECO:0000250}. Note=Found in nuclear foci following treatment with ionizing radiation, but not with ultraviolet irradiation or H(2)O(2).anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to DNA damage stimulus [GO:0006974]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA repair [GO:0006281]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; multicellular organismal development [GO:0007275]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; spermatogenesis, exchange of chromosomal proteins [GO:0035093]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]Ylysine-acetylated histone binding [GO:0070577]; peptidase activator activity [GO:0016504]ocytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spermatoproteasome complex [GO:1990111]#FUNCTION: Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradatio< n of histones following DNA double-strand breaks. {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:18845680, ECO:0000269|PubMed:22550082, ECO:0000269|PubMed:23706739}.Q92934BAD%Bcl2-associated agonist of cell deathSUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm {ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the cytoplasm (By similarity). Upon phosphorylation, locates to the cytoplasm. {ECO:0000250|UniProtKB:Q61337}. activation of cysteine-type endopeptidase activity [GO:0097202]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; ADP metabolic process [GO:0046031]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; ATP metabolic process [GO:0046034]; cellular process regulating host cell cycle in response to virus [GO:0060154]; cellular response to chromate [GO:0071247]; cellular response to hypoxia [GO:0071456]; cellular response to lipid [GO:0071396]; cellular response to mechanical stimulus [GO:0071260]; cellular response to nicotine [GO:0071316]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glucose catabolic process [GO:0006007]; glucose homeostasis [GO:0042593]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; negative regulation of cytolysis [GO:0045918]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; pore complex assembly [GO:0046931]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic process by virus [GO:0060139]; positive regulation of autophagy [GO:0010508]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of glucokinase activity [GO:0033133]; positive regulation of insulin secretion [GO:0032024]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of neuron death [GO:1901216]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of proteolysis [GO:0045862]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of type B pancreatic cell development [GO:2000078]; programmed cell death [GO:0012501]; regulation of mitochondrial membrane permeability [GO:0046902]; release of cytochrome c from mitochondria [GO:0001836]; response to amino acid [GO:0043200]; response to calcium ion [GO:0051592]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to oleic acid [GO:0034201]; response to progesterone [GO:0032570]; response to testosterone [GO:0033574]; suppression by virus of host apoptotic process [GO:0019050]; type B pancreatic cell proliferation [GO:0044342]cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]; protein kinase binding [GO:0019901][cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]zFUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. {ECO:0000250}.O14556G3PT9Glyceraldehyde-3-phosphate dehydrogenase, testis-specific<canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; positive regulation of glycolytic process [GO:0045821]; small molecule metabolic process [GO:0044281]; spermatid development [GO:0007286]; sperm motility [GO:0030317]glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]qcytosol [GO:0005829]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]; sperm principal piece [GO:0097228]FUNCTION: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). {ECO:0000250}.Q00535CDK5Cyclin-dependent-like kinase 57SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cell membrane; Peripheral membrane protein. Perikaryon. Cell projection, lamellipodium {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Note=In axonal growth cone with extension to the peripheral lamellipodia (By similarity). Under neurotoxic stress and neuronal injury conditions, CDK5R (p35) is cleaved by calpain to generate CDK5R1 (p25) in response to increased intracellular calcium. The elevated level of p25, when in complex with CDK5, leads to its subcellular misallocation as well as its hyperactivation. Colocalizes with CTNND2 in the cell body of neuronal cells, and with CTNNB1 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. Reversibly attached to the plasma membrane in an inactive form when complexed to dephosphorylated p35 or CDK5R2 (p39), p35 phosphorylation releases this attachment and activates CDK5. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. axon extension [GO:0048675]; axon guidance [GO:0007411]; behavioral response to cocaine [GO:0048148]; blood coagulation [GO:0007596]; calcium ion import [GO:0070509]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell-matrix adhesion [GO:0007160]; cell proliferation [GO:0008283]; central nervous system neuron development [GO:0021954]; cerebellar cortex formation [GO:0021697]; corpus callosum development [GO:0022038]; cortical actin cytoskeleton organization [GO:0030866]; dendrite morphogenesis [GO:0048813]; hippocampus development [GO:0021766]; intracellular protein transport [GO:0006886]; layer formation in cerebral cortex [GO:0021819]; motor neuron axon guidance [GO:0008045]; negative regulation of axon extension [GO:0030517]; negative regulation of cell cycle [GO:0045786]; negative regulation of neuron death [GO:1901215]; negative regulation of protein export from nucleus [GO:0046826]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of proteolysis [GO:0045861]; negative regulation of synaptic plasticity [GO:0031914]; negative regulation of transcription, DNA-templated [GO:0045892]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; nucleocytoplasmic transport [GO:0006913]; oligodendrocyte differentiation [GO:0048709]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; phosphorylation [GO:0016310]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of neuron apoptotic process [GO:0043525]; posi< tive regulation of protein binding [GO:0032092]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein targeting to membrane [GO:0090314]; protein autophosphorylation [GO:0046777]; protein localization to synapse [GO:0035418]; receptor catabolic process [GO:0032801]; receptor clustering [GO:0043113]; regulated secretory pathway [GO:0045055]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle arrest [GO:0071156]; regulation of cell migration [GO:0030334]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of synaptic plasticity [GO:0048167]; regulation of synaptic vesicle recycling [GO:1903421]; rhythmic process [GO:0048511]; Schwann cell development [GO:0014044]; sensory perception of pain [GO:0019233]; serine phosphorylation of STAT3 protein [GO:0033136]; skeletal muscle tissue development [GO:0007519]; synapse assembly [GO:0007416]; synaptic transmission [GO:0007268]; synaptic transmission, dopaminergic [GO:0001963]; synaptic transmission, glutamatergic [GO:0035249]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle exocytosis [GO:0016079]; visual learning [GO:0008542]acetylcholine receptor activator activity [GO:0030549]; ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; ErbB-2 class receptor binding [GO:0005176]; ErbB-3 class receptor binding [GO:0043125]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]axon [GO:0030424]; cell junction [GO:0030054]; cyclin-dependent protein kinase 5 holoenzyme complex [GO:0016533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]&FUNCTION: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in post-mitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution. {ECO:0000269|PubMed:12393264, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15992363, ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:17121855, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17611284, ECO:0000269|PubMed:17671990, ECO:0000269|PubMed:18042622, ECO:0000269|PubMed:19081376, ECO:0000269|PubMed:19693690, ECO:0000269|PubMed:20061803, ECO:0000269|PubMed:20213743, ECO:0000269|PubMed:20826806, ECO:0000269|PubMed:21209322, ECO:0000269|PubMed:21220307, ECO:0000269|PubMed:21442427, ECO:0000269|PubMed:21465480, ECO:0000269|PubMed:21499257, ECO:0000269|PubMed:24235147, ECO:0000269|PubMed:9822744}.Q11201SIA4AHCMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; N-acetylneuraminate metabolic process [GO:0006054]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; protein O-linked glycosylation [GO:0006493]; protein phosphorylation [GO:0006468]; sialylation [GO:0097503]; small molecule metabolic process [GO:0044281]Hbeta-galactoside (CMP) alpha-2,3-sialyltransferase activity [GO:0003836]extracellular exosome [GO:0070062]; < Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of Golgi membrane [GO:0030173]; membrane [GO:0016020]&FUNCTION: It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values.Q96BW9TAM411Phosphatidate cytidylyltransferase, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.ccardiolipin biosynthetic process [GO:0032049]; CDP-diacylglycerol biosynthetic process [GO:0016024]8phosphatidate cytidylyltransferase activity [GO:0004605]@extrinsic component of mitochondrial inner membrane [GO:0031314]TFUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. Required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane (By similarity). {ECO:0000250}.Q9H098F107BProtein FAM107B(sensory perception of sound [GO:0007605]O43934MFS11UNC93-like protein MFSD11Q14669TRIPC"E3 ubiquitin-protein ligase TRIP12ISUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:20208519}.Ycellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; embryo development [GO:0009790]; negative regulation of double-strand break repair [GO:2000780]; negative regulation of histone H2A K63-linked ubiquitination [GO:1901315]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]ligase activity [GO:0016874]; thyroid hormone receptor binding [GO:0046966]; ubiquitin-protein transferase activity [GO:0004842]FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. {ECO:0000269|PubMed:18627766, ECO:0000269|PubMed:19028681, ECO:0000269|PubMed:20208519, ECO:0000269|PubMed:20829358, ECO:0000269|PubMed:22884692}.Q06203PUR1Amidophosphoribosyltransferase*de novo' IMP biosynthetic process [GO:0006189]; cellular response to drug [GO:0035690]; cellular response to insulin stimulus [GO:0032869]; G1/S transition of mitotic cell cycle [GO:0000082]; glutamine catabolic process [GO:0006543]; kidney development [GO:0001822]; lactation [GO:0007595]; maternal process involved in female pregnancy [GO:0060135]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside metabolic process [GO:0009116]; organ regeneration [GO:0031100]; protein homotetramerization [GO:0051289]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; small molecule metabolic process [GO:0044281]4 iron, 4 sulfur cluster binding [GO:0051539]; amidophosphoribosyltransferase activity [GO:0004044]; metal ion binding [GO:0046872]P48506GSH1,Glutamate--cysteine ligase catalytic subunitapoptotic mitochondrial changes [GO:0008637]; cell redox homeostasis [GO:0045454]; cellular nitrogen compound metabolic process [GO:0034641]; cysteine metabolic process [GO:0006534]; glutamate metabolic process [GO:0006536]; glutathione biosynthetic process [GO:0006750]; glutathione derivative biosynthetic process [GO:1901687]; L-ascorbic acid metabolic process [GO:0019852]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of blood vessel size [GO:0050880]; regulation of mitochondrial depolarization [GO:0051900]; response to arsenic-containing substance [GO:0046685]; response to heat [GO:0009408]; response to hormone [GO:0009725]; response to nitrosative stress [GO:0051409]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; xenobiotic metabolic process [GO:0006805]ADP binding [GO:0043531]; ATP binding [GO:0005524]; coenzyme binding [GO:0050662]; glutamate binding [GO:0016595]; glutamate-cysteine ligase activity [GO:0004357]; magnesium ion binding [GO:0000287]Q13228SBP1Selenium-binding protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=May associate with Golgi membrane. May associate with the membrane of autophagosomes (By similarity). {ECO:0000250}.cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleolus [GO:0005730]FUNCTION: Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity). {ECO:0000250}.Q5T2T1MPP7MAGUK p55 subfamily member 7}SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell junction, tight junction. Cell junction, adherens junction. bicellular tight junction assembly [GO:0070830]; establishment of cell polarity [GO:0030010]; positive regulation of protein complex assembly [GO:0031334]; positive regulation of signal transduction [GO:0009967]; protein localization to adherens junction [GO:0071896]protein complex scaffold [GO:0032947]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; signaling adaptor activity [GO:0035591]adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; mitochondrion [GO:0005739]; MPP7-DLG1-LIN7 complex [GO:0097025]FUNCTION: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact. {ECO:0000269|PubMed:17332497}.Q8IYI6EXOC8Exocyst complex component 8SUBCELLULAR LOCATION: Cytoplasm. Cell projection, growth cone {ECO:0000250}. Note=Redistributes to growing neurites and growth cones during cell differentiation (By similarity). Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups. {ECO:0000250}.-cellular protein metabolic process [GO:0044267]; endosome organization [GO:0007032]; exocyst assembly [GO:0001927]; exocyst localization [GO:0051601]; extracellular matrix disassembly [GO:0022617]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]cytoplasm [GO:0005737]; cytosol [GO:0005829]; exoc< yst [GO:0000145]; growth cone [GO:0030426]; late endosome [GO:0005770]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q9BV68RN126"E3 ubiquitin-protein ligase RNF126eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23026136}. Nucleus {ECO:0000269|PubMed:23026136}.cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process [GO:0071629]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of cell proliferation [GO:0042127]; retrograde transport, endosome to Golgi [GO:0042147]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through ubiquitination of various target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. Through their polyubiquitination, may play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4. May also be part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. May provide the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the mislocalized proteins and their targeting to the proteasome (PubMed:24981174). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (PubMed:24275455). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (PubMed:23026136). May monoubiquitinate AICDA (PubMed:23277564). {ECO:0000250|UniProtKB:Q91YL2, ECO:0000269|PubMed:23277564, ECO:0000269|PubMed:24275455, ECO:0000269|PubMed:24981174, ECO:0000303|PubMed:23026136}.Q9Y283INVSInversinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:12872123}. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to mitotic spindle. Frequently membrane-associated, membrane localization is dependent upon cell-cell contacts and is redistributed when cell adhesion is disrupted after incubation of the cell monolayer with low-calcium/EGTA medium.embryonic heart tube left/right pattern formation [GO:0060971]; kidney development [GO:0001822]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; pancreas development [GO:0031016]; post-embryonic development [GO:0009791]; Wnt signaling pathway [GO:0016055]ciliary base [GO:0097546]; ciliary inversin compartment [GO:0097543]; cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling. Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). {ECO:0000250}.Q9UPN6SCAF8 Protein SCAF8SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Note=Detected in granular nuclear foci which correspond to sites of active transcription. {ECO:0000250}.jnucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA polymerase core enzyme binding [GO:0043175]Xnuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]LFUNCTION: May play a role in mRNA processing. {ECO:0000269|PubMed:11101529}.Q9Y2Z4SYYM$Tyrosine--tRNA ligase, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:15779907}.gene expression [GO:0010467]; mitochondrial tyrosyl-tRNA aminoacylation [GO:0070184]; translation [GO:0006412]; tRNA aminoacylation [GO:0043039]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; tyrosine binding [GO:0072545]; tyrosine-tRNA ligase activity [GO:0004831]FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000269|PubMed:15779907}.Q9HCN4GPN1GPN-loop GTPase 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11058119, ECO:0000269|PubMed:20855544}. Nucleus {ECO:0000269|PubMed:20855544}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:20855544}.UFUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII) (PubMed:20855544, PubMed:21768307). May act at an RNAP assembly step prior to nuclear import (PubMed:21768307). Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation (PubMed:17643375). May be involved in nuclear localization of XPA (PubMed:11058119). {ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:20855544, ECO:0000269|PubMed:21768307, ECO:0000305|PubMed:11058119}.Q14642I5P11Type I inositol 1,4,5-trisphosphate 5-phosphatase-SUBCELLULAR LOCATION: Membrane; Lipid-anchor.inositol phosphate metabolic process [GO:0043647]; phosphatidylinositol dephosphorylation [GO:0046856]; small molecule metabolic process [GO:0044281]inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; PH domain binding [GO:0042731]Wextracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.O75387LAT35Large neutral amino acids transporter small subunit 3amino acid transport [GO:0006865]; ion transport [GO:0006811]; L-alpha-amino acid transmembrane transport [GO:1902475]; neutral amino acid transport [GO:0015804]; transmembrane transport [GO:0055085]L-amino acid transmembrane transporter activity [GO:0015179]; neutral amino acid transmembrane transporter activity [GO:0015175]FUNCTION: Sodium-independent, high affinity transport of large neutral amino acids. Has narrower substrate selectivity compared to SLC7A5 and SLC7A8 and mainly transports branched-chain amino acids and phenylalanine. Plays a role in the development of human prostate cancer, from prostatic intraepithelial neoplasia to invasive prostate cancer. {ECO:0000269|PubMed:11956097, ECO:0000269|PubMed:12930836, ECO:0000269|PubMed:9255310, ECO:0000269|PubMed:9722952}.Q12929EPS83Epidermal growth factor receptor kinase substrate 8SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, stereocilium {ECO:0000250, ECO:0000250|UniProtKB:Q08509}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells (By similarity). Localizes to the midzone of dividing cells. {ECO:0000250, ECO:0000250|UniProtKB:Q< 08509}.actin crosslink formation [GO:0051764]; actin cytoskeleton reorganization [GO:0031532]; actin filament bundle assembly [GO:0051017]; actin polymerization-dependent cell motility [GO:0070358]; adult locomotory behavior [GO:0008344]; barbed-end actin filament capping [GO:0051016]; behavioral response to ethanol [GO:0048149]; cell proliferation [GO:0008283]; dendritic cell migration [GO:0036336]; epidermal growth factor receptor signaling pathway [GO:0007173]; exit from mitosis [GO:0010458]; positive regulation of signal transduction [GO:0009967]; Rac protein signal transduction [GO:0016601]; regulation of actin filament length [GO:0030832]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165]bactin binding [GO:0003779]; Rac GTPase binding [GO:0048365]; SH3/SH2 adaptor activity [GO:0005070]Gbrush border [GO:0005903]; cell cortex [GO:0005938]; cell junction [GO:0030054]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; N-methyl-D-aspartate selective glutamate receptor complex [GO:0017146]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587]; stereocilium [GO:0032420]; vesicle [GO:0031982]FUNCTION: Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes. {ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:17115031}.O00186STXB3Syntaxin-binding protein 3SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10194441}. Cell membrane {ECO:0000269|PubMed:10194441}. Note=In platelets, predominantly cytosolic. Low amounts membrane-associated.blood coagulation [GO:0007596]; brain development [GO:0007420]; glucose transport [GO:0015758]; insulin secretion [GO:0030073]; membrane organization [GO:0061024]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; neutrophil degranulation [GO:0043312]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; protein heterooligomerization [GO:0051291]; protein to membrane docking [GO:0022615]; response to insulin [GO:0032868]; vesicle docking involved in exocytosis [GO:0006904]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; specific granule [GO:0042581]; tertiary granule [GO:0070820]FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. {ECO:0000250}.P33316DUT?Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrialZSUBCELLULAR LOCATION: Isoform 2: Nucleus.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion.DNA replication [GO:0006260]; dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; small molecule metabolic process [GO:0044281]ndUTP diphosphatase activity [GO:0004170]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000269|PubMed:8805593}.Q96AY3FKB10*Peptidyl-prolyl cis-trans isomerase FKBP10P11216PYGB"Glycogen phosphorylase, brain formcarbohydrate metabolic process [GO:0005975]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; small molecule metabolic process [GO:0044281]carbohydrate binding [GO:0030246]; drug binding [GO:0008144]; glycogen phosphorylase activity [GO:0008184]; pyridoxal phosphate binding [GO:0030170]daxon [GO:0030424]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]Q9NUE0ZDH18Palmitoyltransferase ZDHHC18peptidyl-L-cysteine S-palmitoylation [GO:0018230]; protein palmitoylation [GO:0018345]; protein targeting to membrane [GO:0006612]palmitoyltransferase activity [GO:0016409]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; zinc ion binding [GO:0008270]mendoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]PFUNCTION: Has palmitoyltransferase activity towards HRAS and LCK. {ECO:0000250}.P19174PLCG1A1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell projection, ruffle. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.bactivation of MAPKK activity [GO:0000186]; activation of phospholipase C activity [GO:0007202]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; inositol phosphate metabolic process [GO:0043647]; in utero embryonic development [GO:0001701]; leukocyte migration [GO:0050900]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phospholipid catabolic process [GO:0009395]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032] calcium ion binding [GO:0005509]; neurotrophin TRKA receptor binding [GO:0005168]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; protein kinase binding [GO:0019901];< receptor signaling protein activity [GO:0005057]cell-cell junction [GO:0005911]; cell projection [GO:0042995]; COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration. {ECO:0000269|PubMed:17229814}.Q15714T22D1TSC22 domain family protein 1negative regulation of apoptotic process [GO:0043066]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell proliferation [GO:0008284]; transcription from RNA polymerase II promoter [GO:0006366][FUNCTION: Transcriptional repressor. Acts on the C-type natriuretic peptide (CNP) promoter.Q9NYI0PSD3'PH and SEC7 domain-containing protein 3mSUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}.neuron differentiation [GO:0030182]; positive regulation of GTPase activity [GO:0043547]; regulation of ARF protein signal transduction [GO:0032012]acell junction [GO:0030054]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]EFUNCTION: Guanine nucleotide exchange factor for ARF6. {ECO:0000250}.Q15643TRIPB'Thyroid receptor-interacting protein 11SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10189370}; Peripheral membrane protein {ECO:0000269|PubMed:10189370}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10189370}. Note=Associates with the ends of centrosome-nucleated microtubules.organelle organization [GO:0006996]; protein targeting to Golgi [GO:0000042]; regulation of nucleic acid-templated transcription [GO:1903506]; transcription from RNA polymerase II promoter [GO:0006366]; ventricular septum development [GO:0003281]cis-Golgi network [GO:0005801]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; inner acrosomal membrane [GO:0002079]; nucleus [GO:0005634]; outer acrosomal membrane [GO:0002081]FUNCTION: Binds the ligand binding domain of the thyroid receptor (THRB) in the presence of triiodothyronine and enhances THRB-modulated transcription. Golgi auto-antigen; probably involved in maintaining cis-Golgi structure. {ECO:0000269|PubMed:10189370, ECO:0000269|PubMed:9256431}.Q9BT09CNPY3Protein canopy homolog 3Vinnate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses (By similarity). {ECO:0000250}.Q86Y56HEAT2 HEAT repeat-containing protein 24SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}. Cytoplasmic granule {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}. Note=Observed only in the cytoplasm of ciliated cells and absent from cilia. {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}.lcilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159]; outer dynein arm assembly [GO:0036158].dynein intermediate chain binding [GO:0045505]pFUNCTION: Cytoplasmic protein involved in the delivery of the dynein machinery to the motile cilium. It is required for the assembly of the axonemal dynein inner and outer arms, two structures attached to the peripheral outer doublet A microtubule of the axoneme, that play a crucial role in cilium motility. {ECO:0000269|PubMed:23040496, ECO:0000269|PubMed:25232951}.P53990IST1 IST1 homologSUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}. Note=Localizes to the midbody of dividing cells.abscission [GO:0009838]; activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cell division [GO:0051301]; cytokinesis [GO:0000910]; establishment of protein localization [GO:0045184]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of proteolysis [GO:0045862]; protein localization [GO:0008104]; viral capsid secondary envelopment [GO:0046745]; viral release from host cell [GO:0019076]sMIT domain binding [GO:0090541]; protein complex binding [GO:0032403]; protein domain specific binding [GO:0019904]centrosome [GO:0005813]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; Flemming body [GO:0090543]; midbody [GO:0030496]bFUNCTION: Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. {ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480}.Q8N4J0CI041UPF0586 protein C9orf41nSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26001783}. Nucleus {ECO:0000269|PubMed:26001783}.(carnosine metabolic process [GO:0035498]3carnosine N-methyltransferase activity [GO:0030735]FUNCTION: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His). {ECO:0000269|PubMed:26001783}.Q8NBN3TM87ATransmembrane protein 87AQ9H939PPIP2:Proline-serine-threonine phosphatase-interacting protein 2Ccell migration [GO:0016477]; cytoskeleton organization [GO:0007010]Fcytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]sFUNCTION: Binds to F-actin. May be involved in regulation of the actin cytoskeleton (By similarity). {ECO:0000250}.Q9HCN8SDF2L,Stromal cell-derived factor 2-like protein 1lER-associated misfolded protein catabolic process [GO:0071712]; regulation of apoptotic process [GO:0042981]uendoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; membrane [GO:0016020]O75352MPU1/Mannose-P-dolichol utilization defect 1 proteindolichol-linked oligosaccharide biosynthetic process [GO:0006488]; oligosaccharide biosynthetic process [GO:0009312]; protein folding [GO:0006457]; transport [GO:0006810]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors. {ECO:0000250}.P53671LIMK2LIM domain kinase 2SUBCELLULAR LOCATION: Isoform LIMK2a: Cytoplasm. Nucleus. Note=Isoform LIMK2a is distributed in the cytoplasm and the nucleus.; SUBCELLULAR LOCATION: Isoform LIMK2b: Cytoplasm. Nucleus. Note=Isoform LIMK2b occurs mainly in the cytoplasm and is scarcely translocated to the nucleus.:phosphorylation [GO:0016310]; spermatogenesis [GO:0007283]nATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]Lcis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; nucleus [GO:0005634]FUNCTION: Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. {ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:11018042}.O60234GMFGGlia maturation factor gamma6negative regulation of Arp< 2/3 complex-mediated actin nucleation [GO:0034316]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; positive regulation of catalytic activity [GO:0043085]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton reorganization [GO:2000249]Venzyme activator activity [GO:0008047]; protein kinase inhibitor activity [GO:0004860]Q6NXR4TTI2TELO2-interacting protein 2Icentrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. {ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650}.Q16531DDB1DNA damage-binding protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage.DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; histone H2A monoubiquitination [GO:0035518]; interaction with symbiont [GO:0051702]; negative regulation of apoptotic process [GO:0043066]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; positive regulation by virus of viral protein levels in host cell [GO:0046726]; positive regulation of viral genome replication [GO:0045070]; positive regulation of viral release from host cell [GO:1902188]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of mitotic cell cycle phase transition [GO:1901990]; translesion synthesis [GO:0019985]; UV-damage excision repair [GO:0070914]; viral process [GO:0016032]; Wnt signaling pathway [GO:0016055]*Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]2FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2. {ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355}.O75093SLIT1Slit homolog 1 proteinaxon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; dorsal/ventral axon guidance [GO:0033563]; establishment of nucleus localization [GO:0040023]; forebrain morphogenesis [GO:0048853]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of synapse assembly [GO:0051964]; retinal ganglion cell axon guidance [GO:0031290]; tangential migration from the subventricular zone to the olfactory bulb [GO:0022028]Acalcium ion binding [GO:0005509]; Roundabout binding [GO:0048495]3cell [GO:0005623]; extracellular space [GO:0005615]FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. {ECO:0000250}.Q9C0B1FTO-Alpha-ketoglutarate-dependent dioxygenase FTOkSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22002720}. Nucleus speckle {ECO:0000269|PubMed:22002720}.*adipose tissue development [GO:0060612]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA demethylation [GO:0080111]; oxidative demethylation [GO:0070989]; oxidative single-stranded DNA demethylation [GO:0035552]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of lipid storage [GO:0010883]; regulation of multicellular organism growth [GO:0040014]; regulation of respiratory system process [GO:0044065]; regulation of white fat cell proliferation [GO:0070350]; RNA repair [GO:0042245]; temperature homeostasis [GO:0001659]DNA-N1-methyladenine dioxygenase activity [GO:0043734]; ferrous iron binding [GO:0008198]; oxidative DNA demethylase activity [GO:0035516]; oxidative RNA demethylase activity [GO:0035515]vFUNCTION: Dioxygenase that repairs alkylated DNA and RNA by oxidative demethylation. Has highest activity towards single-stranded RNA containing 3-methyluracil, followed by single-stranded DNA containing 3-methylthymine. Has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Requires molecular oxygen, alpha-ketoglutarate and iron. Contributes to the regulation of the global metabolic rate, energy expenditure and energy homeostasis. Contributes to the regulation of body size and body fat accumulation. {ECO:0000269|PubMed:18775698, ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:22002720}.Q53EZ4CEP55Centrosomal protein of 55 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cleavage furrow. Midbody. Note=Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loss of affinity for the centrosome at the onset of prophase and diffusion throughout the cell. This dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in cert< ain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis.cell separation after cytokinesis [GO:0000920]; establishment of protein localization [GO:0045184]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0007067]centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; intercellular bridge [GO:0045171]; membrane [GO:0016020]; midbody [GO:0030496]FUNCTION: Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. {ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:17853893}.P30038AL4A1<Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialv4-hydroxyproline catabolic process [GO:0019470]; cellular nitrogen compound metabolic process [GO:0034641]; glutamate biosynthetic process [GO:0006537]; proline biosynthetic process [GO:0006561]; proline catabolic process [GO:0006562]; proline catabolic process to glutamate [GO:0010133]; proline metabolic process [GO:0006560]; small molecule metabolic process [GO:0044281]1-pyrroline-5-carboxylate dehydrogenase activity [GO:0003842]; aldehyde dehydrogenase (NAD) activity [GO:0004029]; electron carrier activity [GO:0009055]; identical protein binding [GO:0042802]FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. {ECO:0000269|PubMed:22516612}.P30622CLIP1*CAP-Gly domain-containing linker protein 1mSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle. Note=Associated with the cytoskeleton. Detected at the plus ends of microtubules in the cytosol, and close to plasma membrane ruffles. Associates with the membranes of intermediate macropinocytic vesicles.#microtubule bundle formation [GO:0001578]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; positive regulation of microtubule polymerization [GO:0031116]; protein transport into plasma membrane raft [GO:0044861]; small GTPase mediated signal transduction [GO:0007264]metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]; nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270]dcentrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endosome [GO:0005768]; intermediate filament [GO:0005882]; kinetochore [GO:0000776]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; ruffle [GO:0001726]FUNCTION: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:17889670}.Q9UPZ3HPS5#Hermansky-Pudlak syndrome 5 proteinGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15030569}.^blood coagulation [GO:0007596]; organelle organization [GO:0006996]; pigmentation [GO:0043473]BLOC-2 complex [GO:0031084]TFUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. Regulates intracellular vesicular trafficking in fibroblasts. May be involved in the regulation of general functions of integrins. {ECO:0000269|PubMed:15296495, ECO:0000269|PubMed:17301833}.Q8WW43APH1BGamma-secretase subunit APH-1Bapoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; membrane protein intracellular domain proteolysis [GO:0031293]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]iintegral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Probably present in a minority of gamma-secretase complexes compared to APH1A. {ECO:0000269|PubMed:12297508}.Q9NY35CLDN1#Claudin domain-containing protein 1kapical plasma membrane [GO:0016324]; cell surface [GO:0009986]; integral component of membrane [GO:0016021]Q63HK5TSH3Teashirt homolog 3SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000250}. Note=Colocalizes with APBB1 in axonal growth cone (By similarity). Colocalizes with APBB1 in the nucleus. {ECO:0000250}.multicellular organismal development [GO:0007275]; negative regulation of transcription, DNA-templated [GO:0045892]; regulation of respiratory gaseous exchange by neurological system process [GO:0002087]; transcription, DNA-templated [GO:0006351]Xchromatin binding [GO:0003682]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]Hgrowth cone [GO:0030426]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Transcriptional regulator involved in developmental processes. Function in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter. {ECO:0000269|PubMed:19343227}.Q96BP2CHCH1?Coiled-coil-helix-coiled-coil-helix domain-containing protein 1cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q9UHB9SRP68)Signal recognition particle subunit SRP684SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; protein targeting to ER [GO:0045047]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]7S RNA binding [GO:0008312]; endoplasmic reticulum signal peptide binding [GO:0030942]; poly(A) RNA binding [GO:0044822]; signal recognition particle binding [GO:0005047]; signal sequence binding [GO:0005048]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; nucleolus [GO:0005730]; ribosome [GO:0005840]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]oFUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This< ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.P00568KAD1Adenylate kinase isoenzyme 1ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; cell cycle arrest [GO:0007050]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside diphosphate phosphorylation [GO:0006165]; nucleoside triphosphate biosynthetic process [GO:0009142]; small molecule metabolic process [GO:0044281]uadenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; nucleoside diphosphate kinase activity [GO:0004550]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; outer dense fiber [GO:0001520]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]9FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111}.Q93009UBP7'Ubiquitin carboxyl-terminal hydrolase 7SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23973222}. Cytoplasm. Nucleus, PML body. Note=Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies.>histone deubiquitination [GO:0016578]; maintenance of DNA methylation [GO:0010216]; multicellular organismal development [GO:0007275]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; transcription-coupled nucleotide-excision repair [GO:0006283]; viral process [GO:0016032]cysteine-type endopeptidase activity [GO:0004197]; p53 binding [GO:0002039]; protein C-terminus binding [GO:0008022]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]tcytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634]; PML body [GO:0016605]cFUNCTION: Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). {ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18590780, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:20153724, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22689415, ECO:0000269|PubMed:23973222}.O94817ATG12Ubiquitin-like protein ATG12SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000269|PubMed:22342342}; Peripheral membrane protein {ECO:0000269|PubMed:22342342}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane./autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; C-terminal protein lipidation [GO:0006501]; innate immune response [GO:0045087]; mitochondrion degradation [GO:0000422]; negative regulation of type I interferon production [GO:0032480]; nucleophagy [GO:0044804]!Atg8 ligase activity [GO:0019776]YAtg12-Atg5-Atg16 complex [GO:0034274]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus. {ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:17999726, ECO:0000269|PubMed:19074260, ECO:0000269|PubMed:19164948, ECO:0000269|PubMed:19666601, ECO:0000269|PubMed:23202584}.Q92598HS105Heat shock protein 105 kDa=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9931472}. cellular response to heat [GO:0034605]; chaperone mediated protein folding requiring cofactor [GO:0051085]; negative regulation of establishment of protein localization to mitochondrion [GO:1903748]; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:1903751]; negative regulation of p38MAPK cascade [GO:1903753]; positive regulation of MHC class I biosynthetic process [GO:0045345]; positive regulation of NK T cell activation [GO:0051135]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; receptor-mediated endocytosis [GO:0006898]; regulation of cellular response to heat [GO:1900034]; response to unfolded protein [GO:0006986]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]FUNCTION: Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity). {ECO:0000250}.Q7L775EPMIPEPM2A-interacting protein 1JSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12782127}.positive regulation of glycogen (starch) synthase activity [GO:2000467]; positive regulation of glycogen biosynthetic process [GO:0045725]; response to insulin [GO:0032868]Q8N4L2TM55A:Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphataseQ08117AES Amino-terminal en< hancer of splitcellular response to extracellular stimulus [GO:0031668]; multicellular organismal development [GO:0007275]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of gene expression [GO:0010629]; negative regulation of protein binding [GO:0032091]; negative regulation of response to cytokine stimulus [GO:0060761]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; organ morphogenesis [GO:0009887]; positive regulation of anoikis [GO:2000210]; regulation of growth [GO:0040008]; response to interleukin-1 [GO:0070555]; skeletal system development [GO:0001501]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]{FUNCTION: Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development. {ECO:0000269|PubMed:10660609, ECO:0000269|PubMed:10748198}.Q9H6X2ANTR1Anthrax toxin receptor 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell projection, filopodium membrane {ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Note=At the membrane of lamellipodia and at the tip of actin-enriched filopodia. Colocalizes with actin at the base of lamellipodia.actin cytoskeleton reorganization [GO:0031532]; reproductive process [GO:0022414]; signal transduction [GO:0007165]; substrate adhesion-dependent cell spreading [GO:0034446]actin filament binding [GO:0051015]; collagen binding [GO:0005518]; metal ion binding [GO:0046872]; transmembrane signaling receptor activity [GO:0004888]cell surface [GO:0009986]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; integral component of membrane [GO:0016021]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]FUNCTION: Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells. {ECO:0000269|PubMed:15777794, ECO:0000269|PubMed:16762926}.Q68CP4HGNAT/Heparan-alpha-glucosaminide N-acetyltransferaseYSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}. Note=Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain.carbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; lysosomal transport [GO:0007041]; protein oligomerization [GO:0051259]; small molecule metabolic process [GO:0044281]heparan-alpha-glucosaminide N-acetyltransferase activity [GO:0015019]; transferase activity, transferring acyl groups [GO:0016746]Lintegral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]XFUNCTION: Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20650889}.Q9H0H5RGAP1Rac GTPase-activating protein 17SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasmic vesicle, secretory vesicle, acrosome. Cleavage furrow. Midbody. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome (By similarity). During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody. Colocalizes with RHOA at the myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase. {ECO:0000250}. actomyosin contractile ring assembly [GO:0000915]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; embryo development [GO:0009790]; microtubule-based movement [GO:0007018]; mitotic cytokinesis [GO:0000281]; mitotic spindle assembly [GO:0090307]; mitotic spindle midzone assembly [GO:0051256]; neuroblast proliferation [GO:0007405]; positive regulation of cytokinesis [GO:0032467]; positive regulation of GTPase activity [GO:0043547]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; spermatogenesis [GO:0007283]; sulfate transport [GO:0008272]7alpha-tubulin binding [GO:0043014]; beta-tubulin binding [GO:0048487]; gamma-tubulin binding [GO:0043015]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein kinase binding [GO:0019901]acrosomal vesicle [GO:0001669]; centralspindlin complex [GO:0097149]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle midzone [GO:0051233]FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}.P51955NEK2$Serine/threonine-protein kinase Nek21SUBCELLULAR LOCATION: Isoform 1: Nucleus. Nucleus, nucleolus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere {ECO:0000250}. Note=< STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGOL1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Predominantly cytoplasmic.; SUBCELLULAR LOCATION: Isoform 4: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Predominantly nuclear.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; blastocyst development [GO:0001824]; cell division [GO:0051301]; centrosome separation [GO:0051299]; chromosome segregation [GO:0007059]; G2/M transition of mitotic cell cycle [GO:0000086]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly [GO:0090307]; negative regulation of centriole-centriole cohesion [GO:1903126]; negative regulation of DNA binding [GO:0043392]; organelle organization [GO:0006996]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; regulation of mitotic centrosome separation [GO:0046602]; regulation of mitotic nuclear division [GO:0007088]; spindle assembly [GO:0051225]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activity [GO:0004674]scentrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; kinetochore [GO:0000776]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein complex [GO:0043234]; spindle pole [GO:0000922]eFUNCTION: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Isoform 1 phosphorylates and activates NEK11 in G1/S-arrested cells. Isoform 2, which is not present in the nucleolus, does not. {ECO:0000269|PubMed:11742531, ECO:0000269|PubMed:12857871, ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:15161910, ECO:0000269|PubMed:15358203, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:17626005, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18297113, ECO:0000269|PubMed:20034488, ECO:0000269|PubMed:21076410}.Q00534CDK6Cyclin-dependent kinase 6FSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell projection, ruffle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23918663}. Note=Localized to the ruffling edge of spreading fibroblasts. Kinase activity only in nucleus. Localized to the cytosol of neurons and showed prominent staining around either side of the nucleus (By similarity). Present in the cytosol and in the nucleus in interphase cells and at the centrosome during mitosis from prophase to telophase (PubMed:23918663). {ECO:0000250|UniProtKB:Q64261, ECO:0000269|PubMed:23918663}.Gastrocyte development [GO:0014002]; cell cycle arrest [GO:0007050]; cell dedifferentiation [GO:0043697]; cell division [GO:0051301]; dentate gyrus development [GO:0021542]; G1/S transition of mitotic cell cycle [GO:0000082]; generation of neurons [GO:0048699]; gliogenesis [GO:0042063]; hematopoietic stem cell differentiation [GO:0060218]; lateral ventricle development [GO:0021670]; mitotic cell cycle [GO:0000278]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell differentiation [GO:0045596]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cellular senescence [GO:2000773]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of osteoblast differentiation [GO:0045668]; Notch signaling pathway [GO:0007219]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; protein phosphorylation [GO:0006468]; regulation of cell motility [GO:2000145]; regulation of erythrocyte differentiation [GO:0045646]; regulation of gene expression [GO:0010468]; response to virus [GO:0009615]; T cell differentiation in thymus [GO:0033077]; type B pancreatic cell development [GO:0003323]}ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]centrosome [GO:0005813]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ruffle [GO:0001726]vFUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans. May play a role in the centrosome organization during the cell cycle phases (PubMed:23918663). {ECO:0000269|PubMed:12833137, ECO:0000269|PubMed:14985467, ECO:0000269|PubMed:15254224, ECO:0000269|PubMed:15809340, ECO:0000269|PubMed:17420273, ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:20333249, ECO:0000269|PubMed:20668294, ECO:0000269|PubMed:23918663, ECO:0000269|PubMed:8114739}.P63313TYB10Thymosin beta-10FUNCTION: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). {ECO:0000250}.Q15847ADIRFAdipogenesis regulatory factor<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23239344}.dcell differentiation [GO:0030154]; cellular response to cisplatin [GO:0072719]; cellular response to radiation [GO:0071478]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of response to drug [GO:2001023]; transcription, DNA-templated [GO:0006351]uFUNCTION: Plays a role in fat cell development; promotes adipogenic differentiat< ion and stimulates transcription initiation of master adipogenesis factors like PPARG and CEBPA at early stages of preadipocyte differentiation. Its overexpression confers resistance to the anticancer chemotherapeutic drug cisplatin. {ECO:0000269|PubMed:19444912, ECO:0000269|PubMed:23239344}.Q96TA2YMEL1)ATP-dependent zinc metalloprotease YME1L1nSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10843804, ECO:0000269|PubMed:22262461}.cell proliferation [GO:0008283]; misfolded or incompletely synthesized protein catabolic process [GO:0006515]; mitochondrion organization [GO:0007005]dATP binding [GO:0005524]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]mintegral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743] FUNCTION: Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1. {ECO:0000269|PubMed:18076378, ECO:0000269|PubMed:22262461}.P25325THTM$3-mercaptopyruvate sulfurtransferase~SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. cyanate catabolic process [GO:0009440]; hydrogen sulfide biosynthetic process [GO:0070814]; kidney development [GO:0001822]; liver development [GO:0001889]; response to toxic substance [GO:0009636]; spinal cord development [GO:0021510]; transsulfuration [GO:0019346]o3-mercaptopyruvate sulfurtransferase activity [GO:0016784]; thiosulfate sulfurtransferase activity [GO:0004792]cell junction [GO:0030054]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; neuron projection [GO:0043005]; synapse [GO:0045202]kFUNCTION: Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions (By similarity). {ECO:0000250}.Q14CX7NAA254N-alpha-acetyltransferase 25, NatB auxiliary subunit>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18570629}.Ncytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp-Glu. May play a role in normal cell-cycle progression. {ECO:0000269|PubMed:18570629}.Q96H55MYO19Unconventional myosin-XIXSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19932026}. Mitochondrion outer membrane {ECO:0000269|PubMed:19932026}. Note=Probably associated with the outer membrane via its N-terminal mitochondrial targeting region.sATPase activity [GO:0016887]; ATP binding [GO:0005524]; plus-end directed microfilament motor activity [GO:0060002]^cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; myosin complex [GO:0016459]LFUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. MYO19 is involved in mitochondrial motility. {ECO:0000269|PubMed:19932026}.P16083NQO22Ribosyldihydronicotinamide dehydrogenase [quinone]memory [GO:0007613]{electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; NADPH dehydrogenase (quinone) activity [GO:0008753]Tcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]CFUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. {ECO:0000269|PubMed:18254726}.Q9BQT8ODC(Mitochondrial 2-oxodicarboxylate carriercellular nitrogen compound metabolic process [GO:0034641]; lysine catabolic process [GO:0006554]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]FUNCTION: Transports C5-C7 oxodicarboxylates across the inner membranes of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate, glutarate, and to a lesser extent, pimelate, 2-oxopimelate, 2-aminoadipate, oxaloacetate, and citrate.Q8NDF8PAPD5*Non-canonical poly(A) RNA polymerase PAPD5cSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Predominantly expressed in the cytoplasm.cell division [GO:0051301]; histone mRNA catabolic process [GO:0071044]; mitotic nuclear division [GO:0007067]; mRNA processing [GO:0006397]; rRNA processing [GO:0006364]DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; polynucleotide adenylyltransferase activity [GO:0004652]ZFUNCTION: Catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro). Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion. {ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21788334}.Q96IK1BOD17Biorientation of chromosomes in cell division protein 1\SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17938248}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17938248}. Note=Localizes at the centrosomes throughout the cell cycle, only dissociating during cytokinesis. Localizes at the kinetochore from prometaphase until anaphase.qcondensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]FUNCTION: Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000269|PubMed:17938248}.Q12907LMAN2)Vesicular integral-membrane protein VIP36SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:10444376}; Single-pass type I membrane protein {ECO:0000269|PubMed:10444376}. Golgi apparatus membrane {ECO:0000269|PubMed:10444376}; Single-pass membrane protein {ECO:0000269|PubMed:10444376}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10444376}; Single-pass type I membrane protein {ECO:0000269|PubMed:10444376}.positive regulation of phagocytosis [GO:0050766]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]carbohydrate binding [GO:0030246]; glycoprotein binding [GO:0001948]; heat shock protein binding [GO:0031072]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]cell surface [GO:0009986]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]8FUNCTION: Pl< ays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type glycans (By similarity). {ECO:0000250}.P48643TCPE#T-complex protein 1 subunit epsilonde novo' posttranslational protein folding [GO:0051084]; binding of sperm to zona pellucida [GO:0007339]; cellular protein metabolic process [GO:0044267]; protein folding [GO:0006457]; response to virus [GO:0009615]; toxin transport [GO:1901998]hATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; G-protein beta-subunit binding [GO:0031681]+cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; zona pellucida receptor complex [GO:0002199]P55285CADH6 Cadherin-6adherens junction organization [GO:0034332]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]Q9Y679AUP1Ancient ubiquitous protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132}; Single-pass type III membrane protein {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132}; Cytoplasmic side {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132}.8retrograde protein transport, ER to cytosol [GO:0030970]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: May play a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome. {ECO:0000269|PubMed:18711132}.Q9C0D3ZY11BProtein zyg-11 homolog Bfprotein ubiquitination [GO:0016567]; regulation of ubiquitin-protein transferase activity [GO:0051438]/Cul2-RING ubiquitin ligase complex [GO:0031462]pFUNCTION: Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC.Q9GZR2REXO4RNA exonuclease 4dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10908561, ECO:0000269|PubMed:12429849}.exonuclease activity [GO:0004527]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]P51665PSMD7.26S proteasome non-ATPase regulatory subunit 7cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]O75884RBBP9Putative hydrolase RBBP9eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12296629}. Nucleus {ECO:0000269|PubMed:12296629}.FUNCTION: May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1.O75436VP26A/Vacuolar protein sorting-associated protein 26A+SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane protein. Early endosome {ECO:0000269|PubMed:15078903}. Note=Localizes to tubular profiles adjacent to endosomes (PubMed:15078903). Predominantly found in early not late endosomes (By similarity). {ECO:0000250|UniProtKB:P40336}.cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; retromer complex [GO:0030904]; tubular endosome [GO:0097422]; vesicle [GO:0031982]FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins (Probable). The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:15078902, PubMed:15078903). Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (PubMed:15247922). Required for the endosomal localization of FAM21A (indicative for the WASH complex) (PubMed:22070227). Required for the endosomal localization of TBC1D5 (PubMed:20923837). Mediates retromer cargo reognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP (PubMed:22279231). Involved in retromer-independent lysosomal sorting of F2R (PubMed:16407403). Involved in recycling of ADRB2 (PubMed:21602791). Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity). {ECO:0000250|UniProtKB:P40336, ECO:0000269|PubMed:15078902, ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922, ECO:0000269|PubMed:16407403, ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:22279231, ECO:0000303|PubMed:20923837, ECO:0000303|PubMed:21602791, ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491, ECO:0000305}.Q7Z7M0MEGF87Multiple epidermal growth factor-like domains protein 8BMP signaling pathway [GO:0030509]; cell migration involved in gastrulation [GO:0042074]; craniofacial suture morphogenesis [GO:0097094]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of heart left/right asymmetry [GO:0061371]; embryonic heart tube left/right pattern formation [GO:0060971]; embryonic heart tube morphogenesis [GO:0003143]; embryonic limb morphogenesis [GO:0030326]; embryonic skeletal system morphogenesis [GO:0048704]; epiboly involved in gastrulation with mouth forming second [GO:0055113]; fasciculation of sensory neuron axon [GO:0097155]; left/right pattern formation [GO:0060972]; limb morphogenesis [GO:0035108]; positive regulation of axon extension involved in axon guidance [GO:0048842]; regulation of gene expression [GO:0010468]eextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]P11388TOP2ADNA topoisomerase 2-alphaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22013166}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22013166}. Note=Generally located in the nucleoplasm.apoptotic chromosome condensation [GO:0030263]; cellular response to DNA damage stimulus [GO:0006974]; chromosome segregation [GO:0007059]; DNA ligation [GO:0006266]; DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]; embryonic cleavage [GO:0040016]; hematopoietic progenitor cell differentiation [GO:0002244]; mitotic cell cycle [GO:0000278]; mitotic DNA integrity checkpoint [GO:0044774]; positive regulation of apoptotic process [GO:0043065]; positive regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045870]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral genome replication [GO:0045070]; regulation of circadian rhythm [GO:0042752]; resolution of meiotic recombination intermediates [GO:0000712]; rhythmic process [GO:0048511]; sister chromatid segregation [GO:0000819]^ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA-dependent ATPase activ< ity [GO:0008094]; DNA topoisomerase type II (ATP-hydrolyzing) activity [GO:0003918]; drug binding [GO:0008144]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080]; ubiquitin binding [GO:0043130]condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; DNA topoisomerase complex (ATP-hydrolyzing) [GO:0009330]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612}.Q53GS9SNUT2'U4/U6.U5 tri-snRNP-associated protein 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945}.cell cycle [GO:0007049]; cell division [GO:0051301]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]; ubiquitin-dependent protein catabolic process [GO:0006511]Jubiquitinyl hydrolase activity [GO:0036459]; zinc ion binding [GO:0008270]FUNCTION: Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs). {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:18728397}.P09382LEG1 Galectin-1hSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:14617626}.apoptotic process [GO:0006915]; cellular response to glucose stimulus [GO:0071333]; cellular response to organic cyclic compound [GO:0071407]; multicellular organismal response to stress [GO:0033555]; myoblast differentiation [GO:0045445]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of neuron projection development [GO:0010977]; plasma cell differentiation [GO:0002317]; positive regulation of erythrocyte aggregation [GO:0034120]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of viral entry into host cell [GO:0046598]; regulation of apoptotic process [GO:0042981]; response to axon injury [GO:0048678]; response to drug [GO:0042493]; signal transduction [GO:0007165]; T cell costimulation [GO:0031295]galactoside binding [GO:0016936]; lactose binding [GO:0030395]; poly(A) RNA binding [GO:0044822]; signal transducer activity [GO:0004871]cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular [GO:0005622]; nucleus [GO:0005634]; proteinaceous extracellular matrix [GO:0005578]kFUNCTION: May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000269|PubMed:14617626, ECO:0000269|PubMed:18796645, ECO:0000269|PubMed:19497882}.Q15642CIP4Cdc42-interacting protein 4SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Note=Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity). Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, perinuclear region.actin cytoskeleton organization [GO:0030036]; cell communication [GO:0007154]; endocytosis [GO:0006897]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]tcell cortex [GO:0005938]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]ZFUNCTION: Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:11069762, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391}.Q13643FHL3%Four and a half LIM domains protein 3Sactin cytoskeleton organization [GO:0030036]; muscle organ development [GO:0007517]afocal adhesion [GO:0005925]; nucleus [GO:0005634]; stress fiber [GO:0001725]; Z disc [GO:0030018]Q135414EBP1=Eukaryotic translation initiation factor 4E-binding protein 1]cellular protein metabolic process [GO:0044267]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; IRES-dependent translational initiation [GO:0002192]; lung development [GO:0030324]; negative regulation of protein complex assembly [GO:0031333]; negative regulation of translational initiation [GO:0045947]; positive regulation of mitotic cell cycle [GO:0045931]; response to ethanol [GO:0045471]; response to ischemia [GO:0002931]; TOR signaling [GO:0031929]; translation [GO:0006412]; translational initiation [GO:0006413]aeukaryotic initiation factor 4E binding [GO:0008190]; translation repressor activity [GO:0030371]YFUNCTION: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. {ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:7935836}.O15127SCAM2/Secretory carrier-associated membrane protein 2Rpost-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]3extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]; transport vesicle [GO:0030133]A6NKF9GPHRCPutative Golgi pH regulator CO95295SNAPNSNARE-associated protein SnapincSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic ve< sicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408}. Golgi apparatus membrane {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=May be cytoplasmic and peripheral membrane bound or anchored to the vesicular membrane through an N-terminal signal anchor (By similarity). Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000250}.anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; autophagosome maturation [GO:0097352]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; negative regulation of neuron projection development [GO:0010977]; neuron projection development [GO:0031175]; neurotransmitter secretion [GO:0007269]; positive regulation of late endosome to lysosome transport [GO:1902824]; regulation of protein binding [GO:0043393]; synaptic vesicle exocytosis [GO:0016079]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle transport [GO:0048489]; terminal button organization [GO:0072553]; viral process [GO:0016032]BLOC-1 complex [GO:0031083]; cell junction [GO:0030054]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; secretory granule [GO:0030141]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; transport vesicle [GO:0030133]$FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355}.Q14439GP176'Probable G-protein coupled receptor 176]G-protein coupled receptor signaling pathway [GO:0007186]; synaptic transmission [GO:0007268]FUNCTION: Orphan receptor.Q86YS7C2CD5C2 domain-containing protein 5tSUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21907143}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21907143}. Cell membrane {ECO:0000269|PubMed:21907143}. Cell projection, ruffle {ECO:0000269|PubMed:21907143}. Note=Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation.:cellular response to insulin stimulus [GO:0032869]; insulin receptor signaling pathway via phosphatidylinositol 3-kinase [GO:0038028]; intracellular protein transmembrane transport [GO:0065002]; membrane organization [GO:0061024]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of glucose transport [GO:0010828]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of vesicle fusion [GO:0031340]; protein localization to plasma membrane [GO:0072659]; vesicle fusion [GO:0006906]Ucalcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]zFUNCTION: Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. {ECO:0000269|PubMed:21907143}.Q13795ARFRP)ADP-ribosylation factor-related protein 1SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15077113}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8BXL7}. Note=Located in the trans-Golgi in the GTP-bound active state. {ECO:0000250|UniProtKB:Q8BXL7}.gastrulation [GO:0007369]; Golgi to plasma membrane protein transport [GO:0043001]; protein localization to Golgi apparatus [GO:0034067]; retrograde transport, endosome to Golgi [GO:0042147]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]UGolgi apparatus [GO:0005794]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. {ECO:0000250|UniProtKB:Q8BXL7}.Q9HD67MYO10Unconventional myosin-XSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10984435}. Cell projection, lamellipodium {ECO:0000269|PubMed:10984435}. Cell projection, ruffle {ECO:0000269|PubMed:10984435}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10984435}. Cell projection, filopodium tip {ECO:0000269|PubMed:10984435}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10984435}. Cell projection, filopodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Undergoes forward and rearward movements within filopodia. Interacts with microtubules.Vaxon guidance [GO:0007411]; cytoskeleton-dependent intracellular transport [GO:0030705]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; positive regulation of cell-cell adhesion [GO:0022409]; regulation of cell shape [GO:0008360]; regulation of filopodium assembly [GO:0051489]actin-dependent ATPase activity [GO:0030898]; actin filament binding [GO:0051015]; ATP binding [GO:0005524]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; plus-end directed microfilament motor activity [GO:0060002]; spectrin binding [GO:0030507]Jcell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium membrane [GO:0031527]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; myosin complex [GO:0016459]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. {ECO:0000269|PubMed:16894163, ECO:0000269|PubMed:18570893}.; FUNCTION: Isoform Headless: Functions as a dominant-negative regulator of isofo< rm 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion (By similarity). {ECO:0000250}.Q9H3F6BACD3NBTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19125419}.proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein homooligomerization [GO:0051260]; protein ubiquitination [GO:0016567]Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; TCTN-B9D complex [GO:0036038]FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity). {ECO:0000250}.O43854EDIL3@EGF-like repeat and discoidin I-like domain-containing protein 3cell adhesion [GO:0007155]; multicellular organismal development [GO:0007275]; positive regulation of cell-substrate adhesion [GO:0010811]?calcium ion binding [GO:0005509]; integrin binding [GO:0005178]Fextracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]FUNCTION: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.Q5VW32BROX#BRO1 domain-containing protein BROXISUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.P41223BUD31Protein BUD31 homologumRNA splicing, via spliceosome [GO:0000398]; regulation of transcription from RNA polymerase II promoter [GO:0006357]7nucleus [GO:0005634]; spliceosomal complex [GO:0005681]P17844DDX5(Probable ATP-dependent RNA helicase DDX5cSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10837141, ECO:0000269|PubMed:1996094}.cell growth [GO:0016049]; circadian rhythm [GO:0007623]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; in utero embryonic development [GO:0001701]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transcription [GO:0009299]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of osteoblast differentiation [GO:0045667]; regulation of skeletal muscle cell differentiation [GO:2001014]; regulation of viral genome replication [GO:0045069]; RNA secondary structure unwinding [GO:0010501]0androgen receptor binding [GO:0050681]; ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; estrogen receptor binding [GO:0030331]; poly(A) RNA binding [GO:0044822]; pre-mRNA binding [GO:0036002]; RNA helicase activity [GO:0003724]; transcription coactivator activity [GO:0003713]catalytic step 2 spliceosome [GO:0071013]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]YFUNCTION: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. {ECO:0000269|PubMed:10409727, ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:15298701, ECO:0000269|PubMed:15660129, ECO:0000269|PubMed:17011493, ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:18829551, ECO:0000269|PubMed:19718048, ECO:0000269|PubMed:21343338}.P56377AP1S2AP-1 complex subunit sigma-2SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex..AP-type membrane coat adaptor complex [GO:0030119]; clathrin-coated endocytic vesicle membrane [GO:0030669]; coated pit [GO:0005905]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; trans-Golgi network membrane [GO:0032588]Q9H477RBSK Ribokinase'D-ribose catabolic process [GO:0019303]:ATP binding [GO:0005524]; ribokinase activity [GO:0004747]Q9NZC9SMAL1cSWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19793862, ECO:0000269|PubMed:19793863}. Note=Recruited to damaged DNA regions. cellular response to DNA damage stimulus [GO:0006974]; DNA metabolic process [GO:0006259]; DNA repair [GO:0006281]; DNA strand renaturation [GO:0000733]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; replication fork processing [GO:0031297]annealing helicase activity [GO:0036310]; ATP binding [GO:0005524]; DNA-dependent ATPase activity [GO:0008094]; helicase activity [GO:0004386]Xnucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]MFUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks. {ECO:0000269|PubMed:18974355, ECO:0000269|PubMed:19793861, ECO:0000269|PubMed:19793862}.Q9UER7DAXX!Death domain-associated protein 6MAPKKKK regulator0SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus, PML body {ECO:0000269|PubMed:25275136}. Nucleus, nucleolus. Chromosome, centromere. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures.; SUBCELLULAR LOCATION: Isoform beta: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|Pub< Med:21482821}.; SUBCELLULAR LOCATION: Isoform gamma: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|PubMed:21482821}.activation of JUN kinase activity [GO:0007257]; androgen receptor signaling pathway [GO:0030521]; apoptotic process [GO:0006915]; cellular response to anoxia [GO:0071454]; cellular response to tumor necrosis factor [GO:0071356]; chromatin remodeling [GO:0006338]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; mitotic cytokinesis [GO:0000281]; negative regulation of myotube differentiation [GO:0010832]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome assembly [GO:0006334]; PML body organization [GO:0030578]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of histone phosphorylation [GO:0033129]; positive regulation of neuron death [GO:1901216]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; regulation of protein ubiquitination [GO:0031396]; regulation of transcription, DNA-templated [GO:0006355]; response to metal ion [GO:0010038]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]androgen receptor binding [GO:0050681]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; histone binding [GO:0042393]; p53 binding [GO:0002039]; protein homodimerization activity [GO:0042803]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]; receptor signaling protein activity [GO:0005057]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]mcell body [GO:0044297]; cell cortex [GO:0005938]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterochromatin [GO:0000792]; microtubule [GO:0005874]; neuron projection [GO:0043005]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605]; SWI/SNF superfamily-type complex [GO:0070603]; XY body [GO:0001741] FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activatiopn of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upopn neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.P50991TCPD!T-complex protein 1 subunit deltaSUBCELLULAR LOCATION: Cytoplasm. Melanosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.*cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; zona pellucida receptor complex [GO:0002199]Q9NVM9ASUNProtein asunder homolog>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23097494}.?cell division [GO:0051301]; centrosome localization [GO:0051642]; mitotic nuclear division [GO:0007067]; mitotic spindle organization [GO:0007052]; protein localization to nuclear envelope [GO:0090435]; regulation of fertilization [GO:0080154]; regulation of mitotic cell cycle [GO:0007346]; sperm motility [GO:0030317]QFUNCTION: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. {ECO:0000269|PubMed:15737938, ECO:0000269|PubMed:23097494}.Q96EP0RNF31!E3 ubiquitin-protein ligase RNF31CD40 signaling pathway [GO:0023035]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein linear polyubiquitination [GO:0097039]; protein polyubiquitination [GO:0000209]; T cell receptor signaling pathway [GO:0050852]ligase activity [GO:0016874]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; LUBAC complex [GO:0071797]FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC componen< ts by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types. {ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:22863777, ECO:0000269|PubMed:23708998}.O15438MRP35Canalicular multispecific organic anion transporter 2bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; transport [GO:0006810]ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; organic anion transmembrane transporter activity [GO:0008514]FUNCTION: May act as an inducible transporter in the biliary and intestinal excretion of organic anions. Acts as an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). {ECO:0000250}.P06241FYNTyrosine-protein kinase FynSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking. activated T cell proliferation [GO:0050798]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to transforming growth factor beta stimulus [GO:0071560]; dendrite morphogenesis [GO:0048813]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; feeding behavior [GO:0007631]; fibroblast growth factor receptor signaling pathway [GO:0008543]; forebrain development [GO:0030900]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; learning [GO:0007612]; leukocyte migration [GO:0050900]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of protein ubiquitination [GO:0031397]; neuron migration [GO:0001764]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet activation [GO:0030168]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of tyrosine phosphorylation of Stat5 protein [GO:0042523]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of cell proliferation [GO:0042127]; regulation of cell shape [GO:0008360]; regulation of defense response to virus by virus [GO:0050690]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell activation [GO:0042110]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]"ATP binding [GO:0005524]; ephrin receptor binding [GO:0046875]; glycoprotein binding [GO:0001948]; growth factor receptor binding [GO:0070851]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]actin filament [GO:0005884]; cytosol [GO:0005829]; endosome [GO:0005768]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]Q FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. {ECO:0000269|PubMed:11005864, ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117, ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091, ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753, ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597, ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7822789}.Q8N5C7DTWD1DTW domain-containing protein 1Q9C037TRIM4%Tripartite motif-containing protein 4>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}.linnate immune response [GO:0045087]; protein trimerization [GO:0070206]; protein ubiquitination [GO:0016567]FUNCTION: E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn't lead to proteasomal degradation but seems to enhance IFN induction. {ECO:0000269|PubMed:24755855}.Q8WUM9S20A1(Sodium-dependent phosphate transporter 15ion transport [GO:0006811]; phosphate-containing compound metabolic process [GO:0006796]; phosphate ion transmembrane transport [GO:0035435]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]; transmembrane transport [GO:0055085]; transport [GO:0006810]Dhigh-affinity inorganic phosphate:sodium symporter activity [GO:0005316]; inorganic phosphate transmembrane transporter activity [GO:0005315]; receptor activity [GO:0004872]; signal transducer activity [GO:0004871]; sodium:inorganic phosphate symporter activity [GO:0015< 319]; sodium:phosphate symporter activity [GO:0005436]hFUNCTION: Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport, such as absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification. May function as a retroviral receptor as it confers human cells susceptibility to infection to Gibbon Ape Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup B (FeLV-B) as well as 10A1 murine leukemia virus (10A1 MLV). {ECO:0000269|PubMed:11009570, ECO:0000269|PubMed:12097582, ECO:0000269|PubMed:1309898, ECO:0000269|PubMed:1531369, ECO:0000269|PubMed:2078500, ECO:0000269|PubMed:7929240, ECO:0000269|PubMed:7966619, ECO:0000269|PubMed:8041748}.Q6ZNB6NFXL1$NF-X1-type zinc finger protein NFXL1RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270]Xintegral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]P49641MA2A2Alpha-mannosidase 2xcellular protein metabolic process [GO:0044267]; mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein deglycosylation [GO:0006517]; protein N-linked glycosylation via asparagine [GO:0018279]alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; hydrolase activity, hydrolyzing N-glycosyl compounds [GO:0016799]; mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity [GO:0004572]; zinc ion binding [GO:0008270]FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.Q8WVX3CD003Uncharacterized protein C4orf3P19447ERCC3=TFIIH basal transcription factor complex helicase XPB subunit7-methylguanosine mRNA capping [GO:0006370]; apoptotic process [GO:0006915]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; gene expression [GO:0010467]; hair cell differentiation [GO:0035315]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA duplex unwinding [GO:0000717]; nucleotide-excision repair, DNA incision [GO:0033683]; positive regulation of apoptotic process [GO:0043065]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein localization [GO:0008104]; regulation of gene expression, epigenetic [GO:0040029]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]; response to UV [GO:0009411]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; UV protection [GO:0009650]; viral process [GO:0016032]3'-5' DNA helicase activity [GO:0043138]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; damaged DNA binding [GO:0003684]; dATP binding [GO:0032564]; DNA binding [GO:0003677]; GTP binding [GO:0005525]; peptide binding [GO:0042277]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]; transcription factor binding [GO:0008134]pcore TFIIH complex [GO:0000439]; holo TFIIH complex [GO:0005675]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]oFUNCTION: ATP-dependent 3'-5' DNA helicase, component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:8157004}.Q8IYD1ERF3BAEukaryotic peptide chain release factor GTP-binding subunit ERF3Bcell cycle [GO:0007049]; cellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; translation [GO:0006412]; translational termination [GO:0006415]%FUNCTION: Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. {ECO:0000269|PubMed:11524954, ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:17562865}.P50748KNTC1 Kinetochore-associated protein 1[SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Dynamic pattern of localization during the cell cycle. At interphase, uniformly distributed throughout the cytoplasm and nucleus. By prophase and until late stages of prometaphase, a fraction of the total pool is concentrated at kinetochores. By metaphase, detected at kinetochores, along spindle fibers and most prominently at the poles. By late anaphase until the end of telophase, no longer detectable on kinetochores or along spindle fibers, but still present at the spindle poles.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic nuclear division [GO:0007067]; protein complex assembly [GO:0006461]; regulation of exit from mitosis [GO:0007096]; small GTPase mediated signal transduction [GO:0007264] actin cytoskeleton [GO:0015629]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore microtubule [GO:0005828]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RZZ complex [GO:1990423]; spindle pole [GO:0000922]FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (PubMed:11146660, PubMed:11590237, PubMed:15824131). Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. {ECO:0000269|PubMed:11146660, ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15824131, ECO:0000305}.Q96EK6GNA1+Glucosamine 6-phosphate N-acetyltransferaseSUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.iglucosamine 6-phosphate N-acetyltransferase activity [GO:0004343]; identical protein binding [GO:0042802]cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; late endosome [GO:0005770]Q9UHB7AFF4AF4/FMR2 family member 4SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12065898}. Note=Associates to transcriptionally active chromatin but not at snRNA genes. {ECO:0000250}.^spermatid development [GO:0007286]; transcription from RNA polymerase II promoter [GO:0006366]mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleopl< asm [GO:0005654]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]; transcription elongation factor complex [GO:0008023]iFUNCTION: Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:23251033}.Q9BZZ5API5Apoptosis inhibitor 5SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11075807}. Cytoplasm {ECO:0000269|PubMed:11075807}. Note=Mainly nuclear. Can also be cytoplasmic.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; negative regulation of fibroblast apoptotic process [GO:2000270]Ofibroblast growth factor binding [GO:0017134]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs. {ECO:0000269|PubMed:10780674, ECO:0000269|PubMed:17112319, ECO:0000269|PubMed:19387494}.Q9P225DYH2Dynein heavy chain 2, axonemalLSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}.acilium or flagellum-dependent cell motility [GO:0001539]; microtubule-based movement [GO:0007018]>axonemal dynein complex [GO:0005858]; microtubule [GO:0005874]6FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.O94973AP2A2AP-2 complex subunit alpha-2GSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}.Vantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of defense response to virus by virus [GO:0050690]; synaptic transmission [GO:0007268]; viral process [GO:0016032]jlipid binding [GO:0008289]; protein kinase binding [GO:0019901]; protein transporter activity [GO:0008565]AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; plasma membrane [GO:0005886]FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250}.Q9UKI2BORG2Cdc42 effector protein 3(positive regulation of actin filament polymerization [GO:0030838]; positive regulation of GTPase activity [GO:0043547]; positive regulation of pseudopodium assembly [GO:0031274]; regulation of cell shape [GO:0008360]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]zcytoskeletal regulatory protein binding [GO:0005519]; GTPase activator activity [GO:0005096]; GTP-Rho binding [GO:0017049]wactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; plasma membrane [GO:0005886]FUNCTION: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}.P45985MP2K4:Dual specificity mitogen-activated protein kinase kinase 4activation of JUN kinase activity [GO:0007257]; apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]ATP binding [GO:0005524]; JUN kinase kinase activity [GO:0008545]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]Fcytosol [GO:0005829]; intracellular [GO:0005622]; nucleus [GO:0005634]FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in < their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. {ECO:0000269|PubMed:7716521}.Q8N9Z2CC71L)Coiled-coil domain-containing protein 71LP53680AP2S1AP-2 complex subunit sigmaSUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin coat assembly [GO:0048268]; clathrin-mediated endocytosis [GO:0072583]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of defense response to virus by virus [GO:0050690]; regulation of endocytosis [GO:0030100]; synaptic transmission [GO:0007268]; viral process [GO:0016032]AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; plasma membrane [GO:0005886]FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein Transport via Transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). May also play a role in extracellular calcium homeostasis. {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23222959}.Q96HW7INT4Integrator complex subunit 4Q9HC98NEK6$Serine/threonine-protein kinase Nek6SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus speckle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Colocalizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis.apoptotic process [GO:0006915]; chromosome segregation [GO:0007059]; cytokinesis [GO:0000910]; G2 DNA damage checkpoint [GO:0031572]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cellular senescence [GO:2000772]; regulation of mitotic cell cycle [GO:0007346]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; signal transduction [GO:0007165]; spindle assembly [GO:0051225]ATP binding [GO:0005524]; kinesin binding [GO:0019894]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle pole [GO:0000922]FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence. {ECO:0000269|PubMed:12054534, ECO:0000269|PubMed:14563848, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:19414596, ECO:0000269|PubMed:20407017, ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:21099361}.P35609ACTN2Alpha-actinin-2SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11171996, ECO:0000269|PubMed:19932097}. Note=Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.dactin filament uncapping [GO:0051695]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; establishment of protein localization to plasma membrane [GO:0090002]; focal adhesion assembly [GO:0048041]; microspike assembly [GO:0030035]; muscle filament sliding [GO:0030049]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of protein localization to cell surface [GO:2000009]; phospholipase C-activating angiotensin-activated signaling pathway [GO:0086097]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of cation channel activity [GO:2001259]; positive regulation of endocytic recycling [GO:2001137]; positive regulation of potassium ion transmembrane transporter activity [GO:1901018]; positive regulation of potassium ion transport [GO:0043268]; protein homotetramerization [GO:0051289]; regulation of apoptotic process [GO:0042981]; regulation of membrane potential [GO:0042391]; sarcomere organization [GO:0045214]; synaptic transmission [GO:0007268]Acalcium ion binding [GO:0005509]; cytoskeletal protein binding [GO:0008092]; FATZ binding [GO:0051373]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; ion channel binding [GO:0044325]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein dimerization activity [GO:0046983]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; structural constituent of muscle [GO:0008307]; thyroid hormone receptor coactivator activity [GO:0030375]; titin binding [GO:0031432]; titin Z domain binding [GO:0070080]lactin filament [GO:0005884]; cortical actin cytosk< eleton [GO:0030864]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; platelet alpha granule lumen [GO:0031093]; pseudopodium [GO:0031143]; Z disc [GO:0030018]O94830DDHD2Phospholipase DDHD2[SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network. Note=Cycles between the Golgi apparatus and the cytosol. DDHD2 recruitment to the Golgi/endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is regulated by the levels of phosphoinositides, including PI(4)P.cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; microtubule organizing center [GO:0005815]dFUNCTION: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane. {ECO:0000269|PubMed:11788596, ECO:0000269|PubMed:20932832, ECO:0000269|PubMed:22922100}.Q7L273KCTD9'BTB/POZ domain-containing protein KCTD9P49736MCM2%DNA replication licensing factor MCM2;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8175912}.~cell cycle [GO:0007049]; cellular response to interleukin-4 [GO:0071353]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA unwinding involved in DNA replication [GO:0006268]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; nucleosome assembly [GO:0006334]ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA replication origin binding [GO:0003688]; metal ion binding [GO:0046872]chromatin [GO:0000785]; cytoplasm [GO:0005737]; MCM complex [GO:0042555]; microtubule cytoskeleton [GO:0015630]; nuclear origin of replication recognition complex [GO:0005664]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division. {ECO:0000269|PubMed:8175912}.Q9C099LRCC1?Leucine-rich repeat and coiled-coil domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:18728398}. Note=Associates with the centrosome throughout the cell cycle and extensively accumulates during the mitotic phase.acentriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: Required for the organization of the mitotic spindle. Maintains the structural integrity of centrosomes during mitosis. {ECO:0000269|PubMed:18728398}.P05161ISG15Ubiquitin-like protein ISG15SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22859821}. Secreted {ECO:0000269|PubMed:22859821}. Note=Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins.cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; ISG15-protein conjugation [GO:0032020]; modification-dependent protein catabolic process [GO:0019941]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of type I interferon production [GO:0032480]; negative regulation of viral genome replication [GO:0045071]; positive regulation of erythrocyte differentiation [GO:0045648]; regulation of interferon-gamma production [GO:0032649]; response to type I interferon [GO:0034340]; translesion synthesis [GO:0019985]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]Qcytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]( FUNCTION: Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Can also isgylate: EIF2AK2/PKR which results in its activation, DDX58/RIG-I which inhibits its function in antiviral signaling response, EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB which prevents its ability to interact with the upstream activators of the JNK cascade therby inhibiting IFNA-induced JNK signaling. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1 and ebola virus via disruption of viral budding. Inhibits the ubiquitination of HIV-1 Gag and host TSG101 and disrupts their interaction, thereby preventing assembly and release of virions from infected cells. Inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein which causes a loss of function of the protein and the inhibition of virus replication. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. {ECO:0000269|PubMed:1373138, ECO:0000269|PubMed:16009940, ECO:0000269|PubMed:16112642, ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:16434471, ECO:0000269|PubMed:16872604, ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:19270716, ECO:0000269|PubMed:19357168, ECO:0000269|PubMed:2005397, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:20308324, ECO:0000269|PubMed:20639253, ECO:0000269|PubMed:21543490, ECO:0000269|PubMed:22693631, ECO:0000269|PubMed:22859821, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:7526157, ECO:0000269|PubMed:8550581}.P09601HMOX1Heme oxygenase 1SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:22419571}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22419571}; Peripheral membrane protein {ECO:0000269|PubMed:22419571}; Cytoplasmic side {ECO:0000269|PubMed:22419571}. angiogenesis [GO:0001525]; cell death [GO:0008219]; cellular iron ion homeostasis [GO:0006879]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to heat [GO:0034605]; cellular response to hypoxia [GO:0071456]; cellular response to nutrient [GO:0031670]; endothelial cell proliferation [GO:0001935]; erythrocyte homeostasis [GO:0034101]; excretion [GO:0007588]; heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; intracellular signal transduction [GO:0035556]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; iron ion homeostasis [GO:0055072]; low-density lipoprotein particle clearance [GO:0034383< ]; negative regulation of DNA binding [GO:0043392]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mast cell cytokine production [GO:0032764]; negative regulation of mast cell degranulation [GO:0043305]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of smooth muscle cell proliferation [GO:0048662]; porphyrin-containing compound metabolic process [GO:0006778]; positive regulation of angiogenesis [GO:0045766]; positive regulation of chemokine biosynthetic process [GO:0045080]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of vasodilation [GO:0045909]; protein homooligomerization [GO:0051260]; regulation of angiogenesis [GO:0045765]; regulation of blood pressure [GO:0008217]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of transcription from RNA polymerase II promoter in response to iron [GO:0034395]; regulation of transcription from RNA polymerase II promoter in response to oxidative stress [GO:0043619]; response to estrogen [GO:0043627]; response to hydrogen peroxide [GO:0042542]; response to nicotine [GO:0035094]; response to oxidative stress [GO:0006979]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; smooth muscle hyperplasia [GO:0014806]; transmembrane transport [GO:0055085]; wound healing involved in inflammatory response [GO:0002246] enzyme binding [GO:0019899]; heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]; phospholipase D activity [GO:0004630]; protein homodimerization activity [GO:0042803]; signal transducer activity [GO:0004871]caveola [GO:0005901]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.A5PL33KRBA1 Protein KRBA1P00441SODCSuperoxide dismutase [Cu-Zn]SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. activation of MAPK activity [GO:0000187]; anterograde axon cargo transport [GO:0008089]; auditory receptor cell stereocilium organization [GO:0060088]; blood coagulation [GO:0007596]; cell aging [GO:0007569]; cellular iron ion homeostasis [GO:0006879]; cellular response to ATP [GO:0071318]; cellular response to cadmium ion [GO:0071276]; cellular response to potassium ion [GO:0035865]; embryo implantation [GO:0007566]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide biosynthetic process [GO:0050665]; locomotory behavior [GO:0007626]; muscle cell cellular homeostasis [GO:0046716]; myeloid cell homeostasis [GO:0002262]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of neuron apoptotic process [GO:0043524]; neurofilament cytoskeleton organization [GO:0060052]; ovarian follicle development [GO:0001541]; peripheral nervous system myelin maintenance [GO:0032287]; placenta development [GO:0001890]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; positive regulation of cytokine production [GO:0001819]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of superoxide anion generation [GO:0032930]; reactive oxygen species metabolic process [GO:0072593]; regulation of blood pressure [GO:0008217]; regulation of GTPase activity [GO:0043087]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of multicellular organism growth [GO:0040014]; regulation of organ growth [GO:0046620]; regulation of protein kinase activity [GO:0045859]; regulation of T cell differentiation in thymus [GO:0033081]; relaxation of vascular smooth muscle [GO:0060087]; removal of superoxide radicals [GO:0019430]; response to amphetamine [GO:0001975]; response to antibiotic [GO:0046677]; response to antipsychotic drug [GO:0097332]; response to axon injury [GO:0048678]; response to carbon monoxide [GO:0034465]; response to copper ion [GO:0046688]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to nutrient levels [GO:0031667]; response to organic substance [GO:0010033]; response to reactive oxygen species [GO:0000302]; response to superoxide [GO:0000303]; retina homeostasis [GO:0001895]; retrograde axon cargo transport [GO:0008090]; sensory perception of sound [GO:0007605]; spermatogenesis [GO:0007283]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801]; thymus development [GO:0048538]; transmission of nerve impulse [GO:0019226]0chaperone binding [GO:0051087]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein phosphatase 2B binding [GO:0030346]; Rac GTPase binding [GO:0048365]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270]Fcytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; dense core granule [GO:0031045]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisome [GO:0005777]; protein complex [GO:0043234]sFUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.O15427MOT4Monocarboxylate transporter 4"Recepter Escape immunosurveillanceCblood coagulation [GO:0007596]; cellular metabolic process [GO:0044237]; leukocyte migration [GO:0050900]; monocarboxylic acid transport [GO:0015718]; plasma membrane lactate transport [GO:0035879]; pyruvate metabolic process [GO:0006090]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]lactate transmembrane transporter activity [GO:0015129]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; poly(A) RNA binding [GO:0044822]; symporter activity [GO:0015293]actin cytoskeleton [GO:0015629]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]LFUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity). {ECO:0000250}.P63167DYL1!Dynein light chain 1, cytoplasmicSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Note=Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.actin cytoskeleton organization [GO:0030036]; anatomical structure morphogen< esis [GO:0009653]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; apoptotic process [GO:0006915]; cilium morphogenesis [GO:0060271]; female gamete generation [GO:0007292]; G2/M transition of mitotic cell cycle [GO:0000086]; intraciliary retrograde transport [GO:0035721]; intrinsic apoptotic signaling pathway [GO:0097193]; mitotic cell cycle [GO:0000278]; negative regulation of phosphorylation [GO:0042326]; organelle organization [GO:0006996]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; regulation of transcription, DNA-templated [GO:0006355]; substantia nigra development [GO:0021762]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; primary cilium [GO:0072372]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.; FUNCTION: Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.; FUNCTION: Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.; FUNCTION: Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.Q9NQ29LUC7L(Putative RNA-binding protein Luc7-like 1omRNA splice site selection [GO:0006376]; negative regulation of striated muscle tissue development [GO:0045843]Aidentical protein binding [GO:0042802]; mRNA binding [GO:0003729]U1 snRNP [GO:0005685]UFUNCTION: May bind to RNA via its Arg/Ser-rich domain. {ECO:0000269|PubMed:11170747}.P36871PGM1Phosphoglucomutase-1+SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.dcarbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; glycolytic process [GO:0006096]; response to radiation [GO:0009314]; small molecule metabolic process [GO:0044281]Lmagnesium ion binding [GO:0000287]; phosphoglucomutase activity [GO:0004614]RFUNCTION: This enzyme participates in both the breakdown and synthesis of glucose.Q9P2Z0THA10!THAP domain-containing protein 10Q96MH6TMM68Transmembrane protein 68Q96RY7IF140,Intraflagellar transport protein 140 homologSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.cilium assembly [GO:0042384]; intraciliary retrograde transport [GO:0035721]; organelle organization [GO:0006996]; photoreceptor cell outer segment organization [GO:0035845]; protein localization to cilium [GO:0061512]; regulation of cilium assembly [GO:1902017]; renal system development [GO:0072001]; retina development in camera-type eye [GO:0060041]; skeletal system morphogenesis [GO:0048705] axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; intraciliary transport particle A [GO:0030991]; photoreceptor connecting cilium [GO:0032391]; photoreceptor outer segment [GO:0001750]; primary cilium [GO:0072372]FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Plays a pivotal role in proper development and function of ciliated cells. Involved in ciliogenesis and cilia maintenance. {ECO:0000269|PubMed:22503633}.Q09028RBBP4Histone-binding protein RBBP45ATP-dependent chromatin remodeling [GO:0043044]; CENP-A containing nucleosome assembly [GO:0034080]; chromatin assembly [GO:0031497]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA replication [GO:0006260]; DNA replication-dependent nucleosome assembly [GO:0006335]; DNA replication-independent nucleosome assembly [GO:0006336]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; negative regulation of cell proliferation [GO:0008285]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleosome assembly [GO:0006334]; regulation of cell cycle [GO:0051726]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]Fhistone binding [GO:0042393]; histone deacetylase binding [GO:0042826]CAF-1 complex [GO:0033186]; ESC/E(Z) complex [GO:0035098]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; NURF complex [GO:0016589]; protein complex [GO:0043234]; Sin3 complex [GO:0016580]FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654}.O75607NPM3Nucleoplasmin-3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11722795}.=rRNA processing [GO:0006364]; rRNA transcription [GO:0009303]!FUNCTION: May act as a chaperone.Q9NTX5ECHD1Ethylmalonyl-CoA decarboxylaseZcarboxy-lyase activity [GO:0016831]; methylmalonyl-CoA decarboxylase activity [GO:0004492] FUNCTION: Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level. {ECO:0000269|PubMed:22016388}.Q9H6T3RPAP3&RNA polymerase II-associated protein 3FUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. {ECO:0000269|PubMed:17643375}.O75152ZC11A.Zinc finger CCCH domain-containing protein 11A.poly(A)+ mRNA export from nucleus [GO:0016973]FUNCTION: Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex. {ECO:0000269|PubMed:22928037}.P41229KDM5CLysine-specific demethylase 5CSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:17468742}.chromatin organization [GO:0006325]; histone H3-K4 demethylation [GO:0034720]; negative regulation of transcription, DNA-templated [GO:0045892]; rhythmic process [GO:0048511]; transcription, DNA-templated [GO:0006351]CDNA binding [GO:0003677]; histone demethylase activity (H3-K4 specific) [GO:0032453]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one< atom each of oxygen into both donors [GO:0016706]; zinc ion binding [GO:0008270]FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 (By similarity). {ECO:0000250|UniProtKB:P41230, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17468742}.Q9BSH5HDHD3@Haloacid dehalogenase-like hydrolase domain-containing protein 3Q16643DREBDrebrinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20215400}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20215400}. Cell junction {ECO:0000269|PubMed:20215400}. Note=In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC).hactin filament organization [GO:0007015]; cell communication by chemical coupling [GO:0010643]; cell communication by electrical coupling [GO:0010644]; maintenance of protein location in cell [GO:0032507]; neural precursor cell proliferation [GO:0061351]; regulation of dendrite development [GO:0050773]; regulation of neuronal synaptic plasticity [GO:0048168]9actin binding [GO:0003779]; profilin binding [GO:0005522]actin cytoskeleton [GO:0015629]; actomyosin [GO:0042641]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; gap junction [GO:0005921]; plasma membrane [GO:0005886]FUNCTION: Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS. {ECO:0000269|PubMed:20215400}.Q14703MBTP13Membrane-bound transcription factor site-1 proteasecSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9990022}; Single-pass type I membrane protein {ECO:0000269|PubMed:9990022}. Golgi apparatus membrane {ECO:0000269|PubMed:9990022}; Single-pass type I membrane protein {ECO:0000269|PubMed:9990022}. Note=May sort to other organelles, including lysosomal and/or endosomal compartments.ATF6-mediated unfolded protein response [GO:0036500]; cellular protein metabolic process [GO:0044267]; cholesterol metabolic process [GO:0008203]; endoplasmic reticulum unfolded protein response [GO:0030968]; lipid metabolic process [GO:0006629]; lysosome organization [GO:0007040]; membrane protein intracellular domain proteolysis [GO:0031293]; proteolysis [GO:0006508]; response to endoplasmic reticulum stress [GO:0034976]; small molecule metabolic process [GO:0044281]endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of membrane [GO:0016021]IFUNCTION: Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes. {ECO:0000269|PubMed:21719679}.O76024WFS1 Wolframincalcium ion homeostasis [GO:0055074]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; ER overload response [GO:0006983]; glucose homeostasis [GO:0042593]; IRE1-mediated unfolded protein response [GO:0036498]; kidney development [GO:0001822]; negative regulation of ATF6-mediated unfolded protein response [GO:1903892]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of programmed cell death [GO:0043069]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; neurological system process [GO:0050877]; polyubiquitinated misfolded protein transport [GO:0070845]; positive regulation of adenylate cyclase activity [GO:0045762]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of growth [GO:0045927]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of proteolysis [GO:0045862]; protein maturation by protein folding [GO:0022417]; protein stabilization [GO:0050821]; renal water homeostasis [GO:0003091]; response to endoplasmic reticulum stress [GO:0034976]; sensory perception of sound [GO:0007605]; visual perception [GO:0007601]mATPase binding [GO:0051117]; transporter activity [GO:0005215]; ubiquitin protein ligase binding [GO:0031625]dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]FUNCTION: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. {ECO:0000269|PubMed:16989814}.Q3ZAQ7VMA218Vacuolar ATPase assembly integral membrane protein VMA21ySUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}.Hvacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]COPII vesicle coat [GO:0030127]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; lysosome [GO:0005764]FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691}.Q7Z6E9RBBP6!E3 ubiquitin-protein ligase RBBP6SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with mitotic chromosomes. Colocalizes with NEK6 in the centrosome.embryonic organ development [GO:0048568]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; somite development [GO:0061053]chromosome [GO:0005694]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome. May play a role as a scaffold protein to promote the assembly of the p53< /TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth.Q8WXW3PIBF1&Progesterone-induced-blocking factor 1centrosome [GO:0005813]FUNCTION: Mediator of progesterone that by acting on the phospholipase A2 enzyme interferes with arachidonic acid metabolism, induces a Th2 biased immune response, and by controlling NK activity exerts an anti-abortive effect.P46934NEDD4!E3 ubiquitin-protein ligase NEDD4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Recruited to the plasma membrane by GRB10. Once complexed with GRB10 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment (By similarity). May be recruited to exosomes by NDFIP1. {ECO:0000250, ECO:0000269|PubMed:18819914}.adaptive immune response [GO:0002250]; blood vessel morphogenesis [GO:0048514]; cellular response to UV [GO:0034644]; cytokine-mediated signaling pathway [GO:0019221]; development involved in symbiotic interaction [GO:0044111]; endocardial cushion development [GO:0003197]; glucocorticoid receptor signaling pathway [GO:0042921]; lysosomal transport [GO:0007041]; negative regulation of sodium ion transmembrane transporter activity [GO:2000650]; negative regulation of sodium ion transport [GO:0010766]; negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage [GO:0010768]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; neuromuscular junction development [GO:0007528]; neuron projection development [GO:0031175]; outflow tract morphogenesis [GO:0003151]; positive regulation of nucleocytoplasmic transport [GO:0046824]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein catabolic process [GO:0045732]; progesterone receptor signaling pathway [GO:0050847]; protein K63-linked ubiquitination [GO:0070534]; protein monoubiquitination [GO:0006513]; protein targeting to lysosome [GO:0006622]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; receptor catabolic process [GO:0032801]; receptor internalization [GO:0031623]; regulation of dendrite morphogenesis [GO:0048814]; regulation of ion transmembrane transport [GO:0034765]; regulation of membrane potential [GO:0042391]; regulation of potassium ion transmembrane transporter activity [GO:1901016]; regulation of synapse organization [GO:0050807]; response to calcium ion [GO:0051592]; T cell activation [GO:0042110]; transmission of virus [GO:0019089]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]beta-2 adrenergic receptor binding [GO:0031698]; ligase activity [GO:0016874]; phosphoserine binding [GO:0050815]; phosphothreonine binding [GO:0050816]; proline-rich region binding [GO:0070064]; protein domain specific binding [GO:0019904]; RNA polymerase binding [GO:0070063]; sodium channel inhibitor activity [GO:0019871]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]>apicolateral plasma membrane [GO:0016327]; cell cortex [GO:0005938]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). {ECO:0000269|PubMed:11598133, ECO:0000269|PubMed:17218260, ECO:0000269|PubMed:18305167, ECO:0000269|PubMed:18562292, ECO:0000269|PubMed:20086093, ECO:0000269|PubMed:21399620, ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:25631046}.P49761CLK3$Dual specificity protein kinase CLK3 SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus speckle. Note=Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.wprotein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of RNA splicing [GO:0043484]ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]acrosomal vesicle [GO:0001669]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]:FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. {ECO:0000269|PubMed:19168442, ECO:0000269|PubMed:9637771}.O75600KBL72-amino-3-ketobutyrate coenzyme A ligase, mitochondrialSUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17688197}. Note=Translocates to the nucleus upon cold and osmotic stress.biosynthetic process [GO:0009058]; cellular amino acid metabolic process [GO:0006520]; L-threonine catabolic process to glycine [GO:0019518][glycine C-acetyltransferase activity [GO:0008890]; pyridoxal phosphate binding [GO:0030170]P51948MAT1*CDK-activating kinase assembly factor MAT17-methylguanosine mRNA capping [GO:0006370]; adult heart development [GO:0007512]; cell proliferation [GO:0008283]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein complex assembly [GO:0006461]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to cal< cium ion [GO:0051592]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; ventricular system development [GO:0021591]; viral process [GO:0016032]Fprotein N-terminus binding [GO:0047485]; zinc ion binding [GO:0008270]Qcytoplasm [GO:0005737]; holo TFIIH complex [GO:0005675]; nucleoplasm [GO:0005654]FFUNCTION: Stabilizes the cyclin H-CDK7 complex to form a functional CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. {ECO:0000269|PubMed:10024882}.Q8TEU7RPGF6(Rap guanine nucleotide exchange factor 6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11524421}. Cell membrane {ECO:0000269|PubMed:11524421}. Note=Upon binding to M-Ras, it translocates to the plasma membrane.microvillus assembly [GO:0030033]; positive regulation of GTPase activity [GO:0043547]; protein localization to plasma membrane [GO:0072659]; Ras protein signal transduction [GO:0007265]; regulation of GTPase activity [GO:0043087]GTP-dependent protein binding [GO:0030742]; guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidic acid binding [GO:0070300]; Ras GTPase binding [GO:0017016]wapical plasma membrane [GO:0016324]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP. {ECO:0000269|PubMed:11524421, ECO:0000269|PubMed:12581858}.Q5H9R7PP6R3;Serine/threonine-protein phosphatase 6 regulatory subunit 3Ncytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance. {ECO:0000269|PubMed:11401438, ECO:0000269|PubMed:16769727}.O00487PSDE/26S proteasome non-ATPase regulatory subunit 14anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of endopeptidase activity [GO:0010950]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein K63-linked deubiquitination [GO:0070536]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; response to ethanol [GO:0045471]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral process [GO:0016032]endopeptidase activator activity [GO:0061133]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; proteasome binding [GO:0070628]cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]XFUNCTION: Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000269|PubMed:22909820, ECO:0000269|PubMed:9374539}.Q96M27PRRC1 Protein PRRC1DSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15541471}.Q9UBB9TFP11Tuftelin-interacting protein 11SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles. {ECO:0000250}.biomineral tissue development [GO:0031214]; mRNA splicing, via spliceosome [GO:0000398]; regulation of transcription, DNA-templated [GO:0006355]; RNA processing [GO:0006396]; spliceosomal complex disassembly [GO:0000390]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; proteinaceous extracellular matrix [GO:0005578]; spliceosomal complex [GO:0005681]; U2-type post-mRNA release spliceosomal complex [GO:0071008]fFUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix. {ECO:0000269|PubMed:19103666}.P20336RAB3ARas-related protein Rab-3ASynaptic vesicle cyclewaxonogenesis [GO:0007409]; constitutive secretory pathway [GO:0045054]; evoked neurotransmitter secretion [GO:0061670]; glutamate secretion [GO:0014047]; intracellular protein transport [GO:0006886]; lung development [GO:0030324]; maintenance of presynaptic active zone structure [GO:0048790]; mitochondrion organization [GO:0007005]; neuromuscular synaptic transmission [GO:0007274]; neurotransmitter secretion [GO:0007269]; positive regulation of exocytosis [GO:0045921]; positive regulation of regulated secretory pathway [GO:1903307]; post-embryonic development [GO:0009791]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; regulation of synaptic vesicle fusion to presynaptic membrane [GO:0031630]; respiratory system process [GO:0003016]; response to electrical stimulus [GO:005< 1602]; sensory perception of touch [GO:0050975]; synaptic transmission [GO:0007268]; synaptic vesicle exocytosis [GO:0016079]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle recycling [GO:0036465]; vesicle docking involved in exocytosis [GO:0006904]}ATPase activator activity [GO:0001671]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin V binding [GO:0031489]Jacrosomal vesicle [GO:0001669]; axon [GO:0030424]; clathrin-sculpted acetylcholine transport vesicle membrane [GO:0060201]; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202]; clathrin-sculpted glutamate transport vesicle membrane [GO:0060203]; clathrin-sculpted monoamine transport vesicle membrane [GO:0070083]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular vesicle [GO:1903561]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; secretory granule membrane [GO:0030667]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]FUNCTION: Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.P53365ARFP2 Arfaptin-2(actin cytoskeleton organization [GO:0030036]; lamellipodium assembly [GO:0030032]; movement of cell or subcellular component [GO:0006928]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; ruffle organization [GO:0031529]; small GTPase mediated signal transduction [GO:0007264]GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; phosphatidylinositol-4-phosphate binding [GO:0070273]; Rac GTPase binding [GO:0048365]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; trans-Golgi network membrane [GO:0032588]\FUNCTION: Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.Q86X10RLGPB*Ral GTPase-activating protein subunit betaactivation of GTPase activity [GO:0090630]; membrane organization [GO:0061024]; Ral protein signal transduction [GO:0032484]; regulation of exocyst localization [GO:0060178]; regulation of small GTPase mediated signal transduction [GO:0051056]FUNCTION: Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB. {ECO:0000250}.O00469PLOD21Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2fSUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cellular protein modification process [GO:0006464]; cellular response to hormone stimulus [GO:0032870]; extracellular matrix organization [GO:0030198]; response to hypoxia [GO:0001666]{iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-lysine 5-dioxygenase activity [GO:0008475]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; rough endoplasmic reticulum membrane [GO:0030867]FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.Q9BUD6SPON2 Spondin-2"axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense response to virus [GO:0051607]; induction of bacterial agglutination [GO:0043152]; innate immune response [GO:0045087]; mast cell mediated immunity [GO:0002448]; opsonization [GO:0008228]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of tumor necrosis factor production [GO:0032760]eantigen binding [GO:0003823]; lipopolysaccharide binding [GO:0001530]; metal ion binding [GO:0046872]uextracellular exosome [GO:0070062]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens (By similarity). Binds bacterial lipopolysaccharide (LPS). {ECO:0000250}.Q86U38NOP9Nucleolar protein 9Q12959DLG1Disks large homolog 1?SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse. Cell membrane, sarcolemma. Note=Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells. May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities (By similarity). {ECO:0000250}. actin filament organization [GO:0007015]; activation of protein kinase activity [GO:0032147]; amyloid precursor protein metabolic process [GO:0042982]; astral microtubule organization [GO:0030953]; axon guidance [GO:0007411]; bicellular tight junction assembly [GO:0070830]; branching involved in ureteric bud morphogenesis [GO:0001658]; cellular protein complex localization [GO:0034629]; cortical actin cytoskeleton organization [GO:0030866]; cortical microtubule organization [GO:0043622]; dephosphorylation [GO:0016311]; embryonic skeletal system morphogenesis [GO:0048704]; endothelial cell proliferation [GO:0001935]; establishment of centrosome localization [GO:0051660]; establishment or maintenance of cell polarity [GO:0007163]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; hard palate development [GO:0060022]; immunological synapse formation [GO:0001771]; lens development in camera-type eye [GO:0002088]; membrane raft organization [GO:0031579]; mitotic cell cycle checkpoint [GO:0007093]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of p38MAPK cascade [GO:1903753]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nervous system development [GO:0007399]; nucleotide phosphorylation [GO:0046939]; peristalsis [GO:0030432]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell proliferation [GO:0008284]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of potassium ion transport [GO:0043268]; protein localization to plasma membrane [GO:0072659]; receptor clustering [GO:0043113]; receptor localization to synapse [GO:0097120]; regulation of cell shape [GO:0008360]; regulation of membrane potential [GO:0042391]; regulation of myelination [GO:0031641]; regulation of sodium ion transmembrane transport [GO:1902305]; reproductive structure development [GO:0048608]; single organismal cell-cell adhesion [GO:0016337]; smooth muscle tissue development [GO:0048745]; synaptic transmission [GO:0007268]; T cell activation [GO:0042110]; T cell cytokine production [GO:0002369]; viral process [GO:0016032]cytoskeletal protein binding [GO:0008092]; guanylate kinase activity [GO:0004385]; ion channel binding [GO:0044325]; ionotropic glutamate receptor binding [GO:0035255]; L27 domain binding [GO:0097016]; mitogen-activated protein kinase kinase binding [GO:0031434]; phosphatase binding [GO:0019902]; phosphoprotein phosphatase activity [GO:0004721]; potassium channel regulator activity [GO:0015459]; protein C-terminus binding [GO:0008022]; protein kinase binding [GO:0019901]basal lamina [G< O:0005605]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cell junction [GO:0030054]; cell projection membrane [GO:0031253]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; intercalated disc [GO:0014704]; lateral loop [GO:0043219]; lateral plasma membrane [GO:0016328]; membrane raft [GO:0045121]; microtubule [GO:0005874]; MPP7-DLG1-LIN7 complex [GO:0097025]; myelin sheath abaxonal region [GO:0035748]; neuromuscular junction [GO:0031594]; node of Ranvier [GO:0033268]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]FUNCTION: Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. {ECO:0000250, ECO:0000269|PubMed:10656683, ECO:0000269|PubMed:12445884, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15263016, ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:20605917}.Q9Y5R4HEMK1&HemK methyltransferase family member 1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18541145}.DNA methylation [GO:0006306]tDNA binding [GO:0003677]; N-methyltransferase activity [GO:0008170]; protein methyltransferase activity [GO:0008276]FUNCTION: N5-glutamine methyltransferase responsible for the methylation of the GGQ triplet of the mitochondrial translation release factor MTRF1L. {ECO:0000269|PubMed:18541145}.O00423EMAL10Echinoderm microtubule-associated protein-like 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules. Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity). {ECO:0000250}.brain development [GO:0007420]; hematopoietic progenitor cell differentiation [GO:0002244]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]; neuroblast proliferation [GO:0007405]`calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; tubulin binding [GO:0015631]cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se (By similarity). {ECO:0000250}.Q9NVH2INT7Integrator complex subunit 7SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21659603}. Chromosome {ECO:0000269|PubMed:21659603}. Note=Localizes to sites of DNA damage in a H2AX-independent manner.wcellular response to ionizing radiation [GO:0071479]; DNA damage checkpoint [GO:0000077]; snRNA processing [GO:0016180]8chromosome [GO:0005694]; integrator complex [GO:0032039]FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Plays a role in DNA damage response (DDR) signaling during the S phase. {ECO:0000269|PubMed:21659603}.Q9BSR8YIPF4 Protein YIPF4SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:21757827}; Multi-pass membrane protein {ECO:0000269|PubMed:21757827}.endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]\FUNCTION: Involved in the maintenance of the Golgi structure. {ECO:0000269|PubMed:21757827}.Q92990GLMNGlomulin muscle cell differentiation [GO:0042692]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of T cell proliferation [GO:0042130]; neural tube closure [GO:0001843]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of interleukin-2 biosynthetic process [GO:0045086]; positive regulation of phosphorylation [GO:0042327]; regulation of gene expression, epigenetic [GO:0040029]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; vasculogenesis [GO:0001570]hepatocyte growth factor receptor binding [GO:0005171]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase inhibitor activity [GO:0055105]Cul2-RING ubiquitin ligase complex [GO:0031462]; Cul3-RING ubiquitin ligase complex [GO:0031463]; Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; cullin-RING ubiquitin ligase complex [GO:0031461]; intracellular [GO:0005622]nFUNCTION: Essential for normal development of the vasculature. May represent a naturally occurring ligand of the immunophilins FKBP59 and FKBP12. May function as an membrane anchoring protein. Isoform 1 may stimulate the p70S6K pathway. Isoform 2 may inhibit cell proliferation and increase IL2 production. {ECO:0000269|PubMed:11571281, ECO:0000269|PubMed:12604780}.P25205MCM3%DNA replication licensing factor MCM3VATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]alpha DNA polymerase:primase complex [GO:0005658]; centrosome [GO:0005813]; intracellular membrane-bounded organelle [GO:0043231]; MCM complex [GO:0042555]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation.Q52LJ0FA98BProtein FAM98BeSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24608264}. Cytoplasm {ECO:0000269|PubMed:24608264}.Wcytoplasm [GO:0005737]; nucleus [GO:0005634]; tRNA-splicing ligase complex [GO:0072669]P05198IF2A4Eukaryotic translation initiation factor 2 subunit 1/SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules (By similarity). {ECO:0000250}.6activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; PERK-mediated unfolded protein response [GO:0036499]; positive regulation of defense response to virus by h< ost [GO:0002230]; protein autophosphorylation [GO:0046777]; regulation of translational initiation in response to stress [GO:0043558]; translation [GO:0006412]; translational initiation [GO:0006413]; transmembrane transport [GO:0055085]tpoly(A) RNA binding [GO:0044822]; ribosome binding [GO:0043022]; translation initiation factor activity [GO:0003743]Pcytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 2 complex [GO:0005850]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; multi-eIF complex [GO:0043614]; nucleus [GO:0005634]; polysome [GO:0005844]; ribosome [GO:0005840]+FUNCTION: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.Q32P51RA1L21Heterogeneous nuclear ribonucleoprotein A1-like 2TmRNA processing [GO:0006397]; mRNA transport [GO:0051028]; RNA splicing [GO:0008380]9cytoplasm [GO:0005737]; spliceosomal complex [GO:0005681]FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. {ECO:0000250}.Q96A57TM230Transmembrane protein 230Q9UBV7B4GT7 Beta-1,4-galactosyltransferase 7SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Cis cisternae of Golgi stack.carbohydrate metabolic process [GO:0005975]; cellular protein modification process [GO:0006464]; chondroitin sulfate metabolic process [GO:0030204]; extracellular fibril organization [GO:0043206]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic process [GO:0030203]; negative regulation of fibroblast proliferation [GO:0048147]; protein N-linked glycosylation [GO:0006487]; proteoglycan metabolic process [GO:0006029]; small molecule metabolic process [GO:0044281]beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; galactosyltransferase activity [GO:0008378]; manganese ion binding [GO:0030145]; xylosylprotein 4-beta-galactosyltransferase activity [GO:0046525]extracellular matrix [GO:0031012]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. {ECO:0000269|PubMed:24052259}.Q6RFH5WDR74WD repeat-containing protein 74Eblastocyst formation [GO:0001825]; RNA metabolic process [GO:0016070]O43290SNUT1'U4/U6.U5 tri-snRNP-associated protein 1cSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:9449708}. Note=Found in the nucleus of mitogen-activated peripheral blood mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not in normal tissues except testis and fetal liver or in unstimulated PBMCs, suggesting preferential expression in proliferating cells.Dcell cycle arrest [GO:0007050]; intrinsic apoptotic signaling pathway [GO:0097193]; maturation of 5S rRNA [GO:0000481]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cytotoxic T cell differentiation [GO:0045585]; spliceosomal snRNP assembly [GO:0000387]Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; U4/U6 x U5 tri-snRNP complex [GO:0046540]FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945}.P49247RPIARibose-5-phosphate isomerasecarbohydrate metabolic process [GO:0005975]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]; small molecule metabolic process [GO:0044281]Wmonosaccharide binding [GO:0048029]; ribose-5-phosphate isomerase activity [GO:0004751]Kcytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]P48556PSMD8.26S proteasome non-ATPase regulatory subunit 8anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; G1/S transition of mitotic cell cycle [GO:0000082]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of protein stability [GO:0031647]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase.Q9C0D5TANC1 Protein TANC1ddendritic spine maintenance [GO:0097062]; myoblast fusion [GO:0007520]; visual learning [GO:0008542]axon terminus [GO:0043679]; cell junction [GO:0030054]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]QFUNCTION: May be a scaffold component in the postsynaptic density. {ECO:0000250}.Q8IXQ6PARP9Poly [ADP-ribose] polymerase 9SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Shuttles between the nucleus and the cytosol. Export to the cytosol depends on the interaction with DTX3L. Localizes at sites of DNA damage in a PARP1-dependent manner.}cell migration [GO:0016477]; double-strand break repair [GO:0006302]; regulation of response to interferon-gamma [GO:0060330]1NAD+ ADP-ribosyltransferase activity [GO:0003950]tFUNCTION: In concert with DTX3L plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Involved in inducing the expression of IFN-gamma-responsive genes. {ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:23230272}.P24468COT2COUP transcription factor 2anterior/posterior pattern specification [GO:0009952]; blood vessel morphogenes< is [GO:0048514]; fertilization [GO:0009566]; forebrain development [GO:0030900]; intracellular receptor signaling pathway [GO:0030522]; limb development [GO:0060173]; lipid metabolic process [GO:0006629]; maternal placenta development [GO:0001893]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron migration [GO:0001764]; placenta blood vessel development [GO:0060674]; positive regulation of transcription, DNA-templated [GO:0045893]; radial pattern formation [GO:0009956]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of transcription involved in lymphatic endothelial cell fate commitment [GO:0060849]; response to estradiol [GO:0032355]; signal transduction [GO:0007165]; skeletal muscle tissue development [GO:0007519]; transcription, DNA-templated [GO:0006351]; trophoblast giant cell differentiation [GO:0060707]ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0004879]; protein homodimerization activity [GO:0042803]; retinoic acid binding [GO:0001972]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; steroid hormone receptor activity [GO:0003707]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]iFUNCTION: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. {ECO:0000269|PubMed:18798693, ECO:0000269|PubMed:1899293, ECO:0000269|PubMed:9343308}.Q9BTY7HGH1Protein HGH1 homologQ15785TOM34+Mitochondrial import receptor subunit TOM34SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10101285}. Mitochondrion outer membrane {ECO:0000269|PubMed:10101285}; Peripheral membrane protein {ECO:0000269|PubMed:10101285}; Cytoplasmic side {ECO:0000269|PubMed:10101285}./protein targeting to mitochondrion [GO:0006626]'heat shock protein binding [GO:0031072]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays a role in the import of cytosolically synthesized preproteins into mitochondria. Binds the mature portion of precursor proteins. Interacts with cellular components, and possesses weak ATPase activity. May be a chaperone-like protein that helps to keep newly synthesized precursors in an unfolded import compatible state. {ECO:0000269|PubMed:10101285, ECO:0000269|PubMed:11913975, ECO:0000269|PubMed:9324309}.Q16649NFIL3.Nuclear factor interleukin-3-regulated protein0cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; immune response [GO:0006955]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of gene expression [GO:0010628]; transcription from RNA polymerase II promoter [GO:0006366]DNA binding [GO:0003677]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]FUNCTION: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts (By similarity). Represses transcriptional activity of PER1 (By similarity). Represses transcriptional activity of PER2 via the B-site on the promoter (By similarity). Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) (By similarity). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock (By similarity). Protects pro-B cells from programmed cell death (By similarity). {ECO:0000250}.P10114RAP2ARas-related protein Rap-2atSUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side. Midbody. Note=May also localize to the Golgi (PubMed:7962206) and the gelatinase-containing granules of neutrophils (PubMed:8391995). Colocalizes with RASGEF1B to midbody at telophase (PubMed:23894443). {ECO:0000269|PubMed:23894443, ECO:0000269|PubMed:7962206, ECO:0000269|PubMed:8391995}.Jactin cytoskeleton reorganization [GO:0031532]; cellular protein localization [GO:0034613]; cellular response to drug [GO:0035690]; establishment of protein localization [GO:0045184]; microvillus assembly [GO:0030033]; negative regulation of cell migration [GO:0030336]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of protein phosphorylation [GO:0001934]; protein localization to plasma membrane [GO:0072659]; Rap protein signal transduction [GO:0032486]; regulation of dendrite morphogenesis [GO:0048814]; regulation of JNK cascade [GO:0046328]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; midbody [GO:0030496]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading. {ECO:0000269|PubMed:14966141, ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:16540189, ECO:0000269|PubMed:18930710, ECO:0000269|PubMed:20159449}.Q6ZMZ3SYNE3 Nesprin-3SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000269|PubMed:21937718}; Single-pass type IV membrane protein {ECO:0000269|PubMed:21937718}. Nucleus envelope {ECO:0000269|PubMed:21937718}. Rough endoplasmic reticulum {ECO:0000250}.cytoskeletal anchoring at nuclear membrane [GO:0090286]; cytoskeleton organization [GO:0007010]; establishment of protein localization to membrane [GO:0090150]; regulation of cell shape [GO:0008360]integral component of membrane [GO:0016021]; LINC complex [GO:0034993]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear outer membrane [GO:0005640]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells. {ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:21937718}.Q7L1V2MON1B&Vacuolar fusion protein MON1 homolog BP49407ARRB1Beta-arrestin-1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Membr< ane, clathrin-coated pit {ECO:0000305}. Cell projection, pseudopodium {ECO:0000250}. Cytoplasmic vesicle. Note=Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in the nucleus. The oligomeric form is located in the cytoplasm. Translocates to the nucleus upon stimulation of OPRD1 (By similarity). {ECO:0000250}.activation of MAPK activity [GO:0000187]; blood coagulation [GO:0007596]; follicle-stimulating hormone signaling pathway [GO:0042699]; G-protein coupled receptor internalization [GO:0002031]; membrane organization [GO:0061024]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of GTPase activity [GO:0034260]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein ubiquitination [GO:0031397]; Notch signaling pathway [GO:0007219]; phototransduction [GO:0007602]; platelet activation [GO:0030168]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of histone acetylation [GO:0035066]; positive regulation of histone H4 acetylation [GO:0090240]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein binding [GO:0032092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of receptor internalization [GO:0002092]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-Golgi vesicle-mediated transport [GO:0006892]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567]; stress fiber assembly [GO:0043149]; transcription from RNA polymerase II promoter [GO:0006366]angiotensin receptor binding [GO:0031701]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; enzyme inhibitor activity [GO:0004857]; GTPase activator activity [GO:0005096]; insulin-like growth factor receptor binding [GO:0005159]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]; ubiquitin protein ligase binding [GO:0031625]basolateral plasma membrane [GO:0016323]; chromatin [GO:0000785]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; pseudopodium [GO:0031143]@FUNCTION: Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. {ECO:0000250, ECO:0000269|PubMed:12464600, ECO:00< 00269|PubMed:14711824, ECO:0000269|PubMed:15475570, ECO:0000269|PubMed:15611106, ECO:0000269|PubMed:15671180, ECO:0000269|PubMed:15878855, ECO:0000269|PubMed:16144840, ECO:0000269|PubMed:16280323, ECO:0000269|PubMed:16378096, ECO:0000269|PubMed:16492667, ECO:0000269|PubMed:16709866, ECO:0000269|PubMed:18337459, ECO:0000269|PubMed:18419762, ECO:0000269|PubMed:19620252, ECO:0000269|PubMed:19643177, ECO:0000269|PubMed:22457824, ECO:0000269|PubMed:23341447, ECO:0000269|PubMed:23633677}.Q13823NOG2Nucleolar GTP-binding protein 2FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation. {ECO:0000250}.Q8IX01SUGP2,SURP and G-patch domain-containing protein 2:FUNCTION: May play a role in mRNA splicing. {ECO:0000305}.P49757NUMBProtein numb homologDishevelled1/2/3/NUMB/BL(5)Dadherens junction organization [GO:0034332]; axon guidance [GO:0007411]; lateral ventricle development [GO:0021670]; lung epithelial cell differentiation [GO:0060487]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of protein localization to plasma membrane [GO:1903077]; neuroblast division in subventricular zone [GO:0021849]; Notch signaling pathway [GO:0007219]; positive regulation of cell migration [GO:0030335]; positive regulation of neurogenesis [GO:0050769]; positive regulation of polarized epithelial cell differentiation [GO:0030862]Gapical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; extrinsic component of plasma membrane [GO:0019897]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]; plasma membrane [GO:0005886])FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage.Q16831UPP1Uridine phosphorylase 1cellular response to glucose starvation [GO:0042149]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide catabolic process [GO:0009166]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside catabolic process [GO:0046135]; pyrimidine nucleoside salvage [GO:0043097]; small molecule metabolic process [GO:0044281]; UMP salvage [GO:0044206]; uridine catabolic process [GO:0006218]+uridine phosphorylase activity [GO:0004850] FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.Q9HCG7GBA2 Non-lysosomal glucosylceramidaseCSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Not localized to lipid rafts. {ECO:0000269|PubMed:17105727}.Ibile acid metabolic process [GO:0008206]; central nervous system neuron development [GO:0021954]; glucosylceramide catabolic process [GO:0006680]; glycoside catabolic process [GO:0016139]; glycosphingolipid metabolic process [GO:0006687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]Pbeta-glucosidase activity [GO:0008422]; glucosylceramidase activity [GO:0004348]endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo. Plays a role in central nevous system development. Required for proper formation of motor neuron axons. {ECO:0000269|PubMed:17105727, ECO:0000269|PubMed:23332916}.Q96PY6NEK1$Serine/threonine-protein kinase Nek1SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:21211617}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Associated with the pericentriolar material. Localizes to centrosome during interphase and mitosis (By similarity). {ECO:0000250}.activation of MAPK activity [GO:0000187]; cell division [GO:0051301]; cellular response to DNA damage stimulus [GO:0006974]; cilium assembly [GO:0042384]; kidney development [GO:0001822]; MAPK cascade [GO:0000165]; mitotic nuclear division [GO:0007067]; multicellular organism growth [GO:0035264]; protein phosphorylation [GO:0006468]; regulation of DNA damage checkpoint [GO:2000001]; response to ionizing radiation [GO:0010212]; spermatogenesis [GO:0007283] ATP binding [GO:0005524]; kinase activity [GO:0016301]; MAP kinase kinase activity [GO:0004708]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]centrosome [GO:0005813]; cytoplasm [GO:0005737]; intracellular [GO:0005622]; nucleus [GO:0005634]; pericentriolar material [GO:0000242]oFUNCTION: Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Implicated in the control of meiosis (By similarity). Involved in cilium assembly. In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death. {ECO:0000250, ECO:0000269|PubMed:20230784, ECO:0000269|PubMed:21211617}.P04150GCRGlucocorticoid receptorLSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946}. Mitochondrion. Nucleus {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946}. Note=Cytoplasmic in the absence of ligand, nuclear after ligand-binding.; SUBCELLULAR LOCATION: Isoform Beta: Nucleus. Note=Localized largely in the nucleus.xadrenal gland development [GO:0030325]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin modification [GO:0016568]; gene expression [GO:0010467]; glucocorticoid metabolic process [GO:0008211]; mammary gland duct morphogenesis [GO:0060603]; maternal behavior [GO:0042711]; negative regulation of glucocorticoid mediated signaling pathway [GO:1900170]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of glucocorticoid biosynthetic process [GO:0031946]; regulation of gluconeogenesis [GO:0006111]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]Uglucocorticoid-activated RNA polymerase II transcription factor binding transcription factor activity [GO:0038051]; glucocorticoid receptor activity [GO:0004883]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondria< l matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression. {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:21664385}.Q7Z434MAVS)Mitochondrial antiviral-signaling proteinNSUBCELLULAR LOCATION: Mitochondrion outer membrane. Mitochondrion. Peroxisome.activation of innate immune response [GO:0002218]; cellular response to exogenous dsRNA [GO:0071360]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of type I interferon production [GO:0032480]; negative regulation of viral genome replication [GO:0045071]; positive regulation of chemokine (C-C motif) ligand 5 production [GO:0071651]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of IP-10 production [GO:0071660]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type I interferon-mediated signaling pathway [GO:0060340]; regulation of peroxisome organization [GO:1900063]; RIG-I signaling pathway [GO:0039529]; signal transduction [GO:0007165]; viral process [GO:0016032]nCARD domain binding [GO:0050700]; protein kinase binding [GO:0019901]; signal transducer activity [GO:0004871]integral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778] FUNCTION: Required for innate immune defense against viruses. Acts downstream of DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis. {ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20451243}.Q8NF37PCAT1)Lysophosphatidylcholine acyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21498505}; Single-pass type II membrane protein {ECO:0000269|PubMed:21498505}. Golgi apparatus membrane {ECO:0000269|PubMed:21498505}; Single-pass type II membrane protein {ECO:0000269|PubMed:21498505}. Lipid droplet {ECO:0000269|PubMed:21498505}. Note=May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm.cellular lipid metabolic process [GO:0044255]; glycerophospholipid biosynthetic process [GO:0046474]; negative regulation of phosphatidylcholine biosynthetic process [GO:2001246]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylglycerol acyl-chain remodeling [GO:0036148]; phospholipid biosynthetic process [GO:0008654]; phospholipid metabolic process [GO:0006644]; positive regulation of protein catabolic process [GO:0045732]; retina development in camera-type eye [GO:0060041]; small molecule metabolic process [GO:0044281]; surfactant homeostasis [GO:0043129]; triglyceride biosynthetic process [GO:0019432];1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-alkenylglycerophosphocholine O-acyltransferase activity [GO:0047159]; 1-alkylglycerophosphocholine O-acetyltransferase activity [GO:0047192]; 1-alkylglycerophosphocholine O-acyltransferase activity [GO:0047191]; calcium ion binding [GO:0005509]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; membrane [GO:0016020] FUNCTION: Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology. {ECO:0000269|PubMed:16864775, ECO:0000269|PubMed:21498505}.Q9UIA9XPO7 Exportin-7SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000305}. Nucleus, nuclear pore complex {ECO:0000305}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000305}.EmRNA transport [GO:0051028]; protein export from nucleus [GO:0006611]4nuclear export signal receptor activity [GO:0005049]Gcytoplasm [GO:0005737]; nuclear pore [GO:0005643]; nucleus [GO:0005634]JFUNCTION: Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:11024021, ECO:0000269|PubMed:15282546}.P40123CAP2%Adenylyl cyclase-associated protein 2activation of adenylate cyclase activity [GO:0007190]; axon guidance [GO:0007411]; cytoskeleton organization [GO:0007010]; establishment or maintenance of cell polarity [GO:0007163]; signal transduction [GO:0007165]Hneuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]2FUNCTION: May have a regulatory bifunctional role.O96019ACL6AActin-like protein 6A<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18026119}.ATP-dependent chromatin remodeling [GO:0043044]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; neural retina development [GO:0003407]; positive regulation of protein < targeting to mitochondrion [GO:1903955]; regulation of growth [GO:0040008]; regulation of mitochondrion degradation [GO:1903146]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; spinal cord development [GO:0021510]; transcription, DNA-templated [GO:0006351]Ochromatin binding [GO:0003682]; transcription coactivator activity [GO:0003713]Ino80 complex [GO:0031011]; npBAF complex [GO:0071564]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; SWI/SNF complex [GO:0016514]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. {ECO:0000250, ECO:0000269|PubMed:14966270}.Q13547HDAC1Histone deacetylase 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170}.^ATP-dependent chromatin remodeling [GO:0043044]; blood coagulation [GO:0007596]; chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; embryonic digit morphogenesis [GO:0042733]; epidermal cell differentiation [GO:0009913]; eyelid development in camera-type eye [GO:0061029]; fungiform papilla formation [GO:0061198]; gene expression [GO:0010467]; hair follicle placode formation [GO:0060789]; histone deacetylation [GO:0016575]; histone H3 deacetylation [GO:0070932]; histone H4 deacetylation [GO:0070933]; mitotic cell cycle [GO:0000278]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell cycle [GO:0045786]; negative regulation of gene expression [GO:0010629]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of cell proliferation [GO:0008284]; positive regulation of receptor biosynthetic process [GO:0010870]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein deacetylation [GO:0006476]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]hactivating transcription factor binding [GO:0033613]; core promoter binding [GO:0001047]; deacetylase activity [GO:0019213]; enzyme binding [GO:0019899]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; NAD-dependent histone deacetylase activity (H3-K14 specific) [GO:0032041]; NF-kappaB binding [GO:0051059]; protein deacetylase activity [GO:0033558]; protein N-terminus binding [GO:0047485]; repressing transcription factor binding [GO:0070491]; RNA polymerase II repressing transcription factor binding [GO:0001103]; RNA polymerase II transcription corepressor activity [GO:0001106]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]; transcription regulatory region sequence-specific DNA binding [GO:0000976]chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone deacetylase complex [GO:0000118]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; protein complex [GO:0043234]; Sin3 complex [GO:0016580]lFUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. {ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227}.P15056BRAF%Serine/threonine-protein kinase B-rafSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cell membrane {ECO:0000250}. Note=Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes. {ECO:0000250}.activation of MAPKK activity [GO:0000186]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; cellular response to calcium ion [GO:0071277]; cellular response to drug [GO:0035690]; establishment of protein localization to membrane [GO:0090150]; fibroblast growth factor receptor signaling pathway< [GO:0008543]; glucose transport [GO:0015758]; head morphogenesis [GO:0060323]; long-term synaptic potentiation [GO:0060291]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ morphogenesis [GO:0009887]; positive regulation of axonogenesis [GO:0050772]; positive regulation of axon regeneration [GO:0048680]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive T cell selection [GO:0043368]; protein heterooligomerization [GO:0051291]; protein phosphorylation [GO:0006468]; regulation of cell proliferation [GO:0042127]; response to cAMP [GO:0051591]; response to peptide hormone [GO:0043434]; small GTPase mediated signal transduction [GO:0007264]; somatic stem cell maintenance [GO:0035019]; synaptic transmission [GO:0007268]; visual learning [GO:0008542]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]cell body [GO:0044297]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]3FUNCTION: Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway. {ECO:0000269|PubMed:21441910}.Q9H1A3METL9 Methyltransferase-like protein 9Q13356PPIL2*Peptidyl-prolyl cis-trans isomerase-like 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:8660300}. Note=May also localize to the cytoplasm and the cell membrane. {ECO:0000269|PubMed:15946952}.blood coagulation [GO:0007596]; leukocyte migration [GO:0050900]; protein folding [GO:0006457]; protein localization to plasma membrane [GO:0072659]; protein peptidyl-prolyl isomerization [GO:0000413]; protein polyubiquitination [GO:0000209]ligase activity [GO:0016874]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-ubiquitin ligase activity [GO:0034450]~cytoplasm [GO:0005737]; Golgi lumen [GO:0005796]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins (By similarity). May also function as a chaperone, playing a role in transport to the cell membrane of BSG for instance (PubMed:15946952). May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed:11435423). {ECO:0000250|UniProtKB:Q08752, ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:15946952, ECO:0000303|PubMed:8660300}.Q9NUA8ZBT400Zinc finger and BTB domain-containing protein 40bone mineralization [GO:0030282]; cellular response to DNA damage stimulus [GO:0006974]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]Q9UGJ1GCP4!Gamma-tubulin complex component 4G2/M transition of mitotic cell cycle [GO:0000086]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; protein complex assembly [GO:0006461]centrosome [GO:0005813]; cytosol [GO:0005829]; gamma-tubulin ring complex [GO:0008274]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; recycling endosome [GO:0055037]; spindle pole [GO:0000922]Q9HAT2SIAESialate O-acetylesterase7SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Secreted.]carbohydrate metabolic process [GO:0005975]; regulation of immune system process [GO:0002682].sialate O-acetylesterase activity [GO:0001681][extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosome [GO:0005764]|FUNCTION: Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid.P48634PRC2AProtein PRRC2AeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15752841}. Nucleus {ECO:0000269|PubMed:15752841}.cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]`FUNCTION: May play a role in the regulation of pre-mRNA splicing. {ECO:0000269|PubMed:14667819}.Q96BY6DOC10#Dedicator of cytokinesis protein 10aregulation of cell migration [GO:0030334]; small GTPase mediated signal transduction [GO:0007264]Uextracellular exosome [GO:0070062]; intracellular [GO:0005622]; membrane [GO:0016020]FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP.Q9BX95SGPP1%Sphingosine-1-phosphate phosphatase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12815058}; Multi-pass membrane protein {ECO:0000269|PubMed:12815058}.Vextrinsic apoptotic signaling pathway [GO:0097191]; intrinsic apoptotic signaling pathway [GO:0097193]; small molecule metabolic process [GO:0044281]; sphinganine-1-phosphate metabolic process [GO:0006668]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingosine metabolic process [GO:0006670]9sphingosine-1-phosphate phosphatase activity [GO:0042392]FUNCTION: Has enzymatic activity against both sphingosine 1-phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels. {ECO:0000269|PubMed:12815058}.Q8N6U8GP161G-protein coupled receptor 161SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded (By similarity). {ECO:0000250}.G-protein coupled receptor signaling pathway [GO:0007186]; multicellular organismal development [GO:0007275]; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:1901621]; positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway [GO:0010579]; positive regulation of cAMP biosynthetic process [GO:0030819]; regulation of smoothened signaling pathway [GO:0008589]; sensory perception of chemical stimulus [GO:0007606]hG-protein coupled amine receptor activity [GO:0008227]; G-protein coupled receptor activity [GO:0004930]ciliary membrane [GO:0060170]; endocytic vesicle membrane [GO:0030666]; integral component of plasma membrane [GO:0005887]; primary cilium [GO:0072372]; recycling endosome [GO:0055037]rFUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized< into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity). {ECO:0000250}.O00193SMAPSmall acidic proteinQ92834RPGR.X-linked retinitis pigmentosa GTPase regulatorJSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9R0X5}. Golgi apparatus {ECO:0000269|PubMed:15772089}.; SUBCELLULAR LOCATION: Isoform 6: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme.(cellular response to light stimulus [GO:0071482]; cilium assembly [GO:0042384]; eye photoreceptor cell development [GO:0042462]; intracellular protein transport [GO:0006886]; intraciliary transport [GO:0042073]; retina morphogenesis in camera-type eye [GO:0060042]; visual perception [GO:0007601]Yguanyl-nucleotide exchange factor activity [GO:0005085]; poly(A) RNA binding [GO:0044822]centrosome [GO:0005813]; ciliary basal body [GO:0036064]; Golgi apparatus [GO:0005794]; photoreceptor connecting cilium [GO:0032391]; photoreceptor outer segment [GO:0001750]; sperm flagellum [GO:0036126]FUNCTION: Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia. {ECO:0000250, ECO:0000269|PubMed:21933838}.Q12792TWF1 Twinfilin-1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts (By similarity). {ECO:0000250}.negative regulation of actin filament polymerization [GO:0030837]; regulation of actin phosphorylation [GO:0043538]; sequestering of actin monomers [GO:0042989]xactin monomer binding [GO:0003785]; ATP binding [GO:0005524]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]actin cytoskeleton [GO:0015629]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; myofibril [GO:0030016]; perinuclear region of cytoplasm [GO:0048471]]FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). {ECO:0000250}.O75762TRPA1@Transient receptor potential cation channel subfamily A member 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297}; Multi-pass membrane protein {ECO:0000305}.calcium ion transmembrane transport [GO:0070588]; cell surface receptor signaling pathway [GO:0007166]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; ion transmembrane transport [GO:0034220]; ion transport [GO:0006811]; protein homotetramerization [GO:0051289]; response to cold [GO:0009409]; response to drug [GO:0042493]; response to hydrogen peroxide [GO:0042542]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to pain [GO:0048265]; sensory perception of pain [GO:0019233]; thermoception [GO:0050955]; transmembrane transport [GO:0055085]channel activity [GO:0015267]; intracellular ligand-gated calcium channel activity [GO:0005218]; temperature-gated cation channel activity [GO:0097604]rintegral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; stereocilium bundle [GO:0032421]FUNCTION: Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function (PubMed:25389312, PubMed:25855297). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, cinnamaldehyde, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes (PubMed:25389312, PubMed:20547126). Is also activated by menthol (in vitro)(PubMed:25389312). Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity). {ECO:0000250|UniProtKB:Q8BLA8, ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297}.Q969K7TMM54Transmembrane protein 54Q96GM8TOE1Target of EGR1 protein 1SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12562764}. Nucleus speckle {ECO:0000269|PubMed:12562764}. Note=Localizes to nuclear speckles.bnuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Inhibits cell growth rate and cell cycle. Induces CDKN1A expression as well as TGF-beta expression. Mediates the inhibitory growth effect of EGR1. {ECO:0000269|PubMed:12562764}.Q8N567ZCHC9,Zinc finger CCHC domain-containing protein 9SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18721783}. Nucleus {ECO:0000269|PubMed:18721783}. Note=Expressed throughout the nucleus and concentrated mainly in the nucleolus. {ECO:0000269|PubMed:18721783}.8negative regulation of phosphatase activity [GO:0010923]FUNCTION: May down-regulate transcription mediated by NF-kappa-B and the serum response element. {ECO:0000269|PubMed:18721783}.O95528GTR10BSolute carrier family 2, facilitated glucose transporter member 10SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000269|PubMed:16550171}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}.glucose import [GO:0046323]; glucose transport [GO:0015758]; hexose transmembrane transport [GO:0035428]; proton transport [GO:0015992]; transmembrane transport [GO:0055085]cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]+FUNCTION: Facilitative glucose transporter.Q5SYE7NHSL1NHS-like protein 1Q96CN9GCC10GRIP and coiled-coil domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10209125}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.ocytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886];FUNCTION: Probably involved in maintaining Golgi structure.Q9NZJ4SACSSacsinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19208651}. Note=Predominantly cytoplasmic, a small portion is present in the nucleus and also shows a partial mitochondrial overlap with the mitochondrial marker Hsp60.Ynegative regulation of inclusion body assembly [GO:0090084]; protein folding [GO:0006457]cchaperone binding [GO:0051087]; Hsp70 protein binding [GO:0030544]; proteasome binding [GO:0070628]axon [GO:0030424]; cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. {ECO:0000269|PubMed:19208651}.P14324FPPSFarnesyl pyrophosphate synthasecholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate < biosynthetic process [GO:0033384]; small molecule metabolic process [GO:0044281]; viral process [GO:0016032]dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.O94880PHF14PHD finger protein 14?lung alveolus development [GO:0048286]; negative regulation of mesenchymal cell proliferation involved in lung development [GO:2000791]; negative regulation of platelet-derived growth factor receptor-alpha signaling pathway [GO:2000584]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]Q99547MPH6M-phase phosphoprotein 6QSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Cytoplasmic in M phase.$maturation of 5.8S rRNA [GO:0000460]jcytoplasm [GO:0005737]; exosome (RNase complex) [GO:0000178]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and may play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D. {ECO:0000269|PubMed:17412707}.Q9BRA0LSMD14N-alpha-acetyltransferase 38, NatC auxiliary subuniteSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19398576}. Nucleus {ECO:0000269|PubMed:19398576}.acytoplasm [GO:0005737]; NatC complex [GO:0031417]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. {ECO:0000269|PubMed:19398576}.P61326MGNProtein mago nashi homologSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19324961}. Nucleus speckle {ECO:0000269|PubMed:19324961}. Cytoplasm {ECO:0000269|PubMed:19324961}. Note=Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. {ECO:0000250}.catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator WIBG/PYM leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. {ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:22203037}.Q9Y6H1CHCH2NCoiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23303788}.positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cellular response to hypoxia [GO:1900037]; transcription, DNA-templated [GO:0006351]Usequence-specific DNA binding [GO:0043565]; transcription factor binding [GO:0008134]FUNCTION: Transcription factor. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen) (PubMed:23303788). {ECO:0000269|PubMed:23303788}.P12931SRC*Proto-oncogene tyrosine-protein kinase SrcSUBCELLULAR LOCATION: Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.angiotensin-activated signaling pathway involved in heart process [GO:0086098]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; bone resorption [GO:0045453]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to fluid shear stress [GO:0071498]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to progesterone stimulus [GO:0071393]; cellular response to reactive oxygen species [GO:0034614]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; forebrain development [GO:0030900]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; leukocyte migration [GO:0050900]; membrane organization [GO:0061024]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of mitochondrial depolarization [GO:0051902]; negative regulation of protein homooligomerization [GO:0032463]; neurotrophin TRK receptor signaling pathway [GO:0048011]; oogenesis [GO:0048477]; osteoclast development [GO:0036035]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet activation [GO:0030168]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of integrin activation [GO:0033625]; positive regulation of lamellipodium morphogenesis [GO:2000394]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein kinase B signaling [GO:0051897]; progesterone receptor signaling pathway [GO:0050847]; protein autophosphorylation [GO:0046777]; protein destabilization [GO:0031648]; Ras protein signal transduction [GO:0007265]; regulation of bone resorption [GO:0045124]; regulation of caveolin-mediated endocytosis [GO:2001286]; regulation of cell-cell adhesion [GO:0022407]; regulation of cell cycle [GO:0051726]; regulation of cell projection assembly [GO:0060491]; regulation of cell proliferation [GO:0042127]; regulation of early endosome to late endosome transport [GO< :2000641]; regulation of epithelial cell migration [GO:0010632]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of podosome assembly [GO:0071801]; regulation of protein binding [GO:0043393]; regulation of vascular permeability [GO:0043114]; response to interleukin-1 [GO:0070555]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress fiber assembly [GO:0043149]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell costimulation [GO:0031295]; transforming growth factor beta receptor signaling pathway [GO:0007179]; uterus development [GO:0060065]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]vATP binding [GO:0005524]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; growth factor receptor binding [GO:0070851]; heme binding [GO:0020037]; hormone receptor binding [GO:0051427]; integrin binding [GO:0005178]; ion channel binding [GO:0044325]; kinase activity [GO:0016301]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphoprotein binding [GO:0051219]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; scaffold protein binding [GO:0097110]; SH2 domain binding [GO:0042169]; SH3/SH2 adaptor activity [GO:0005070]actin filament [GO:0005884]; caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; late endosome [GO:0005770]; lysosome [GO:0005764]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]}FUNCTION: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. {ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483, ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729}.Q96DH6MSI2H%RNA-binding protein Musashi homolog 2OSUBCELLULAR LOCATION: Cytoplasm. Note=Associated with polysomes. {ECO:0000250}."stem cell development [GO:0048864]cnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]-cytoplasm [GO:0005737]; polysome [GO:0005844]FUNCTION: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity). {ECO:0000250}.Q99576T22D3TSC22 domain family protein 3?SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the cytoplasm, but in differentiating myoblasts, isoform 1 is localized to the nucleus (By similarity). {ECO:0000250}.ion transmembrane transport [GO:0034220]; negative regulation of activation-induced cell death of T cells [GO:0070236]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription, DNA-templated [GO:0006355]; response to osmotic stress [GO:0006970]; transmembrane transport [GO:0055085]FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities (By similarity). Iso< form 1 inhibits myogenic differentiation and mediates anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG (By similarity). {ECO:0000250}.Q70EK8UBP531Inactive ubiquitin carboxyl-terminal hydrolase 53:ubiquitin-dependent protein catabolic process [GO:0006511]+ubiquitinyl hydrolase activity [GO:0036459]CFUNCTION: Has no peptidase activity. {ECO:0000269|PubMed:14715245}.Q9NQ34TMM9BTransmembrane protein 9BSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:18541524}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18541524}; Single-pass membrane protein {ECO:0000255}.rearly endosome membrane [GO:0031901]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]FUNCTION: Enhances production of proinflammatory cytokines induced by TNF, IL1B, and TLR ligands. Has a role in TNF activation of both the NF-kappaB and MAPK pathways. {ECO:0000269|PubMed:18541524}.Q9H4A5GLP3LGolgi phosphoprotein 3-likeSUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:23345592}; Peripheral membrane protein {ECO:0000269|PubMed:23345592}; Cytoplasmic side {ECO:0000269|PubMed:23345592}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23345592}; Peripheral membrane protein {ECO:0000269|PubMed:23345592}; Cytoplasmic side {ECO:0000269|PubMed:23345592}. Note=Phosphatidylinositol 4-phosphate (PtdIns4P)-binding mediates recruitment to Golgi membranes.VGolgi organization [GO:0007030]; positive regulation of protein secretion [GO:0050714]lGolgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; trans-Golgi network membrane [GO:0032588]FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that may antagonize the action of GOLPH3 which is required for the process of vesicle budding at the Golgi and anterograde transport to the plasma membrane. {ECO:0000269|PubMed:23345592}.Q14651PLSI Plastin-1 intestinal D-glucose absorption [GO:0001951]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of multicellular organism growth [GO:0040018]; regulation of microvillus length [GO:0032532]; terminal web assembly [GO:1902896]zactin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; structural constituent of cytoskeleton [GO:0005200]Xbrush border [GO:0005903]; extracellular exosome [GO:0070062]; terminal web [GO:1990357];FUNCTION: Actin-bundling protein in the absence of calcium.Q01085TIARNucleolysin TIARSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic granule. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules (By similarity). Cytoplasmic granules of cytolytic T-lymphocytes. {ECO:0000250}.apoptotic process [GO:0006915]; defense response [GO:0006952]; germ cell development [GO:0007281]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; stem cell division [GO:0017145]AU-rich element binding [GO:0017091]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; nucleus [GO:0005634]FUNCTION: RNA-binding protein. Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.Q9BYX7ACTBM"Putative beta-actin-like protein 3eblood coagulation [GO:0007596]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]vcytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]Q99986VRK1$Serine/threonine-protein kinase VRK1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis.cell division [GO:0051301]; endocytosis [GO:0006897]; Golgi disassembly [GO:0090166]; histone H3-S10 phosphorylation [GO:0043987]; histone H3-T3 phosphorylation [GO:0072355]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; mitotic nuclear envelope reassembly [GO:0007084]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; Wnt signaling pathway [GO:0016055]3ATP binding [GO:0005524]; histone kinase activity (H3-S10 specific) [GO:0035175]; histone kinase activity (H3-T3 specific) [GO:0072354]; nucleosomal histone binding [GO:0031493]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi stack [GO:0005795]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity. {ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:15105425, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:19103756}.Q8WU76SCFD2'Sec1 family domain-containing protein 2Sprotein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]/FUNCTION: May be involved in protein transport.Q8IZJ3CPMD8AC3 and PZP-like alpha-2-macroglobulin domain-containing protein 8SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15177561}. Cell membrane {ECO:0000269|PubMed:15177561}; Peripheral membrane protein {ECO:0000269|PubMed:15177561}; Extracellular side {ECO:0000269|PubMed:15177561}.>extracellular space [GO:0005615]; plasma membrane [GO:0005886]Q5T5U3RHG21 Rho GTPase-activating protein 21SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Cell junction. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Note=Localization to the Golgi is dependent on interaction with GTP-bound ARF1.0establishment of Golgi localization [GO:0051683]; Golgi organization [GO:0007030]; maintenance of Golgi location [GO:0051684]; organelle transport along microtubule [GO:0072384]; positive regulation of GTPase activity [GO:0043547]; regulation of endocytosis [GO:0030100]; signal transduction [GO:0007165]cell junction [GO:0030054]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]FUNCTION: Functions as a GTPase-activating protein (GAP) for RHOA and CDC42. Downstream partner of ARF1 which may control Golgi apparatus structure and function. Also required for CTNNA1 recruitment to adherens junctions. {ECO:0000269|PubMed:15793564, ECO:0000269|PubMed:16184169}.Q15637SF01Splicing factor 1Leydig cell differentiation [GO:0033327]; male sex determination [GO:0030238]; mRNA 3'-splice site recognition [GO:0000389]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of smooth muscle cell proliferation [GO:0048662]; regulation of steroid biosynthetic process [GO:0050810]; regulation of transcription, DNA-templated [GO:0006355]; spliceosomal complex assembly [GO:0000245]; transcription, DN< A-templated [GO:0006351]poly(A) RNA binding [GO:0044822]; pre-mRNA branch point binding [GO:0045131]; RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]hnucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribosome [GO:0005840]; spliceosomal complex [GO:0005681]FUNCTION: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}.Q8IXS6PALM2 Paralemmin-2nSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.%regulation of cell shape [GO:0008360]P05067A4Amyloid beta A4 protein3SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions.adult locomotory behavior [GO:0008344]; axon cargo transport [GO:0008088]; axon midline choice point recognition [GO:0016199]; axonogenesis [GO:0007409]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cellular copper ion homeostasis [GO:0006878]; cholesterol metabolic process [GO:0008203]; collateral sprouting in absence of injury [GO:0048669]; dendrite development [GO:0016358]; endocytosis [GO:0006897]; extracellular matrix organization [GO:0030198]; forebrain development [GO:0030900]; innate immune response [GO:0045087]; ionotropic glutamate receptor signaling pathway [GO:0035235]; locomotory behavior [GO:0007626]; mating behavior [GO:0007617]; membrane organization [GO:0061024]; mRNA polyadenylation [GO:0006378]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of neuron differentiation [GO:0045665]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; neuron projection development [GO:0031175]; neuron remodeling [GO:0016322]; Notch signaling pathway [GO:0007219]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-Golgi vesicle-mediated transport [GO:0006892]; protein phosphorylation [GO:0006468]; regulation of epidermal growth factor-activated receptor activity [GO:0007176]; regulation of multicellular organism growth [GO:0040014]; regulation of protein binding [GO:0043393]; regulation of synapse structure or activity [GO:0050803]; regulation of translation [GO:0006417]; response to oxidative stress [GO:0006979]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563]; suckling behavior [GO:0001967]; synaptic growth at neuromuscular junction [GO:0051124]; visual learning [GO:0008542]yacetylcholine receptor binding [GO:0033130]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; peptidase activator activity [GO:0016504]; PTB domain binding [GO:0051425]; receptor binding [GO:0005102]; serine-type endopeptidase inhibitor activity [GO:0004867]; transition metal ion binding [GO:0046914]3apical part of cell [GO:0045177]; axon [GO:0030424]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; endosome [GO:0005768]; endosome lumen [GO:0031904]; ER to Golgi transport vesicle [GO:0030134]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; membrane raft [GO:0045121]; neuromuscular junction [GO:0031594]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; receptor complex [GO:0043235]; smooth endoplasmic reticulum [GO:0005790]; spindle midzone [GO:0051233]; synapse [GO:0045202]; terminal bouton [GO:0043195]; trans-Golgi network membrane [GO:0032588] FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. {ECO:0000250}.; FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts.; FUNCTION: Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. {ECO:0000250}.; FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.; FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase< -3) and axons (via caspase-6).Q86WA6BPHLValacyclovir hydrolase\cellular amino acid metabolic process [GO:0006520]; response to toxic substance [GO:0009636]FUNCTION: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. {ECO:0000269|PubMed:18256025}.Q5T9A4ATD3B.ATPase family AAA domain-containing protein 3BSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16909202, ECO:0000269|PubMed:18063578}; Peripheral membrane protein {ECO:0000269|PubMed:16909202, ECO:0000269|PubMed:18063578}. Note=Has been found to co-purify with nucleoids (PubMed:22453275). Since it does not face the mitochondrial matrix, the association with nucleoids could be mediated by ATAD3A. {ECO:0000269|PubMed:22453275}.PFUNCTION: May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes. {ECO:0000269|PubMed:22664726}.P50281MMP14Matrix metalloproteinase-14SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Melanosome. Cytoplasm. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm. angiogenesis [GO:0001525]; astrocyte cell migration [GO:0043615]; branching morphogenesis of an epithelial tube [GO:0048754]; chondrocyte proliferation [GO:0035988]; collagen catabolic process [GO:0030574]; craniofacial suture morphogenesis [GO:0097094]; embryonic cranial skeleton morphogenesis [GO:0048701]; endochondral ossification [GO:0001958]; endodermal cell differentiation [GO:0035987]; endothelial cell proliferation [GO:0001935]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; lung development [GO:0030324]; male gonad development [GO:0008584]; negative regulation of focal adhesion assembly [GO:0051895]; ovarian follicle development [GO:0001541]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; proteolysis [GO:0006508]; response to estrogen [GO:0043627]; response to hypoxia [GO:0001666]; response to mechanical stimulus [GO:0009612]; response to oxidative stress [GO:0006979]; tissue remodeling [GO:0048771]; zymogen activation [GO:0031638]calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; peptidase activator activity [GO:0016504]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]cytoplasmic vesicle [GO:0031410]; extracellular matrix [GO:0031012]; focal adhesion [GO:0005925]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; macropinosome [GO:0044354]; melanosome [GO:0042470]; plasma membrane [GO:0005886]FUNCTION: Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. {ECO:0000269|PubMed:12714657, ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:22065321}.Q8NEM2SHCBP SHC SH2 domain-binding protein 1fibroblast growth factor receptor signaling pathway [GO:0008543]; regulation of neural precursor cell proliferation [GO:2000177]FUNCTION: May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells (By similarity). {ECO:0000250}.Q13017RHG05Rho GTPase-activating protein 5SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Also membrane-associated when found in fibrillar patterns that colocalize with the alpha5-beta1 integrin receptor (ITGA5/ITGB1) for fibronectin.cell adhesion [GO:0007155]; positive regulation of cell migration [GO:0030335]; positive regulation of GTPase activity [GO:0043547]; positive regulation of mesenchymal cell proliferation [GO:0002053]; regulation of cell size [GO:0008361]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; SH2 domain binding [GO:0042169]FUNCTION: GTPase-activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of RASA1/p120GAP.Q15771RAB30Ras-related protein Rab-30SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:22188167}. Cytoplasm {ECO:0000269|PubMed:22188167}. Golgi apparatus {ECO:0000269|PubMed:22188167}.Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; lipid particle organization [GO:0034389]; Rab protein signal transduction [GO:0032482]cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi stack [GO:0005795]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]TFUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for maintaining the structural integrity of the Golgi apparatus, possibly by mediating interactions with cytoplasmic scaffolding proteins. {ECO:0000250, ECO:0000269|PubMed:22188167}.Q8NI37PPTC7 Protein phosphatase PTC7 homologQ96ES6MFSD39Major facilitator superfamily domain-containing protein 35proton transport [GO:0015992]; transport [GO:0006810]-solute:proton symporter activity [GO:0015295]P46379BAG6Large proline-rich protein BAG6SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=The C-terminal fragment generated by caspase-3 is cytoplasmic. Also found in extracellular vesicular exosomes in some tumor cells.brain development [GO:0007420]; cell differentiation [GO:0030154]; chromatin modification [GO:0016568]; embryo development [GO:0009790]; immune system process [GO:0002376]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; lung development [GO:0030324]; maintenance of unfolded protein involved in ERAD pathway [GO:1904378]; negative regulation of apoptotic process [GO:0043066]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of proteolysis [GO:0045861]; protein localization to cytosolic proteasome complex involved in ERAD pathway [GO:1904379]; protein stabilization [GO:0050821]; regulation of cell proliferation [GO:0042127]; regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903069]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; transport [GO:0006810]; ubiquitin-dependent protein c< atabolic process [GO:0006511]misfolded protein binding [GO:0051787]; polyubiquitin binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease binding [GO:1990381]BAT3 complex [GO:0071818]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]. FUNCTION: Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. Moreover, it regulates the stability and the degradation of proteins by the proteasome. For instance, it is required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. It is also involved in ubiquitin-mediated proteasomal degradation of proteins of the secretory pathway that are mislocalized to the cytosol. Binds the mislocalized proteins, preventing their aggregation in the cytosol, and promotes their ubiquitination. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. {ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:24981174}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}.; FUNCTION: Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cells (NK) activation and cytotoxicity. {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.O95260ATE1#Arginyl-tRNA--protein transferase 1SUBCELLULAR LOCATION: Isoform ATE1-1: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform ATE1-2: Cytoplasm {ECO:0000250}.!protein arginylation [GO:0016598](arginyltransferase activity [GO:0004057]FUNCTION: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). {ECO:0000250}.Q96G75RMD5BProtein RMD5 homolog BQ3SY69AL1L25Mitochondrial 10-formyltetrahydrofolate dehydrogenaseBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20498374}.10-formyltetrahydrofolate catabolic process [GO:0009258]; biosynthetic process [GO:0009058]; one-carbon metabolic process [GO:0006730]aldehyde dehydrogenase (NAD) activity [GO:0004029]; formyltetrahydrofolate dehydrogenase activity [GO:0016155]; hydroxymethyl-, formyl- and related transferase activity [GO:0016742]; methyltransferase activity [GO:0008168]O60568PLOD31Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3basement membrane assembly [GO:0070831]; cellular protein modification process [GO:0006464]; cellular response to hormone stimulus [GO:0032870]; collagen fibril organization [GO:0030199]; endothelial cell morphogenesis [GO:0001886]; epidermis morphogenesis [GO:0048730]; extracellular matrix organization [GO:0030198]; in utero embryonic development [GO:0001701]; lung morphogenesis [GO:0060425]; neural tube development [GO:0021915]; protein localization [GO:0008104]; vasodilation [GO:0042311]iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen galactosyltransferase activity [GO:0050211]; procollagen glucosyltransferase activity [GO:0033823]; procollagen-lysine 5-dioxygenase activity [GO:0008475]Q6P1L5F117BProtein FAM117BQ63HN8RN213"E3 ubiquitin-protein ligase RNF213>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21799892}.Lprotein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]ATPase activity [GO:0016887]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]Ecytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]vFUNCTION: Probable E3 ubiquitin-protein ligase that may play a role in angiogenesis. May also have an ATPase activity.P53582MAP11Methionine aminopeptidase 1BSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}.N-terminal protein amino acid modification [GO:0031365]; peptidyl-methionine modification [GO:0018206]; phototransduction, visible light [GO:0007603]; platelet aggregation [GO:0070527]; protein initiator methionine removal [GO:0070084]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; regulation of translation [GO:0006417]; rhodopsin mediated signaling pathway [GO:0016056]aminopeptidase activity [GO:0004177]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235]ccytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; nucleus [GO:0005634]FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:17114291}.O95363SYFM)Phenylalanine--tRNA ligase, mitochondrialgene expression [GO:0010467]; phenylalanyl-tRNA aminoacylation [GO:0006432]; tRNA aminoacylation for protein translation [GO:0006418]; tRNA processing [GO:0008033]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049]FUNCTION: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins. {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}.Q9Y2E4DIP2C%Disco-interacting protein 2 homolog CP51151RAB9ARas-related protein Rab-9ASUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}. Late endosome. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, phagosome. Note=Colocalizes with OSBPL1A at the late endosome. Recruited to phagosomes containing S.aureus or M.tuberculosis.:intracellular protein transport [GO:0006886]; negative regulation by host of symbiont molecular function [GO:0052405]; positive regulati< on of exocytosis [GO:0045921]; Rab protein signal transduction [GO:0032482]; regulation of protein localization [GO:0032880]; retrograde transport, endosome to Golgi [GO:0042147]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; late endosome [GO:0005770]; lysosome [GO:0005764]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]bFUNCTION: Involved in the transport of proteins between the endosomes and the trans Golgi network.Q6A1A2PDPK26Putative 3-phosphoinositide-dependent protein kinase 2FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development (By similarity). {ECO:0000250}.Q99615DNJC7!DnaJ homolog subfamily C member 7~SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Note=Colocalizes with NR1I3 to microtubules. {ECO:0000250}.cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0070389]; protein folding [GO:0006457]; regulation of cellular response to heat [GO:1900034]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). {ECO:0000250}.Q99871HAUS7"HAUS augmin-like complex subunit 7SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules.cell division [GO:0051301]; centrosome organization [GO:0051297]; mitotic nuclear division [GO:0007067]; spindle assembly [GO:0051225]!thioesterase binding [GO:0031996]centrosome [GO:0005813]; cytoplasm [GO:0005737]; HAUS complex [GO:0070652]; microtubule [GO:0005874]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; spindle [GO:0005819]FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.Q151722A5AOSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoformYSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8703017}. Nucleus {ECO:0000269|PubMed:8703017}. Chromosome, centromere {ECO:0000269|PubMed:16541025}. Note=From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase. {ECO:0000269|PubMed:16541025}.9negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; negative regulation of lipid kinase activity [GO:0090219]; positive regulation of protein dephosphorylation [GO:0035307]; regulation of protein phosphatase type 2A activity [GO:0034047]; signal transduction [GO:0007165]Xkinase binding [GO:0019900]; protein phosphatase type 2A regulator activity [GO:0008601]chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; M band [GO:0031430]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]; Z disc [GO:0030018]O95864FADS2Fatty acid desaturase 2alpha-Linolenic acid metabolismalpha-linolenic acid metabolic process [GO:0036109]; linoleic acid metabolic process [GO:0043651]; small molecule metabolic process [GO:0044281]; unsaturated fatty acid biosynthetic process [GO:0006636]; unsaturated fatty acid metabolic process [GO:0033559]vendoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]FUNCTION: Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum. {ECO:0000269|PubMed:12713571, ECO:0000269|PubMed:9867867}.Q9ULE0WWC3 Protein WWC3P62310LSM3(U6 snRNA-associated Sm-like protein LSm31exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]Ucatalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleus [GO:0005634]DFUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.O43395PRPF3*U4/U6 small nuclear ribonucleoprotein Prp3QSUBCELLULAR LOCATION: Nucleus speckle. Note=Colocalizes with spliceosomal snRNPs.mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]FUNCTION: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889, ECO:0000303|PubMed:20595234}.Q15032R3HD1R3H domain-containing protein 1Q6EMK4VASNVasorinSUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:15247411}; Single-pass type I membrane protein {ECO:0000305|PubMed:15247411}. Secreted {ECO:0000269|PubMed:15247411}.cellular response to hypoxia [GO:0071456]; cellular response to redox state [GO:0071461]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]4transforming growth factor beta binding [GO:0050431]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]WFUNCTION: May act as an inhibitor of TGF-beta signaling. {ECO:0000269|PubMed:15247411}.Q96JB2COG3,Conserved oligomeric Golgi complex subunit 3SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11292827}; Peripheral membrane protein {ECO:0000269|PubMed:11292827}. Note=Associated with the peripheral membrane of cis/medial cisternae.ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein glycosylation [GO:0006486]; protein localization to organelle [GO:0033365]; protein stabilization [GO:0050821]; retrograde transport, vesicle recycling within Golgi [GO:0000301]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi transport complex [GO:0017119]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]HFUNCTION: Involved in ER-Golgi transport. {ECO:0000269|P< ubMed:11929878}.Q96P50ACAP3GArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 3ZFUNCTION: GTPase-activating protein for the ADP ribosylation factor family. {ECO:0000305}.Q96PE2ARHGH)Rho guanine nucleotide exchange factor 17actin cytoskeleton organization [GO:0030036]; apoptotic signaling pathway [GO:0097190]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]tguanyl-nucleotide exchange factor activity [GO:0005085]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]kFUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. {ECO:0000269|PubMed:12071859}.Q92989CLP1*Polyribonucleotide 5'-hydroxyl-kinase Clp1zSUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035, ECO:0000269|PubMed:11060040, ECO:0000269|PubMed:24766810}.Dcerebellar cortex development [GO:0021695]; gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA cleavage [GO:0006379]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; siRNA loading onto RISC involved in RNA interference [GO:0035087]; targeting of mRNA for destruction involved in RNA interference [GO:0030423]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]ATP binding [GO:0005524]; ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity [GO:0046404]; ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity [GO:0051736]; polydeoxyribonucleotide kinase activity [GO:0051733]cytoplasm [GO:0005737]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; tRNA-intron endonuclease complex [GO:0000214]FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA (PubMed:24766809, PubMed:24766810). Its role in tRNA splicing and maturation is required for cerebellar development (PubMed:24766809, PubMed:24766810). Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing. {ECO:0000269|PubMed:17495927, ECO:0000269|PubMed:18648070, ECO:0000269|PubMed:24766809, ECO:0000269|PubMed:24766810}.Q9NPF5DMAP1,DNA methyltransferase 1-associated protein 1hSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Targeted to replication foci throughout S phase by DNMT1.chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA methylation [GO:0006306]; DNA repair [GO:0006281]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription factor import into nucleus [GO:0042993]; regulation of growth [GO:0040008]; response to ethanol [GO:0045471]; transcription, DNA-templated [GO:0006351]wRNA polymerase II repressing transcription factor binding [GO:0001103]; transcription corepressor activity [GO:0003714]cytoplasm [GO:0005737]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]FUNCTION: Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity. {ECO:0000269|PubMed:14665632, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102, ECO:0000269|PubMed:15367675}.P55081MFAP1#Microfibrillar-associated protein 1;extracellular region [GO:0005576]; microfibril [GO:0001527];FUNCTION: Component of the elastin-associated microfibrils.Q13057COASY Bifunctional coenzyme A synthaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix {ECO:0000269|PubMed:24360804}. Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate.ATP binding [GO:0005524]; dephospho-CoA kinase activity [GO:0004140]; pantetheine-phosphate adenylyltransferase activity [GO:0004595]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. {ECO:0000269|PubMed:11923312}.Q8TCG1CIP2A Protein CIP2ASUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12118381}. Note=Slightly concentrates in the perinuclear region.epositive regulation of neural precursor cell proliferation [GO:2000179]; spermatogenesis [GO:0007283]acytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Oncoprotein that inhibits PP2A and stabilizes MYC in human malignancies. Promotes anchorage-independent cell growth and tumor formation. {ECO:0000269|PubMed:17632056}.Q8IYB7DI3L2DIS3-like exonuclease 2QSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24141620}. Cytoplasm, P-body.cell division [GO:0051301]; miRNA catabolic process [GO:0010587]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid separation [GO:0051306]; negative regulation of cell proliferation [GO:0008285]; nuclear-transcribed mRNA catabolic process, exonucleolytic [GO:0000291]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyuridylation-dependent mRNA catabolic process [GO:1990< 074]; RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; stem cell maintenance [GO:0019827]3'-5'-exoribonuclease activity [GO:0000175]; magnesium ion binding [GO:0000287]; poly(U) RNA binding [GO:0008266]; ribonuclease activity [GO:0004540]cytoplasm [GO:0005737]; cytoplasmic exosome (RNase complex) [GO:0000177]; cytoplasmic mRNA processing body [GO:0000932]; nuclear exosome (RNase complex) [GO:0000176]; polysome [GO:0005844]FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation. {ECO:0000255|HAMAP-Rule:MF_03045, ECO:0000269|PubMed:23756462, ECO:0000269|PubMed:24141620}.Q96HE7ERO1AERO1-like protein alphanSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Peripheral membrane protein {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}; Lumenal side {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:14517240}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum. 4-hydroxyproline metabolic process [GO:0019471]; brown fat cell differentiation [GO:0050873]; cell redox homeostasis [GO:0045454]; cellular protein metabolic process [GO:0044267]; cellular protein modification process [GO:0006464]; chaperone mediated protein folding requiring cofactor [GO:0051085]; endoplasmic reticulum unfolded protein response [GO:0030968]; extracellular matrix organization [GO:0030198]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; protein folding [GO:0006457]; protein maturation by protein folding [GO:0022417]; release of sequestered calcium ion into cytosol [GO:0051209]; response to endoplasmic reticulum stress [GO:0034976]; response to reactive oxygen species [GO:0000302]; response to temperature stimulus [GO:0009266]oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; protein disulfide isomerase activity [GO:0003756]; protein disulfide oxidoreductase activity [GO:0015035]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]FUNCTION: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. {ECO:0000269|PubMed:10671517, ECO:0000269|PubMed:10970843, ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:12403808, ECO:0000269|PubMed:18833192, ECO:0000269|PubMed:18971943, ECO:0000269|PubMed:23027870}.Q93088BHMT1+Betaine--homocysteine S-methyltransferase 1amino-acid betaine catabolic process [GO:0006579]; amino-acid betaine metabolic process [GO:0006577]; cellular nitrogen compound metabolic process [GO:0034641]; L-methionine salvage [GO:0071267]; protein methylation [GO:0006479]; regulation of homocysteine metabolic process [GO:0050666]; small molecule metabolic process [GO:0044281]; S-methylmethionine cycle [GO:0033528]; sulfur amino acid metabolic process [GO:0000096]betaine-homocysteine S-methyltransferase activity [GO:0047150]; S-adenosylmethionine-homocysteine S-methyltransferase activity [GO:0008898]; zinc ion binding [GO:0008270]FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.Q13277STX3 Syntaxin-3-exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; long-term synaptic potentiation [GO:0060291]; neuron projection development [GO:0031175]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of protein localization to plasma membrane [GO:1903078]; synaptic vesicle fusion to presynaptic membrane [GO:0031629]; vesicle docking [GO:0048278]farachidonic acid binding [GO:0050544]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]apical plasma membrane [GO:0016324]; azurophil granule [GO:0042582]; cell-cell junction [GO:0005911]; dendrite [GO:0030425]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; integral component of membrane [GO:0016021]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; specific granule [GO:0042581]; synaptic vesicle [GO:0008021]; vacuole [GO:0005773][FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones.Q9BUN8DERL1Derlin-1<SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}; Multi-pass membrane protein {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189}.endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; ER-associated misfolded protein catabolic process [GO:0071712]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; establishment of protein localization [GO:0045184]; intracellular transport of viral protein in host cell [GO:0019060]; positive regulation of protein binding [GO:0032092]; positive regulation of protein ubiquitination [GO:0031398]; protein destabilization [GO:0031648]; protein homooligomerization [GO:0051260]; response to unfolded protein [GO:0006986]; retrograde protein transport, ER to cytosol [GO:0030970]ATPase binding [GO:0051117]; MHC class I protein binding [GO:0042288]; protease binding [GO:0002020]; receptor activity [GO:0004872]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease binding [GO:1990381]KDerlin-1-VIMP complex [GO:0036502]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; host cell [GO:0043657]; Hrd1p ubiquitin ligase complex [GO:0000836]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; membrane [GO:0016020]FUNCTION: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains.< Also participates in the degradation process of misfolded cytomegalovirus US2 protein. {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:15215856}.P29120NEC1Neuroendocrine convertase 1gSUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Note=Localized in the secretion granules..cell-cell signaling [GO:0007267]; cellular protein metabolic process [GO:0044267]; metabolic process [GO:0008152]; peptide biosynthetic process [GO:0043043]; peptide hormone processing [GO:0016486]; protein processing [GO:0016485]; proteolysis [GO:0006508]; regulation of insulin secretion [GO:0050796]fextracellular space [GO:0005615]; secretory granule lumen [GO:0034774]; transport vesicle [GO:0030133]FUNCTION: Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin.P21359NF1 NeurofibrominnSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14988005}. Nucleus, nucleolus {ECO:0000269|PubMed:14988005}. actin cytoskeleton organization [GO:0030036]; adrenal gland development [GO:0030325]; artery morphogenesis [GO:0048844]; brain development [GO:0007420]; camera-type eye morphogenesis [GO:0048593]; cell communication [GO:0007154]; cellular response to heat [GO:0034605]; cerebral cortex development [GO:0021987]; cognition [GO:0050890]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; forebrain astrocyte development [GO:0021897]; forebrain morphogenesis [GO:0048853]; heart development [GO:0007507]; liver development [GO:0001889]; MAPK cascade [GO:0000165]; metanephros development [GO:0001656]; myelination in peripheral nervous system [GO:0022011]; negative regulation of angiogenesis [GO:0016525]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cell migration [GO:0030336]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of neurotransmitter secretion [GO:0046929]; negative regulation of oligodendrocyte differentiation [GO:0048715]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of Rac protein signal transduction [GO:0035021]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of transcription factor import into nucleus [GO:0042992]; neural tube development [GO:0021915]; osteoblast differentiation [GO:0001649]; peripheral nervous system development [GO:0007422]; phosphatidylinositol 3-kinase signaling [GO:0014065]; pigmentation [GO:0043473]; positive regulation of adenylate cyclase activity [GO:0045762]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron apoptotic process [GO:0043525]; Ras protein signal transduction [GO:0007265]; regulation of angiogenesis [GO:0045765]; regulation of blood vessel endothelial cell migration [GO:0043535]; regulation of bone resorption [GO:0045124]; regulation of cell-matrix adhesion [GO:0001952]; regulation of glial cell differentiation [GO:0045685]; regulation of GTPase activity [GO:0043087]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of synaptic transmission, GABAergic [GO:0032228]; response to hypoxia [GO:0001666]; Schwann cell development [GO:0014044]; skeletal muscle tissue development [GO:0007519]; smooth muscle tissue development [GO:0048745]; spinal cord development [GO:0021510]; sympathetic nervous system development [GO:0048485]; visual learning [GO:0008542]; wound healing [GO:0042060]GTPase activator activity [GO:0005096]; phosphatidylcholine binding [GO:0031210]; phosphatidylethanolamine binding [GO:0008429]axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity. {ECO:0000269|PubMed:2121371, ECO:0000269|PubMed:8417346}.P13010XRCC5*X-ray repair cross-complementing protein 5>SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome.cell proliferation [GO:0008283]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of integrated proviral latency [GO:0075713]; hematopoietic stem cell differentiation [GO:0060218]; innate immune response [GO:0045087]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of neurogenesis [GO:0050769]; positive regulation of type I interferon production [GO:0032481]; regulation of smooth muscle cell proliferation [GO:0048660]; telomere maintenance [GO:0000723]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]; telomeric DNA binding [GO:0042162]; transcription regulatory region DNA binding [GO:0044212]; ubiquitin protein ligase binding [GO:0031625]?cytosol [GO:0005829]; Ku70:Ku80 complex [GO:0043564]; membrane [GO:0016020]; nonhomologous end joining complex [GO:0070419]; nuclear chromosome, telomeric region [GO:0000784]; nuclear telomere cap complex [GO:0000783]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. {ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:20383123, ECO:0000269|PubMed:7957065, ECO:0000269|PubMed:8621488}.O75843AP1G2!AP-1 complex subunit gamma-like 2SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Endosome membrane< ; Peripheral membrane protein. Note=Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures.intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; vesicle-mediated transport [GO:0016192]; viral process [GO:0016032]AP-1 adaptor complex [GO:0030121]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; transport vesicle [GO:0030133]FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982, ECO:0000269|PubMed:17553870, ECO:0000269|PubMed:9733768}.Q15276RABE1%Rab GTPase-binding effector protein 1YSUBCELLULAR LOCATION: Cytoplasm. Early endosome. Recycling endosome. Cytoplasmic vesicle.apoptotic process [GO:0006915]; endocytosis [GO:0006897]; membrane fusion [GO:0061025]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]VGTPase activator activity [GO:0005096]; protein homodimerization activity [GO:0042803]early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231]; recycling endosome [GO:0055037]FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane (PubMed:22841712). Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. {ECO:0000269|PubMed:10698684, ECO:0000269|PubMed:11452015, ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:8521472}.P09488GSTM1Glutathione S-transferase Mu 1Qcellular detoxification of nitrogen compound [GO:0070458]; glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; nitrobenzene metabolic process [GO:0018916]; small molecule metabolic process [GO:0044281]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]enzyme binding [GO:0019899]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; protein homodimerization activity [GO:0042803]FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:16548513}.Q7KZI7MARK2%Serine/threonine-protein kinase MARK2SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm. Lateral cell membrane. Cytoplasm, cytoskeleton. Note=Phosphorylation at Thr-596 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm.activation of protein kinase activity [GO:0032147]; establishment of cell polarity [GO:0030010]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; intracellular signal transduction [GO:0035556]; mitochondrion degradation [GO:0000422]; mitochondrion localization [GO:0051646]; neuron migration [GO:0001764]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of neuron projection development [GO:0010976]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of axonogenesis [GO:0050770]; regulation of cytoskeleton organization [GO:0051493]; Wnt signaling pathway [GO:0016055] ATP binding [GO:0005524]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]actin filament [GO:0005884]; basal cortex [GO:0045180]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microtubule bundle [GO:0097427]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU, and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000269|PubMed:11433294, ECO:0000269|PubMed:12429843, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15158914, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:15365179, ECO:0000269|PubMed:16775013, ECO:0000269|PubMed:16980613, ECO:0000269|PubMed:18626018, ECO:0000269|PubMed:20194617}.Q9HAV0GBB41Guanine nucleotide-binding protein subunit beta-4cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; small molecule metabolic process [GO:0044281]; substantia nigra development [GO:0021762]Mprotein complex binding [GO:0032403]; signal transducer activity [GO:0004871]}extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]Q8N465D2HDH1D-2-hydroxyglutarate dehydrogenase, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:15070399}.&2-oxoglutarate metabolic process [GO:0006103]; cellular metabolic process [GO:0044237]; cellular protein metabolic process [GO:0044267]; response to cobalt ion [GO:0032025]; response to manganese ion [GO:0010042]; response to zinc ion [GO:0010043]; small molecule metabolic process [GO:0044281](R)-2-hydroxyglutarate dehydrogenase activity [GO:0051990]; flavin adenine dinucleotide binding [GO:0050660]; UDP-N-acetylmuramate dehydrogenase activity [GO:0008762]pFUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate. {ECO:0000269|PubMed:15070399}.Q9Y4I1MYO5AUnconventional myosin-Vaactin filament-based movement [GO:0030048]; cellular protein metabolic process [GO:0044267]; cellular response to insulin stimulus [GO:0032869]; endoplasmic reticulum localization [GO:0051643]; exocytosis [GO:0006887]; insulin secretion [GO:0030073]; locomotion involved in locomotory behavior [GO:0031987]; long-chain fatty acid biosynthetic process [GO:0042759]; melanin biosynthetic process [GO:0042438]; melanocyte differentiation [GO:0030318]; melanosome transport [GO:0032402]; membrane organization [GO:0061024]; myelination [GO:0042552]; odontogenesis [GO:0042476]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization to plasma membrane [GO:0072659]; regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0031585]; secretory granule localization [GO:0032252]; synapse organization [GO:0050808]; synaptic transmission [GO:0007268]; transport [GO:0006810]; vesicle-mediated transport [GO:0016192]; vesicle transport along actin filament [GO:0030050]; visual< perception [GO:0007601]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; microfilament motor activity [GO:0000146]; poly(A) RNA binding [GO:0044822]; Rab GTPase binding [GO:0017137]actomyosin [GO:0042641]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filopodium tip [GO:0032433]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; insulin-responsive compartment [GO:0032593]; intermediate filament [GO:0005882]; melanosome [GO:0042470]; membrane [GO:0016020]; microtubule plus-end [GO:0035371]; myosin complex [GO:0016459]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; photoreceptor outer segment [GO:0001750]; ruffle [GO:0001726]TFUNCTION: Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation. {ECO:0000269|PubMed:10448864}.O43175SERA"D-3-phosphoglycerate dehydrogenasebrain development [GO:0007420]; cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; G1 to G0 transition [GO:0070314]; gamma-aminobutyric acid metabolic process [GO:0009448]; glial cell development [GO:0021782]; glutamine metabolic process [GO:0006541]; glycine metabolic process [GO:0006544]; L-serine biosynthetic process [GO:0006564]; neural tube development [GO:0021915]; neuron projection development [GO:0031175]; regulation of gene expression [GO:0010468]; small molecule metabolic process [GO:0044281]; spinal cord development [GO:0021510]; taurine metabolic process [GO:0019530]; threonine metabolic process [GO:0006566]velectron carrier activity [GO:0009055]; NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]Tcytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]Q12904AIMP1EAminoacyl tRNA synthase complex-interacting multifunctional protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (By similarity). Also secreted in response to hypoxia and both apoptotic and necrotic cell death. {ECO:0000250}.angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; chemotaxis [GO:0006935]; defense response to virus [GO:0051607]; gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; inflammatory response [GO:0006954]; leukocyte migration [GO:0050900]; negative regulation of endothelial cell proliferation [GO:0001937]; response to wounding [GO:0009611]; signal transduction [GO:0007165]; tRNA aminoacylation for protein translation [GO:0006418]cytokine activity [GO:0005125]; GTPase binding [GO:0051020]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]4aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]; transport vesicle [GO:0030133]FUNCTION: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7. {ECO:0000269|PubMed:10358004, ECO:0000269|PubMed:11157763, ECO:0000269|PubMed:11306575, ECO:0000269|PubMed:11818442, ECO:0000269|PubMed:12237313, ECO:0000269|PubMed:19362550}.Q3LXA3DHAKLBifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; cellular carbohydrate metabolic process [GO:0044262]; fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate [GO:0061624]; fructose metabolic process [GO:0006000]; glycerol metabolic process [GO:0006071]; innate immune response [GO:0045087]; negative regulation of MDA-5 signaling pathway [GO:0039534]; regulation of innate immune response [GO:0045088]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; FAD-AMP lyase (cyclizing) activity [GO:0034012]; glycerone kinase activity [GO:0004371]; metal ion binding [GO:0046872]; triokinase activity [GO:0050354]FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (PubMed:17600090). {ECO:0000250|UniProtKB:F1RKQ4, ECO:0000250|UniProtKB:Q4KLZ6, ECO:0000269|PubMed:16289032, ECO:0000269|PubMed:17600090, ECO:0000269|PubMed:4688871}.Q9NYL9TMOD3Tropomodulin-3 actin filament organization [GO:0007015]; erythrocyte development [GO:0048821]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; positive regulation of mitotic cell cycle phase transition [GO:1901992]]cytoskeleton [GO:0005856]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}.O95197RTN3 Reticulon-3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.apoptotic process [GO:0006915]; endoplasmic reticulum tubular network organization [GO:0071786]; vesicle-mediated transport [GO:0016192]; viral process [GO:0016032]endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. In case of enteroviruses infection, RTN3 may be involved in the viral replication or pathogenesis. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123}.Q9NSD9SYFB'Phenylalanine--tRNA ligase beta subunitgene expression [GO:0010467]; phenylalanyl-tRNA aminoacylation [GO:0006432]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; RNA binding [GO:0003723]scytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; phenylalanine-tRNA ligase complex [GO:0009328]Q14534ERG1Squalene monooxygenaseSUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.cellular aromatic compound metabolic process [GO:0< 006725]; cholesterol biosynthetic process [GO:0006695]; response to organic substance [GO:0010033]; small molecule metabolic process [GO:0044281]; sterol biosynthetic process [GO:0016126]^flavin adenine dinucleotide binding [GO:0050660]; squalene monooxygenase activity [GO:0004506]FUNCTION: Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.O75150BRE1B!E3 ubiquitin-protein ligase BRE1B<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10944455}.histone H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; negative regulation of mRNA polyadenylation [GO:1900364]; positive regulation of histone H2B ubiquitination [GO:2001168]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein polyubiquitination [GO:1902916]; response to peptide hormone [GO:0043434]; ubiquitin-dependent protein catabolic process [GO:0006511]ligase activity [GO:0016874]; mRNA 3'-UTR binding [GO:0003730]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]axon terminus [GO:0043679]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; HULC complex [GO:0033503]; membrane [GO:0016020]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543}.P04114APOBApolipoprotein B-100fSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22580899}. Secreted {ECO:0000269|PubMed:22580899}.qartery morphogenesis [GO:0048844]; blood coagulation [GO:0007596]; cellular response to prostaglandin stimulus [GO:0071379]; cellular response to tumor necrosis factor [GO:0071356]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; fertilization [GO:0009566]; in utero embryonic development [GO:0001701]; leukocyte migration [GO:0050900]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; low-density lipoprotein particle clearance [GO:0034383]; low-density lipoprotein particle remodeling [GO:0034374]; nervous system development [GO:0007399]; phototransduction, visible light [GO:0007603]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of gene expression [GO:0010628]; positive regulation of lipid storage [GO:0010884]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; post-embryonic development [GO:0009791]; receptor-mediated endocytosis [GO:0006898]; regulation of cholesterol biosynthetic process [GO:0045540]; response to carbohydrate [GO:0009743]; response to lipopolysaccharide [GO:0032496]; response to selenium ion [GO:0010269]; response to virus [GO:0009615]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; sperm motility [GO:0030317]; triglyceride catabolic process [GO:0019433]; triglyceride mobilization [GO:0006642]; very-low-density lipoprotein particle assembly [GO:0034379]cholesterol transporter activity [GO:0017127]; heparin binding [GO:0008201]; lipase binding [GO:0035473]; low-density lipoprotein particle receptor binding [GO:0050750]; phospholipid binding [GO:0005543]Ractin cytoskeleton [GO:0015629]; chylomicron [GO:0042627]; chylomicron remnant [GO:0034360]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; intermediate-density lipoprotein particle [GO:0034363]; intracellular membrane-bounded organelle [GO:0043231]; low-density lipoprotein particle [GO:0034362]; mature chylomicron [GO:0034359]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.Q8N954GPT11$G patch domain-containing protein 11!nucleic acid binding [GO:0003676]Q15102PA1B3;Platelet-activating factor acetylhydrolase IB subunit gammabrain development [GO:0007420]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; nervous system development [GO:0007399]; spermatogenesis [GO:0007283]1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; identical protein binding [GO:0042802]; platelet-activating factor acetyltransferase activity [GO:0047179]FUNCTION: Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.Q12791KCMA13Calcium-activated potassium channel subunit alpha-1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288}; Multi-pass membrane protein {ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288}.Oadult walking behavior [GO:0007628]; auditory receptor cell differentiation [GO:0042491]; blood coagulation [GO:0007596]; cell maturation [GO:0048469]; cellular potassium ion homeostasis [GO:0030007]; eye blink reflex [GO:0060082]; locomotor rhythm [GO:0045475]; micturition [GO:0060073]; negative regulation of cell volume [GO:0045794]; neuromuscular process controlling balance [GO:0050885]; neuronal action potential [GO:0019228]; positive regulation of apoptotic process [GO:0043065]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of aldosterone metabolic process [GO:0032344]; regulation of membrane potential [GO:0042391]; relaxation of vascular smooth muscle [GO:0060087]; response to calcium ion [GO:0051592]; response to carbon monoxide [GO:0034465]; response to hypoxia [GO:0001666]; response to osmotic stress [GO:0006970]; saliva secretion [GO:0046541]; sensory perception of sound [GO:0007605]; smooth muscle contraction involved in micturition [GO:0060083]; synaptic transmission [GO:0007268]actin binding [GO:0003779]; calcium-activated potassium channel activity [GO:0015269]; large conductance calcium-activated potassium channel activity [GO:0060072]; metal ion binding [GO:0046872]; voltage-gated potassium channel activity [GO:0005249]sapical plasma membrane [GO:0016324]; caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; terminal bouton [GO:0043195]; voltage-gated potassium channel complex [GO:0008076]yFUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory ev< ents that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).Q9NV06DCA13#DDB1- and CUL4-associated factor 13SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24754225}. Note=In the nucleolus, localizes predominantly in the granular component, but also detected in the fibrillar center and dense fibrillar component. {ECO:0000269|PubMed:24754225}.maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; protein ubiquitination [GO:0016567]qCul4-RING E3 ubiquitin ligase complex [GO:0080008]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]FUNCTION: Possible role in ribosomal RNA processing (By similarity). May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250, ECO:0000269|PubMed:16949367}.O15121DEGS1%Sphingolipid delta(4)-desaturase DES1aSUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum membrane; Multi-pass membrane protein.small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; unsaturated fatty acid biosynthetic process [GO:0006636]]electron carrier activity [GO:0009055]; sphingolipid delta-4 desaturase activity [GO:0042284]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; mitochondrion [GO:0005739]FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). {ECO:0000269|PubMed:11937514}.Q8N350DOS Protein DosP62306RUXF!Small nuclear ribonucleoprotein Factivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; gene expression [GO:0010467]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; RNA splicing [GO:0008380]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; pICln-Sm protein complex [GO:0034715]; small nuclear ribonucleoprotein complex [GO:0030532]; small nucleolar ribonucleoprotein complex [GO:0005732]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U4 snRNP [GO:0005687]; U7 snRNP [GO:0005683]9FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}.Q14683SMC1A0Structural maintenance of chromosomes protein 1ASUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12199140}. Chromosome {ECO:0000269|PubMed:12199140}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12199140}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function. Integral component of the functional centromere-kinetochore complex at the kinetochore region during mitosis. cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; DNA repair [GO:0006281]; gene expression [GO:0010467]; meiotic nuclear division [GO:0007126]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic sister chromatid cohesion [GO:0007064]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle organization [GO:0007052]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of DNA endoreduplication [GO:0032876]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; response to radiation [GO:0009314]; RNA splicing [GO:0008380]; signal transduction in response to DNA damage [GO:0042770]; sister chromatid cohesion [GO:0007062]; stem cell maintenance [GO:0019827]ATP binding [GO:0005524]; chromatin binding [GO:0003682]; microtubule motor activity [GO:0003777]; poly(A) RNA binding [GO:0044822]; protein heterodimerization activity [GO:0046982]{chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cohesin core heterodimer [GO:0008280]; condensed chromosome kinetochore [GO:0000777]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; meiotic cohesin complex [GO:0030893]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269|PubMed:11877377}.O60812HNRC10Heterogeneous nuclear ribonucleoprotein C-like 1^SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of ribonucleosomes. {ECO:0000250}.{FUNCTION: May play a role in nucleosome assembly by neutralizing basic proteins such as A and B core hnRNPs. {ECO:0000250}.Q96NE9FRMD6 FERM domain-containing protein 6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16137681}. Cell membrane {ECO:0000269|PubMed:16137681}; Peripheral membrane protein {ECO:0000269|PubMed:16137681}; Cytoplasmic side {ECO:0000269|PubMed:16137681}. Note=Can colocalize with actin.apical constriction [GO:0003383]; cellular protein localization [GO:0034613]; regulation of actin filament-based process [GO:0032970]uapical junction complex [GO:0043296]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]Q9ULI3HEG1Protein HEG homolog 1SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Sing< le-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.cardiac atrium morphogenesis [GO:0003209]; cardiac muscle tissue growth [GO:0055017]; cell-cell junction assembly [GO:0007043]; endothelial cell morphogenesis [GO:0001886]; in utero embryonic development [GO:0001701]; lung development [GO:0030324]; lymph circulation [GO:0003017]; lymph vessel development [GO:0001945]; multicellular organism growth [GO:0035264]; pericardium development [GO:0060039]; positive regulation of fibroblast growth factor production [GO:0090271]; post-embryonic development [GO:0009791]; regulation of body fluid levels [GO:0050878]; vasculogenesis [GO:0001570]; venous blood vessel morphogenesis [GO:0048845]; ventricular septum development [GO:0003281]; ventricular trabecula myocardium morphogenesis [GO:0003222]cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]FUNCTION: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity May act through the stabilization of endothelial cell junctions. {ECO:0000250}.Q8N697S15A4!Solute carrier family 15 member 4ion transport [GO:0006811]; oligopeptide transport [GO:0006857]; protein transport [GO:0015031]; transmembrane transport [GO:0055085]symporter activity [GO:0015293]FUNCTION: Proton oligopeptide cotransporter. Transports free histidine and certain di- and tripeptides. {ECO:0000269|PubMed:16289537}.Q9UET6TRM7APutative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseBSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}.Ucytoplasmic translation [GO:0002181]; tRNA nucleoside ribose methylation [GO:0002128],tRNA methyltransferase activity [GO:0008175]FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000255|HAMAP-Rule:MF_03162}.Q12974TP4A2'Protein tyrosine phosphatase type IVA 2?SUBCELLULAR LOCATION: Cell membrane. Early endosome. Cytoplasm.0peptidyl-tyrosine dephosphorylation [GO:0035335]=prenylated protein tyrosine phosphatase activity [GO:0004727]ucytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB. {ECO:0000269|PubMed:14643450}.P19784CSK22Casein kinase II subunit alpha'apoptotic process [GO:0006915]; axon guidance [GO:0007411]; mitotic cell cycle [GO:0000278]; mitotic spindle checkpoint [GO:0071174]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of mitochondrion degradation [GO:1903146]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]xATP binding [GO:0005524]; protein N-terminus binding [GO:0047485]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. {ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064}.P36897TGFR1TGF-beta receptor type-1hSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, tight junction. activation of MAPKK activity [GO:0000186]; activin receptor signaling pathway [GO:0032924]; angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; apoptotic process [GO:0006915]; artery morphogenesis [GO:0048844]; blastocyst development [GO:0001824]; cardiac epithelial to mesenchymal transition [GO:0060317]; cell cycle arrest [GO:0007050]; cell motility [GO:0048870]; cellular response to transforming growth factor beta stimulus [GO:0071560]; collagen fibril organization [GO:0030199]; embryonic cranial skeleton morphogenesis [GO:0048701]; endothelial cell activation [GO:0042118]; endothelial cell migration [GO:0043542]; epithelial to mesenchymal transition [GO:0001837]; extracellular structure organization [GO:0043062]; germ cell migration [GO:0008354]; heart development [GO:0007507]; intracellular signal transduction [GO:0035556]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; lens development in camera-type eye [GO:0002088]; male gonad development [GO:0008584]; mesenchymal cell differentiation [GO:0048762]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neuron fate commitment [GO:0048663]; palate development [GO:0060021]; parathyroid gland development [GO:0060017]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; pharyngeal system development [GO:0060037]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell growth [GO:0030307]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular component movement [GO:0051272]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of gene expression [GO:0010628]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of SMAD protein import into nucleus [GO:0060391]; positive regulation of transcription, DNA-templated [GO:0045893]; post-embryonic development [GO:0009791]; protein phosphorylation [GO:0006468]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gene expression [GO:0010468]; regulation of protein binding [GO:0043393]; regulation of protein ubiquitination [GO:0031396]; regulation of transcription, DNA-templated [GO:0006355]; response to cholesterol [GO:0070723]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; skeletal system morphogenesis [GO:0048705]; thymus development [GO:0048538]; transforming growth factor beta receptor signaling pathway [GO:0007179]; wound healing [GO:0042060]XATP binding [GO:0005524]; I-SMAD < binding [GO:0070411]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; receptor signaling protein activity [GO:0005057]; receptor signaling protein serine/threonine kinase activity [GO:0004702]; SMAD binding [GO:0046332]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]; type II transforming growth factor beta receptor binding [GO:0005114] bicellular tight junction [GO:0005923]; cell [GO:0005623]; endosome [GO:0005768]; intracellular [GO:0005622]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; transforming growth factor beta receptor homodimeric complex [GO:0070022]FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation. {ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9346908}.Q8N442GUF1&Translation factor GUF1, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}.Ipositive regulation of translation [GO:0045727]; translation [GO:0006412]UGTPase activity [GO:0003924]; GTP binding [GO:0005525]; ribosome binding [GO:0043022],FUNCTION: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_03137}.Q8NEJ9NGDN NeuroguidinSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:18547334}. Chromosome, centromere {ECO:0000269|PubMed:18547334}. Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Note=Detected in axons, dendrites and filopodia. Colocalized with EIF4E in neurites (By similarity). Translocated from nucleolus to nuclear foci in response to UV damage. {ECO:0000250}.maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; regulation of translation [GO:0006417]axon [GO:0030424]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium [GO:0030175]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]FUNCTION: Involved in the translational repression of cytoplasmic polyadenylation element (CPE)-containing mRNAs. {ECO:0000250}.Q9HB07MYG1#UPF0160 protein MYG1, mitochondrialiSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19014353}. Mitochondrion {ECO:0000269|PubMed:19014353}.Glocomotory exploration behavior [GO:0035641]; pigmentation [GO:0043473]nextracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q92917GPKOW0G patch domain and KOW motifs-containing proteinQ9H553ALG2&Alpha-1,3/1,6-mannosyltransferase ALG2ccellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; protein glycosylation in endoplasmic reticulum [GO:0033577]; protein N-linked glycosylation via asparagine [GO:0018279]; response to calcium ion [GO:0051592]Lalpha-1,3-mannosyltransferase activity [GO:0000033]; calcium-dependent protein binding [GO:0048306]; GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity [GO:0004378]; glycolipid 6-alpha-mannosyltransferase activity [GO:0033164]; protein heterodimerization activity [GO:0046982]; protein N-terminus binding [GO:0047485]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. {ECO:0000269|PubMed:12684507}.P23919KTHYThymidylate kinaseqcell cycle [GO:0007049]; cell proliferation [GO:0008283]; cellular response to growth factor stimulus [GO:0071363]; dTDP biosynthetic process [GO:0006233]; dTTP biosynthetic process [GO:0006235]; dUDP biosynthetic process [GO:0006227]; myoblast differentiation [GO:0045445]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside monophosphate phosphorylation [GO:0046940]; nucleotide phosphorylation [GO:0046939]; response to cadmium ion [GO:0046686]; response to estrogen [GO:0043627]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; nucleoside phosphate kinase activity [GO:0050145]; thymidylate kinase activity [GO:0004798]; uridylate kinase activity [GO:0009041]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]3FUNCTION: Catalyzes the conversion of dTMP to dTDP.P19474RO52"E3 ubiquitin-protein ligase TRIM21SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus {ECO:0000269|PubMed:17156811}. Cytoplasm, P-body. Note=Enters the nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-like structures in the cytoplasm, called cytoplasmic bodies (P-body) that are located underneath the plasma membrane and also diffusely in the cytoplasm and are highly motil in cells. Cytoplasmic bodies are located along the microtubules and do not share the same cytoplasmic bodies with TRIM5. Colocalizes with DCP2 in P-body.cell cycle [GO:0007049]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein deubiquitination [GO:0090086]; negative regulation of viral release from host cell [GO:1902187]; negative regulation of viral transcription [GO:0032897]; positive regulation of cell cycle [GO:0045787]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of type I interferon production [GO:0032481]; positive regulation of viral entry into host cell [GO:0046598]; protein autoubiquitination [GO:0051865]; protein destabilization [GO:0031648]; protein monoubiquitination [GO:0006513]; protein polyubiq< uitination [GO:0000209]; protein trimerization [GO:0070206]; protein ubiquitination [GO:0016567]; regulation of type I interferon production [GO:0032479]DNA binding [GO:0003677]; identical protein binding [GO:0042802]; ligase activity [GO:0016874]; RNA binding [GO:0003723]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529] FUNCTION: E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. {ECO:0000269|PubMed:16297862, ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18022694, ECO:0000269|PubMed:18361920, ECO:0000269|PubMed:18641315, ECO:0000269|PubMed:18845142, ECO:0000269|PubMed:19675099}.Q9BVM2DPCD Protein DPCDdetermination of left/right symmetry [GO:0007368]; epithelial cilium movement [GO:0003351]; lateral ventricle development [GO:0021670]; left/right pattern formation [GO:0060972]; spermatogenesis [GO:0007283]; sperm motility [GO:0030317]; third ventricle development [GO:0021678]hFUNCTION: May play a role in the formation or function of ciliated cells. {ECO:0000269|PubMed:14630615}.Q8NBI6XXLT1Xyloside xylosyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22117070}; Single-pass type II membrane protein {ECO:0000269|PubMed:22117070}.?transferase activity, transferring pentosyl groups [GO:0016763]FUNCTION: Alpha-1,3-xylosyltransferase, which elongates the O-linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of the second xylose. {ECO:0000269|PubMed:22117070}.Q9Y2S2CRYL1Lambda-crystallin homolog3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD+ binding [GO:0070403]; protein homodimerization activity [GO:0042803]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q9NZ63CI078Uncharacterized protein C9orf78Q6P1M0S27A4)Long-chain fatty acid transport protein 4SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250}.fatty acid transport [GO:0015908]; lipid metabolic process [GO:0006629]; long-chain fatty acid import [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty acid transport [GO:0015909]; medium-chain fatty acid transport [GO:0001579]; response to nutrient [GO:0007584]; skin development [GO:0043588]; transmembrane transport [GO:0055085]; transport [GO:0006810]; very long-chain fatty acid catabolic process [GO:0042760]fatty acid transporter activity [GO:0015245]; long-chain fatty acid-CoA ligase activity [GO:0004467]; nucleotide binding [GO:0000166]; very long-chain fatty acid-CoA ligase activity [GO:0031957]brush border membrane [GO:0031526]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]>FUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (VLCFAs). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity). {ECO:0000250}.Q9NPF4OSGEP7Probable tRNA N6-adenosine threonylcarbamoyltransferaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:22912744}.Umetal ion binding [GO:0046872]; N(6)-L-threonylcarbamoyladenine synthase [GO:0061711]Lcytoplasm [GO:0005737]; EKC/KEOPS complex [GO:0000408]; nucleus [GO:0005634]FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-Rule:MF_03180}.P17028ZNF24Zinc finger protein 24bSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:24224020}.myelination [GO:0042552]; negative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]FUNCTION: Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro. {ECO:0000250, ECO:0000269|PubMed:10585455}.Q15599NHRF2/Na(+)/H(+) exchange regulatory cofactor NHE-RF2SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:9054412}; Peripheral membrane protein {ECO:0000269|PubMed:9054412}. Nucleus {ECO:0000269|PubMed:9054412}. Apical cell membrane {ECO:0000250}. Note=Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes (By similarity). Nuclear, in a punctate pattern. {ECO:0000250}.inner ear development [GO:0048839]; positive regulation of membrane potential [GO:0045838]; protein complex assembly [GO:0006461]beta-catenin binding [GO:0008013]; channel regulator activity [GO:0016247]; phosphatase binding [GO:0019902]; protein C-terminus binding [GO:0008022]; receptor binding [GO:0005102]apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO< :0043234]FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3 (PubMed:18829453). May also act as scaffold protein in the nucleus. {ECO:0000269|PubMed:10455146, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:9096337}.Q9H2K8TAOK3$Serine/threonine-protein kinase TAO3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:13679851}. Cell membrane {ECO:0000269|PubMed:13679851}; Peripheral membrane protein {ECO:0000269|PubMed:13679851}. Note=Also localized to the peripheral cell membrane.activation of MAPKK activity [GO:0000186]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; MAPK cascade [GO:0000165]; mitotic G2 DNA damage checkpoint [GO:0007095]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of JNK cascade [GO:0046329]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase inhibitor activity [GO:0004860]; protein serine/threonine kinase activity [GO:0004674]; transferase activity [GO:0016740]FUNCTION: Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF). {ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:10924369, ECO:0000269|PubMed:17396146}.Q14118DAG1 DystroglycanSUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular space.; SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli. {ECO:0000250}.basement membrane organization [GO:0071711]; branching involved in salivary gland morphogenesis [GO:0060445]; calcium-dependent cell-matrix adhesion [GO:0016340]; commissural neuron axon guidance [GO:0071679]; cytoskeletal anchoring at plasma membrane [GO:0007016]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; extracellular matrix organization [GO:0030198]; membrane protein ectodomain proteolysis [GO:0006509]; microtubule anchoring [GO:0034453]; modulation by virus of host morphology or physiology [GO:0019048]; morphogenesis of an epithelial sheet [GO:0002011]; myelination in peripheral nervous system [GO:0022011]; negative regulation of cell migration [GO:0030336]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of protein kinase B signaling [GO:0051898]; nerve maturation [GO:0021682]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; regulation of embryonic cell shape [GO:0016476]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gastrulation [GO:0010470]; response to peptide hormone [GO:0043434]3actin binding [GO:0003779]; alpha-actinin binding [GO:0051393]; calcium ion binding [GO:0005509]; laminin-1 binding [GO:0043237]; SH2 domain binding [GO:0042169]; structural constituent of muscle [GO:0008307]; tubulin binding [GO:0015631]; vinculin binding [GO:0017166]; virus receptor activity [GO:0001618]basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell-cell adherens junction [GO:0005913]; cell outer membrane [GO:0009279]; contractile ring [GO:0070938]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystroglycan complex [GO:0016011]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; node of Ranvier [GO:0033268]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]FUNCTION: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.; FUNCTION: Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.; FUNCTION: Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.Q15208STK38"Serine/threonine-protein kinase 38cellular protein modification process [GO:0006464]; intracellular signal transduction [GO:0035556]; negative regulation of MAP kinase activity [GO:0043407]; protein phosphorylation [GO:0006468]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein serine/threonine kinase activity [GO:0004674]Icytoplasm [GO:0005737]; MLL5-L complex [GO:0070688]; nucleus [GO:0005634] FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2. {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:7761441}.O15084ANR28JSerine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit ArSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:16564677}. Note=Seems to be excluded from nucleoli.FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation. {ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:18186651}.P05091ALDH2%Aldehyde dehydrogenase, mitochondrialMalcohol metabolic process [GO:0006066]; carbohydrate metabolic process < [GO:0005975]; ethanol catabolic process [GO:0006068]; ethanol oxidation [GO:0006069]; neurotransmitter biosynthetic process [GO:0042136]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; xenobiotic metabolic process [GO:0006805]aldehyde dehydrogenase (NAD) activity [GO:0004029]; aldehyde dehydrogenase [NAD(P)+] activity [GO:0004030]; electron carrier activity [GO:0009055]Q29RF7PDS5A0Sister chromatid cohesion protein PDS5 homolog A%SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:15019998}. Note=Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase. {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:15019998}.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid cohesion [GO:0007064]; negative regulation of DNA replication [GO:0008156]chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Probable regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19907496}.Q99755PI51A6Phosphatidylinositol 4-phosphate 5-kinase type-1 alphaSUBCELLULAR LOCATION: Cell membrane. Cytoplasm {ECO:0000250}. Nucleus speckle. Cell projection, ruffle. Note=Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.actin cytoskeleton reorganization [GO:0031532]; activation of GTPase activity [GO:0090630]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; fibroblast migration [GO:0010761]; focal adhesion assembly [GO:0048041]; glycerophospholipid metabolic process [GO:0006650]; keratinocyte differentiation [GO:0030216]; phagocytosis [GO:0006909]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid biosynthetic process [GO:0008654]; phospholipid metabolic process [GO:0006644]; protein targeting to plasma membrane [GO:0072661]; ruffle assembly [GO:0097178]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]x1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]; kinase binding [GO:0019900]cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587](FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs. {ECO:0000269|PubMed:18288197, ECO:0000269|PubMed:19158393, ECO:0000269|PubMed:20660631}.O95696BRD1 Bromodomain-containing protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21880731}.histone H3 acetylation [GO:0043966]; response to electrical stimulus [GO:0051602]; response to immobilization stress [GO:0035902];histone binding [GO:0042393]; zinc ion binding [GO:0008270]dendrite [GO:0030425]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]FUNCTION: Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:21880731}.Q9BSC4NOL10Nucleolar protein 10Q63ZY3KANK27KN motif and ankyrin repeat domain-containing protein 2apoptotic process [GO:0006915]; negative regulation of cell proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of programmed cell death [GO:0043069]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of vitamin D receptor signaling pathway [GO:0070563]; transcription, DNA-templated [GO:0006351]FUNCTION: Involved in transcription regulation by sequestering nuclear receptor coactivators, such as NCOA1, NCOA2 and NCOA3, in the cytoplasm; the function is deregulated by phosphorylation. Involved in the negative control of vitamin D receptor signaling pathway (PubMed:24671081). May be involved in the control of cytoskeleton formation by regulating actin polymerization. Involved in regulation of caspase-independent apoptosis; proposed to sequester AIFM1 in mitochondria and apoptotic stimuli lead to its proteasomal degradation allowing the release of AIFM1 to the nucleus (PubMed:22371500). May be involved in promotion of cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q8BX02, ECO:0000269|PubMed:17476305, ECO:0000269|PubMed:22371500, ECO:0000269|PubMed:24671081}.O94916NFAT5%Nuclear factor of activated T-cells 5SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Nuclear distribution increases under hypertonic conditions. {ECO:0000250}.Qcytokine production [GO:0001816]; excretion [GO:0007588]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of calcineurin-NFAT signaling cascade [GO:0070884]; response to osmotic stress [GO:0006970]; signal transduction [GO:0007165]; transcription from RNA polymerase II promoter [GO:0006366]FUNCTION: Transcription factor involved in the transcriptional regulation of osmoprotective and inflammatory genes. Regulates hypertonicity-induced cellular accumulation of osmolytes.P38919IF4A3#Eukaryotic initiation factor 4A-IIIjSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites (By similarity). {ECO:0000250}.cytokine-mediated signaling pathway [GO:0019221]; embryonic cranial skeleton morphogenesis [GO:0048701]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; nuclear-transcribed mRNA ca< tabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of translation [GO:0045727]; RNA secondary structure unwinding [GO:0010501]; RNA splicing [GO:0008380]; rRNA processing [GO:0006364]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]QFUNCTION: ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Involved in craniofacial development. {ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:24360810}.O15069NACAD%NAC-alpha domain-containing protein 1FUNCTION: May prevent inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). May bind to nascent polypeptide chains as they emerge from the ribosome and block their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. May also reduce the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). {ECO:0000250}.Q96ES7SGF29!SAGA-associated factor 29 homologchromatin organization [GO:0006325]; establishment of protein localization to chromatin [GO:0071169]; histone H3 acetylation [GO:0043966]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351][Ada2/Gcn5/Ada3 transcription activator complex [GO:0005671]; SAGA-type complex [GO:0070461]FUNCTION: Involved in transcriptional regulation, through association with histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA-type complexes, required to recruit complexes to H3K4me. May be involved in MYC-mediated oncogenic transformation. {ECO:0000269|PubMed:19103755}.Q9HB09B2L12Bcl-2-like protein 12dinhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; negative regulation of cellular senescence [GO:2000773]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]Q9UKV5AMFR E3 ubiquitin-protein ligase AMFRSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11724934}; Multi-pass membrane protein {ECO:0000269|PubMed:11724934}.endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; movement of cell or subcellular component [GO:0006928]; positive regulation of protein binding [GO:0032092]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein oligomerization [GO:0051259]; protein polyubiquitination [GO:0000209]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process [GO:0006511]BAT3 complex binding [GO:1904288]; chaperone binding [GO:0051087]; ligase activity [GO:0016874]; protein binding, bridging [GO:0030674]; receptor activity [GO:0004872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-specific protease binding [GO:1990381]; ubiquitin-ubiquitin ligase activity [GO:0034450]; zinc ion binding [GO:0008270]+endoplasmic reticulum membrane [GO:0005789]; Hrd1p ubiquitin ligase complex [GO:0000836]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]FUNCTION: E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor. {ECO:0000269|PubMed:10456327, ECO:0000269|PubMed:11724934, ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:19103148}.Q6PKC3TXD11(Thioredoxin domain-containing protein 11oSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.$FUNCTION: May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.P57105SYJ2BSynaptojanin-2-binding proteinOintracellular distribution of mitochondria [GO:0048312]; negative regulation of activin receptor signaling pathway [GO:0032926]; positive regulation of activin receptor signaling pathway [GO:0032927]; positive regulation of protein localization to cell surface [GO:2000010]; positive regulation of receptor internalization [GO:0002092]vcell surface [GO:0009986]; integral component of mitochondrial outer membrane [GO:0031307]; mitochondrion [GO:0005739]Q9H3U5MFSD19Major facilitator superfamily domain-containing protein 1Bsubstrate-specific transmembrane transporter activity [GO:0022891]Q8TE82S3TC1<SH3 domain and tetratricopeptide repeat-containing protein 1O15212PFD6Prefoldin subunit 6de novo' posttranslational protein folding [GO:0051084]; cellular protein metabolic process [GO:0044267]; chaperone-mediated protein complex assembly [GO:0051131]; protein folding [GO:0006457]Echaperone binding [GO:0051087]; un< folded protein binding [GO:0051082]Q96GP6SREC2#Scavenger receptor class F member 2Xheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]FUNCTION: Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL) (By similarity). {ECO:0000250}.Q9UK10ZN225Zinc finger protein 225P00966ASSYArgininosuccinate synthaseacute-phase response [GO:0006953]; aging [GO:0007568]; arginine biosynthetic process [GO:0006526]; argininosuccinate metabolic process [GO:0000053]; aspartate metabolic process [GO:0006531]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to amine stimulus [GO:0071418]; cellular response to amino acid stimulus [GO:0071230]; cellular response to ammonium ion [GO:0071242]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucagon stimulus [GO:0071377]; cellular response to interferon-gamma [GO:0071346]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oleic acid [GO:0071400]; cellular response to tumor necrosis factor [GO:0071356]; citrulline metabolic process [GO:0000052]; diaphragm development [GO:0060539]; kidney development [GO:0001822]; liver development [GO:0001889]; midgut development [GO:0007494]; negative regulation of leukocyte cell-cell adhesion [GO:1903038]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to growth hormone [GO:0060416]; response to mycotoxin [GO:0010046]; response to nutrient [GO:0007584]; response to zinc ion [GO:0010043]; small molecule metabolic process [GO:0044281]; urea cycle [GO:0000050]amino acid binding [GO:0016597]; argininosuccinate synthase activity [GO:0004055]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; toxic substance binding [GO:0015643]cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; perikaryon [GO:0043204]QFUNCTION: Is indirectly involved in the control of blood pressure. {ECO:0000250}.P28715ERCC5+DNA repair protein complementing XP-G cells;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7651464}.DNA repair [GO:0006281]; negative regulation of apoptotic process [GO:0043066]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA incision, 3'-to lesion [GO:0006295]; response to UV [GO:0009411]; response to UV-C [GO:0010225]; transcription-coupled nucleotide-excision repair [GO:0006283]; UV protection [GO:0009650]=bubble DNA binding [GO:0000405]; double-stranded DNA binding [GO:0003690]; endodeoxyribonuclease activity [GO:0004520]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein N-terminus binding [GO:0047485]; single-stranded DNA binding [GO:0003697]FUNCTION: Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Acts as a cofactor for a DNA glycosylase that removes oxidized pyrimidines from DNA. May also be involved in transcription-coupled repair of this kind of damage, in transcription by RNA polymerase II, and perhaps in other processes too.Q9NQB0TF7L2Transcription factor 7-like 2SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9916915}. Note=Diffuse pattern. Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia) nuclear bodies. blood vessel development [GO:0001568]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition [GO:0044334]; catenin import into nucleus [GO:0035411]; cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; cellular glucose homeostasis [GO:0001678]; cellular response to starvation [GO:0009267]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic genitalia morphogenesis [GO:0030538]; embryonic hindgut morphogenesis [GO:0048619]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; generation of neurons [GO:0048699]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glycogen metabolic process [GO:0005977]; insulin metabolic process [GO:1901142]; maintenance of DNA repeat elements [GO:0043570]; multicellular organism growth [GO:0035264]; myoblast fate commitment [GO:0048625]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of organ growth [GO:0046621]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; neural tube development [GO:0021915]; odontogenesis of dentin-containing tooth [GO:0042475]; oligodendrocyte development [GO:0014003]; pancreas development [GO:0031016]; pituitary gland development [GO:0021983]; positive regulation of apoptotic process [GO:0043065]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of heparan sulfate proteoglycan biosynthetic process [GO:0010909]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein binding [GO:0032092]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of triglyceride biosynthetic process [GO:0010867]; post-embryonic development [GO:0009791]; regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter [GO:0035947]; regulation of hormone metabolic process [GO:0032350]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of myelination [GO:0031641]; regulation of oligodendrocyte differentiation [GO:0048713]; regulation of skeletal muscle tissue development [GO:0048641]; regulation of smooth muscle cell proliferation [GO:0048660]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to glucose [GO:0009749]; secretory granule localization [GO:0032252]; skin development [GO:0043588]; somatic stem cell maintenance [GO:0035019]; transcription, DNA-templated [GO:0006351]armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; gamma-catenin binding [GO:0045295]; nuclear hormone receptor binding [GO:0035257]; protein kinase binding [GO:0019901]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II repressing transcription factor binding [GO:0001103]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]beta-catenin-TCF7L2 complex [GO:0070369]; cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005< 654]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-DNA complex [GO:0032993]; transcription factor complex [GO:0005667]FUNCTION: Participates in the Wnt signaling pathway and modulates MYC expression by binding to its promoter in a sequence-specific manner. Acts as repressor in the absence of CTNNB1, and as activator in its presence. Activates transcription from promoters with several copies of the Tcf motif 5'-CCTTTGATC-3' in the presence of CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants results in cell-cycle arrest in G1. Necessary for the maintenance of the epithelial stem-cell compartment of the small intestine. {ECO:0000269|PubMed:12408868, ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:19443654, ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9727977}.Q9H6S3ES8L2BEpidermal growth factor receptor kinase substrate 8-like protein 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565974}.positive regulation of GTPase activity [GO:0043547]; positive regulation of ruffle assembly [GO:1900029]; regulation of Rho protein signal transduction [GO:0035023]; Rho protein signal transduction [GO:0007266]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; ruffle membrane [GO:0032587]; vesicle [GO:0031982]FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. {ECO:0000269|PubMed:14565974}.Q8NF91SYNE1 Nesprin-1SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres. In myoblasts, relocalized from the nuclear envelope to the nucleus and cytoplasm during cell differentiation.; SUBCELLULAR LOCATION: Isoform GSRP-56: Golgi apparatus {ECO:0000269|PubMed:16875688}.cytoskeletal anchoring at nuclear membrane [GO:0090286]; establishment of nucleus localization [GO:0040023]; Golgi organization [GO:0007030]; muscle cell differentiation [GO:0042692]; nuclear matrix anchoring at nuclear membrane [GO:0090292]; nucleus organization [GO:0006997]actin binding [GO:0003779]; actin filament binding [GO:0051015]; identical protein binding [GO:0042802]; lamin binding [GO:0005521]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]fcytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; LINC complex [GO:0034993]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211]; sarcomere [GO:0030017]FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. May be involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. May be required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:18396275}.Q7Z698SPRE21Sprouty-related, EVH1 domain-containing protein 2sSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm. Note=Especially found in the cytoplasm of the stratum spinosum cells called membrane-coated granules.;inactivation of MAPK activity [GO:0000188]; multicellular organismal development [GO:0007275]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; regulation of protein deacetylation [GO:0090311]protein kinase binding [GO:0019901]; protein serine/threonine kinase inhibitor activity [GO:0030291]; stem cell factor receptor binding [GO:0005173]wcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658]bFUNCTION: Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase.Q9NXH8TOR4A Torsin-4AQ86YM7HOME1Homer protein homolog 1&SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum. {ECO:0000250}.behavioral response to cocaine [GO:0048148]; chemical homeostasis within a tissue [GO:0048875]; circadian rhythm [GO:0007623]; phospholipase C-activating G-protein coupled glutamate receptor signaling pathway [GO:0007206]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of signal transduction [GO:0009967]; protein localization to synapse [GO:0035418]; regulation of calcium ion import [GO:0090279]; regulation of cation channel activity [GO:2001257]; regulation of store-operated calcium entry [GO:2001256]; response to calcium ion [GO:0051592]; response to nicotine [GO:0035094]; skeletal muscle contraction [GO:0003009]; skeletal muscle fiber development [GO:0048741]; synaptic transmission [GO:0007268]G-protein coupled glutamate receptor binding [GO:0035256]; ion channel binding [GO:0044325]; signaling adaptor activity [GO:0035591]Japical part of cell [GO:0045177]; axon [GO:0030424]; cell junction [GO:0030054]; costamere [GO:0043034]; dendritic shaft [GO:0043198]; excitatory synapse [GO:0060076]; neuronal cell body [GO:0043025]; neuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; Z disc [GO:0030018]FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoform 1 regulates the trafficking and surface expression of GRM5. Isoform 3 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1 to regulate synaptic metabotropic glutamate function. Isoform 3, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development.Q8IZ21PHAR4!Phosphatase and actin regulator 4\SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; closure of optic fissure [GO:0061386]; enteric nervous system development [GO:0048484]; negative regulation of integrin-mediated signaling pathway [GO:2001045]; neural crest cell migration [GO:0001755]; neural tube closure [GO:0001843]; positive regulation of catalytic activity [GO:0043085]; regulation of cell cycle [GO:0051726]; Rho protein signal transduction [GO:0007266]actin binding [GO:0003779]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase type 1 activator activity [GO:0071862]2cytoplasm [GO:0005737]; lamellipodium [GO:0030027]FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENC< Cs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). {ECO:0000250}.P42285SK2L2)Superkiller viralicidic activity 2-like 2?SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus.umaturation of 5.8S rRNA [GO:0000460]; mRNA splicing, via spliceosome [GO:0000398]; RNA catabolic process [GO:0006401]^ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; RNA helicase activity [GO:0003724]qcatalytic step 2 spliceosome [GO:0071013]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: May be involved in pre-mRNA splicing. Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA. {ECO:0000269|PubMed:17412707}.Q13242SRSF9&Serine/arginine-rich splicing factor 9SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10196175, ECO:0000269|PubMed:11694584, ECO:0000269|PubMed:12024014, ECO:0000269|PubMed:12604611}. Note=Cellular stresses such as heat shock may induce localization to discrete nuclear bodies termed SAM68 nuclear bodies (SNBs), HAP bodies, or stress bodies. Numerous splicing factors including SRSF1/SFRS1/SF2, SRSF7/SFRS7, SAFB and KHDRBS1/SAM68 accumulate at these structures, which may participate in the post-transcriptional regulation of mRNAs in stressed cells.gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splice site selection [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]0nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:10196175, ECO:0000269|PubMed:11875052, ECO:0000269|PubMed:12024014, ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:15009090, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:15695522, ECO:0000269|PubMed:7556075}.Q96SL1DIRC2&Disrupted in renal carcinoma protein 2SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21692750}; Multi-pass membrane protein {ECO:0000269|PubMed:21692750}.MFUNCTION: Electrogenic metabolite transporter. {ECO:0000269|PubMed:21692750}.Q8NBQ5DHB11"Estradiol 17-beta-dehydrogenase 11Randrogen catabolic process [GO:0006710]; steroid biosynthetic process [GO:0006694]bestradiol 17-beta-dehydrogenase activity [GO:0004303]; steroid dehydrogenase activity [GO:0016229]Vcytoplasm [GO:0005737]; extracellular region [GO:0005576]; lipid particle [GO:0005811]FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell lymphoma.P06132DCUPUroporphyrinogen decarboxylase\cellular response to arsenic-containing substance [GO:0071243]; heme biosynthetic process [GO:0006783]; liver development [GO:0001889]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to amine [GO:0014075]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to fungicide [GO:0060992]; response to iron ion [GO:0010039]; response to mercury ion [GO:0046689]; response to methylmercury [GO:0051597]; small molecule metabolic process [GO:0044281]; uroporphyrinogen III metabolic process [GO:0046502]Wferrous iron binding [GO:0008198]; uroporphyrinogen decarboxylase activity [GO:0004853]wFUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.P06454PTMAProthymosin alphauFUNCTION: Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.Q14008CKAP5!Cytoskeleton-associated protein 5'SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21646404}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:21646404}. Note=Detected on centrosomes during interphase. Detected on spindle poles and microtubules during mitosis.cell division [GO:0051301]; centrosome organization [GO:0051297]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; organelle organization [GO:0006996]; RNA transport [GO:0050658]; small GTPase mediated signal transduction [GO:0007264]; spindle organization [GO:0007051]}centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; protein complex [GO:0043234]; spindle pole [GO:0000922]FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. {ECO:0000269|PubMed:12569123, ECO:0000269|PubMed:21646404}.Q8TEQ6GEMI5Gem-associated protein 5OSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11714716}. Nucleus, gem {ECO:0000269|PubMed:11714716}. Cytoplasm {ECO:0000269|PubMed:11714716}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; protein complex assembly [GO:0006461]; spliceosomal snRNP assembly [GO:0000387]<poly(A) RNA binding [GO:0044822]; snRNA binding [GO:0017069]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; membrane [GO:0016020]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. GEMIN5 acts as the snRNA-binding protein of the SMN complex. {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:16857593, ECO:0000269|PubMed:18984161}.Q9BYV8CEP41Centrosomal protein of 41 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Note=Localizes mainly to the cilium basal body and in primary cilia.cilium assembly [GO:0042384]; G2/M transition of mitotic cell c< ycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; protein polyglutamylation [GO:0018095]; protein transport [GO:0015031]centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; membrane [GO:0016020]; primary cilium [GO:0072372]FUNCTION: Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium. {ECO:0000269|PubMed:22246503}.Q13563PKD2 Polycystin-2SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:18695040}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. aorta development [GO:0035904]; branching involved in ureteric bud morphogenesis [GO:0001658]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cell cycle arrest [GO:0007050]; cellular response to fluid shear stress [GO:0071498]; cellular response to hydrostatic pressure [GO:0071464]; cellular response to osmotic stress [GO:0071470]; cellular response to reactive oxygen species [GO:0034614]; centrosome duplication [GO:0051298]; cytoplasmic sequestering of transcription factor [GO:0042994]; detection of mechanical stimulus [GO:0050982]; detection of nodal flow [GO:0003127]; determination of left/right symmetry [GO:0007368]; determination of liver left/right asymmetry [GO:0071910]; embryonic placenta development [GO:0001892]; heart development [GO:0007507]; heart looping [GO:0001947]; JAK-STAT cascade [GO:0007259]; liver development [GO:0001889]; mesonephric duct development [GO:0072177]; mesonephric tubule development [GO:0072164]; metanephric ascending thin limb development [GO:0072218]; metanephric cortex development [GO:0072214]; metanephric cortical collecting duct development [GO:0072219]; metanephric distal tubule development [GO:0072235]; metanephric mesenchyme development [GO:0072075]; metanephric part of ureteric bud development [GO:0035502]; metanephric smooth muscle tissue development [GO:0072208]; metanephric S-shaped body morphogenesis [GO:0072284]; negative regulation of cell proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; neural tube development [GO:0021915]; placenta blood vessel development [GO:0060674]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0031587]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of calcium ion import [GO:0090279]; regulation of cAMP metabolic process [GO:0030814]; regulation of cell proliferation [GO:0042127]; release of sequestered calcium ion into cytosol [GO:0051209]; renal artery morphogenesis [GO:0061441]; renal tubule morphogenesis [GO:0061333]; sodium ion transmembrane transport [GO:0035725]; spinal cord development [GO:0021510]actinin binding [GO:0042805]; ATPase binding [GO:0051117]; calcium-induced calcium release activity [GO:0048763]; calcium ion binding [GO:0005509]; cytoskeletal protein binding [GO:0008092]; HLH domain binding [GO:0043398]; identical protein binding [GO:0042802]; ion channel binding [GO:0044325]; phosphoprotein binding [GO:0051219]; potassium channel activity [GO:0005267]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated cation channel activity [GO:0022843]; voltage-gated ion channel activity [GO:0005244]; voltage-gated sodium channel activity [GO:0005248]basal cortex [GO:0045180]; basal plasma membrane [GO:0009925]; cell-cell junction [GO:0005911]; ciliary basal body [GO:0036064]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of cytoplasmic side of endoplasmic reticulum membrane [GO:0071458]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; integral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; mitotic spindle [GO:0072686]; motile primary cilium [GO:0031512]; nonmotile primary cilium [GO:0031513]; plasma membrane [GO:0005886]; polycystin complex [GO:0002133]FUNCTION: Functions as a calcium permeable cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary for normal tubulogenesis. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left/right axis specification downstream of nodal flow: forms a complex with PKD1L1 in cilia to facilitate flow detection in left/right patterning (By similarity). {ECO:0000250|UniProtKB:O35245, ECO:0000269|PubMed:18695040}.Q9BUH6CI142 Uncharacterized protein C9orf142SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25574025}. Note=Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation. {ECO:0000269|PubMed:25574025}.cellular response to DNA damage stimulus [GO:0006974]; DNA ligation involved in DNA repair [GO:0051103]; double-strand break repair via nonhomologous end joining [GO:0006303]3FUNCTION: Involved in DNA non-homologous end joining (NHEJ). May act as a scaffold required to stabilize the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at DNA ends and thus promote assembly and/or stability of the NHEJ machinery at double-strand break (DSB) sites. {ECO:0000269|PubMed:25574025}.O14933UB2L6(Ubiquitin/ISG15-conjugating enzyme E2 L6ocellular protein modification process [GO:0006464]; cytokine-mediated signaling pathway [GO:0019221]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; ISG15-protein conjugation [GO:0032020]; modification-dependent protein catabolic process [GO:0019941]; negative regulation of type I interferon production [GO:0032480]; translesion synthesis [GO:0019985]zISG15 transferase activity [GO:0042296]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]3FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. {ECO:0000269|PubMed:15131269, ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20508617}.Q5T7M9FA69AProtein FAM69AP08754GNAI35Guanine nucleotide-binding protein G(k) subunit alphaDSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; blood coagulation [GO:0007596]; cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of adenylate cyclase activity [GO:0007194]; platelet activation [GO:0030168]; synaptic transmission [GO:0007268]; transport [GO:0006810]; vesicle fusion [GO:00< 06906]G-protein beta/gamma-subunit complex binding [GO:0031683]; G-protein coupled serotonin receptor binding [GO:0031821]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]Fcentrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; heterotrimeric G-protein complex [GO:0005834]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; midbody [GO:0030496]; plasma membrane [GO:0005886]; zymogen granule [GO:0042588]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor-regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division. {ECO:0000269|PubMed:17635935}.P0CG38POTEI#POTE ankyrin domain family member Iretina homeostasis [GO:0001895]Q8IWJ2GCC20GRIP and coiled-coil domain-containing protein 2lSUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein.Golgi ribbon formation [GO:0090161]; late endosome to Golgi transport [GO:0034499]; microtubule anchoring [GO:0034453]; microtubule organizing center organization [GO:0031023]; protein localization to Golgi apparatus [GO:0034067]; protein targeting to Golgi [GO:0000042]; protein targeting to lysosome [GO:0006622]; recycling endosome to Golgi transport [GO:0071955]; regulation of protein exit from endoplasmic reticulum [GO:0070861]; retrograde transport, endosome to Golgi [GO:0042147]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802]qFUNCTION: Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2. {ECO:0000269|PubMed:16885419, ECO:0000269|PubMed:17488291, ECO:0000269|PubMed:17543864}.P01116RASK GTPase KRasSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361}; Lipid-anchor {ECO:0000305|PubMed:23698361}; Cytoplasmic side {ECO:0000305|PubMed:23698361}. Cytoplasm, cytosol {ECO:0000269|PubMed:23698361}.Yactin cytoskeleton organization [GO:0030036]; activation of MAPKK activity [GO:0000186]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cytokine-mediated signaling pathway [GO:0019221]; endocrine signaling [GO:0038002]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; homeostasis of number of cells within a tissue [GO:0048873]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; leukocyte migration [GO:0050900]; MAPK cascade [GO:0000165]; negative regulation of cell differentiation [GO:0045596]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of cell proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Rac protein signal transduction [GO:0035022]; Ras protein signal transduction [GO:0007265]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of synaptic transmission, GABAergic [GO:0032228]; response to glucocorticoid [GO:0051384]; response to mineralocorticoid [GO:0051385]; small GTPase mediated signal transduction [GO:0007264]; social behavior [GO:0035176]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; striated muscle cell differentiation [GO:0051146]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; visual learning [GO:0008542]rGDP binding [GO:0019003]; GMP binding [GO:0019002]; GTP binding [GO:0005525]; protein complex binding [GO:0032403]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation (PubMed:23698361, PubMed:22711838). {ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000305}.O94913PCF11)Pre-mRNA cleavage complex 2 protein Pcf11FmRNA binding [GO:0003729]; RNA polymerase II core binding [GO:0000993][cytoplasm [GO:0005737]; mRNA cleavage factor complex [GO:0005849]; nucleoplasm [GO:0005654]4FUNCTION: Component of pre-mRNA cleavage complex II.Q9H694BICC1Protein bicaudal C homolog 1vmulticellular organismal development [GO:0007275]; negative regulation of canonical Wnt signaling pathway [GO:0090090]FUNCTION: Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development. {ECO:0000269|PubMed:21922595}.P47897SYQGlutamine--tRNA ligase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24656866}.brain development [GO:0007420]; gene expression [GO:0010467]; glutaminyl-tRNA aminoacylation [GO:0006425]; tRNA aminoacylation for protein translation [GO:0006418]EATP binding [GO:0005524]; glutamine-tRNA ligase activity [GO:0004819]Ocytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]TFUNCTION: Plays a critical role in brain development. {ECO:0000269|PubMed:24656866}.Q15526SURF1Surfeit locus protein 1aerobic respiration [GO:0009060]; ATP biosynthetic process [GO:0006754]; oxidation-reduction process [GO:0055114]; oxidative phosphorylation [GO:0006119]; respiratory chain complex IV assembly [GO:0008535]Yintegral component of membrane [GO:0016021]; mitochondrial respiratory chain [GO:0005746]AFUNCTION: Probably involved in the biogenesis of the COX complex.Q9UKD2MRT4mRNA turnover protein 4 homologSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20083226}. Cytoplasm {ECO:0000269|PubMed:20083226}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:20083226}.}cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes. {ECO:0000269|PubMed:20083226}.Q96NL6SCLT1$Sodium channel and clathrin linker 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23348840}. Note=Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane.{cilium assembly [GO:0042384]; clustering of voltage-gated sodium channels [GO:0045162]; organelle organization [GO:0006996].sodium channel regulator activity [GO:0017080]centriole [GO:0005814]; centrosome [GO:0005813]; ciliary transition fiber [GO:0097539]; clathrin complex [GO:0< 071439]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]FUNCTION: Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization (By similarity). {ECO:0000250}.Q9HC36MRM3'rRNA methyltransferase 3, mitochondrial_SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282}.Mpoly(A) RNA binding [GO:0044822]; RNA methyltransferase activity [GO:0008173]FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282, ECO:0000269|PubMed:25074936}.Q05682CALD1 CaldesmonSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril {ECO:0000250}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250}.Wmovement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]]actin binding [GO:0003779]; calmodulin binding [GO:0005516]; tropomyosin binding [GO:0005523]actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; myofibril [GO:0030016]; plasma membrane [GO:0005886]FUNCTION: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). {ECO:0000250}.Q9Y5Q9TF3C3-General transcription factor 3C polypeptide 3FUNCTION: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.Q9NRL2BAZ1A5Bromodomain adjacent to zinc finger domain protein 1ATSUBCELLULAR LOCATION: Nucleus. Note=May target the CHRAC complex to heterochromatin.chromatin remodeling [GO:0006338]; DNA-dependent DNA replication [GO:0006261]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]MACF complex [GO:0016590]; CHRAC [GO:0008623]; nuclear chromosome [GO:0000228]FUNCTION: Component of the ACF complex, an ATP-dependent chromatin remodeling complex, that regulates spacing of nucleosomes using ATP to generate evenly spaced nucleosomes along the chromatin. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process. BAZ1A is the accessory, non-catalytic subunit of the complex which can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. May have a role in nuclear receptor-mediated transcription repression.; FUNCTION: Component of the histone-fold protein complex CHRAC complex which faciliates nucleosome sliding by the ACF complex and enhances ACF-mediated chromatin assembly. The C-terminal regions of both CHRAC1 and POLE1 are required for these functions.Q14566MCM6%DNA replication licensing factor MCM6cSUBCELLULAR LOCATION: Nucleus. Note=Binds to chromatin during G1 and detach from it during S phase.DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA unwinding involved in DNA replication [GO:0006268]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]ATP binding [GO:0005524]; DNA helicase activity [GO:0003678]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]HMCM complex [GO:0042555]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]uFUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. {ECO:0000269|PubMed:9305914}.P51608MECP2Methyl-CpG-binding protein 2NSUBCELLULAR LOCATION: Nucleus. Note=Colocalized with methyl-CpG in the genome.adult locomotory behavior [GO:0008344]; behavioral fear response [GO:0001662]; cardiolipin metabolic process [GO:0032048]; catecholamine secretion [GO:0050432]; cerebellum development [GO:0021549]; chromatin silencing [GO:0006342]; dendrite development [GO:0016358]; glucocorticoid metabolic process [GO:0008211]; glutamine metabolic process [GO:0006541]; histone acetylation [GO:0016573]; histone methylation [GO:0016571]; inositol metabolic process [GO:0006020]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; negative regulation of histone acetylation [GO:0035067]; negative regulation of histone methylation [GO:0031061]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neurological system process involved in regulation of systemic arterial blood pressure [GO:0001976]; neuron maturation [GO:0042551]; pathogenesis [GO:0009405]; phosphatidylcholine metabolic process [GO:0046470]; positive regulation of cell proliferation [GO:0008284]; positive regulation of synapse assembly [GO:0051965]; positive regulation of transcription, DNA-templated [GO:0045893]; post-embryonic development [GO:0009791]; proprioception [GO:0019230]; protein localization [GO:0008104]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of respiratory gaseous exchange by neurological system process [GO:0002087]; respiratory gaseous exchange [GO:0007585]; response to hypoxia [GO:0001666]; response to radiation [GO:0009314]; sensory perception of pain [GO:0019233]; social behavior [GO:0035176]; startle response [GO:0001964]; synapse assembly [GO:0007416]; transcription, DNA-templated [GO:0006351]; ventricular system development [GO:0021591]; visual learning [GO:0008542]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded methylated DNA binding [GO:0010385]; methyl-CpG binding [GO:0008327]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; protein N-terminus binding [GO:0047485]; sequence-specific DNA binding transcription factor activity [GO:0003700]; siRNA binding [GO:0035197]; transcription corepressor activity [GO:0003714]cytosol [GO:0005829]; extracellular space [GO:0005615]; heterochromatin [GO:0000792]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcyto< sine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC). {ECO:0000250|UniProtKB:Q9Z2D6}.O95453PARN"Poly(A)-specific ribonuclease PARNfSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus. Note=Some nuclear fraction is nucleolar.female gamete generation [GO:0007292]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; RNA modification [GO:0009451]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; nuclease activity [GO:0004518]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly(A)-specific ribonuclease activity [GO:0004535]; protein kinase binding [GO:0019901]Zcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]CFUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization. {ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:9736620}.O60641AP180$Clathrin coat assembly protein AP180SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.clathrin coat assembly [GO:0048268]; protein transport [GO:0015031]; regulation of clathrin-mediated endocytosis [GO:2000369]; synaptic transmission [GO:0007268]P1-phosphatidylinositol binding [GO:0005545]; protein kinase binding [GO:0019901]FUNCTION: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats (By similarity). {ECO:0000250}.Q92968PEX13"Peroxisomal membrane protein PEX13SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11390669}; Single-pass membrane protein {ECO:0000269|PubMed:11390669}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cerebral cortex cell migration [GO:0021795]; fatty acid alpha-oxidation [GO:0001561]; locomotory behavior [GO:0007626]; microtubule-based peroxisome localization [GO:0060152]; neuron migration [GO:0001764]; positive regulation of defense response to virus by host [GO:0002230]; protein import into peroxisome matrix, docking [GO:0016560]; suckling behavior [GO:0001967]integral component of peroxisomal membrane [GO:0005779]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Component of the peroxisomal translocation machinery with PEX14 and PEX17. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1 and PTS2 proteins.O43493TGON2/Trans-Golgi network integral membrane protein 2SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes.Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; transport vesicle [GO:0030133]YFUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network.H3BNL8CF229 Uncharacterized protein C6orf229Q86VF7NRAP!Nebulin-related-anchoring proteinSUBCELLULAR LOCATION: Note=Localized at the myotendinous junction in skeletal muscle and at the intercalated disk in cardiac muscle. {ECO:0000269|PubMed:12789664}.dactin binding [GO:0003779]; muscle alpha-actinin binding [GO:0051371]; zinc ion binding [GO:0008270]Afascia adherens [GO:0005916]; muscle tendon junction [GO:0005927]FUNCTION: May be involved in anchoring the terminal actin filaments in the myofibril to the membrane and in transmitting tension from the myofibrils to the extracellular matrix. {ECO:0000250|UniProtKB:Q80XB4}.P02545LMNA Prelamin-A/CSUBCELLULAR LOCATION: Nucleus. Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C.; SUBCELLULAR LOCATION: Isoform C: Nucleus speckle {ECO:0000269|PubMed:16061563}.hapoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular protein metabolic process [GO:0044267]; cellular response to hypoxia [GO:0071456]; endoplasmic reticulum unfolded protein response [GO:0030968]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; IRE1-mediated unfolded protein response [GO:0036498]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mitotic nuclear envelope reassembly [GO:0007084]; muscle organ development [GO:0007517]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; positive regulation of cell aging [GO:0090343]; programmed cell death [GO:0012501]; protein localization to nucleus [GO:0034504]; regulation of cell migration [GO:0030334]; regulation of protein localization to nucleus [GO:1900180]; spermatogenesis [GO:0007283]; sterol regulatory element binding protein import into nucleus [GO:0035105]; ventricular cardiac muscle cell development [GO:0055015]_cytoplasm [GO:0005737]; cytosol [GO:0005829]; intermediate filament [GO:0005882]; lamin filament [GO:0005638]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone.; FUNCTION: Prelamin-A< /C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.Q9NX58LYAR(Cell growth-regulating nucleolar proteinQ6Y288B3GLTBeta-1,3-glucosyltransferaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:16899492}; Single-pass type II membrane protein {ECO:0000269|PubMed:16899492}.cellular protein metabolic process [GO:0044267]; fucose metabolic process [GO:0006004]; post-translational protein modification [GO:0043687]; protein O-linked fucosylation [GO:0036066]; protein O-linked glycosylation [GO:0006493]FUNCTION: O-fucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan. {ECO:0000269|PubMed:16899492}.Q9UJX2CDC23&Cell division cycle protein 23 homologanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell division [GO:0051301]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic cell cycle [GO:0000278]; mitotic metaphase plate congression [GO:0007080]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K11-linked ubiquitination [GO:0070979]; regulation of exit from mitosis [GO:0007096]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; ubiquitin-dependent protein catabolic process [GO:0006511]sanaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]Q92667AKAP1(A-kinase anchor protein 1, mitochondrialASUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305}.Gblood coagulation [GO:0007596]; cellular response to cAMP [GO:0071320]; cellular response to peptide hormone stimulus [GO:0071375]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of NFAT protein import into nucleus [GO:0051534]; negative regulation of protein dephosphorylation [GO:0035308]tpoly(A) RNA binding [GO:0044822]; protein kinase A regulatory subunit binding [GO:0034237]; RNA binding [GO:0003723]Kcytosol [GO:0005829]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211]FUNCTION: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.P09471GNAO5Guanine nucleotide-binding protein G(o) subunit alphaGoalpha2SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.^adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; aging [GO:0007568]; dopamine receptor signaling pathway [GO:0007212]; forebrain development [GO:0030900]; locomotory behavior [GO:0007626]; muscle contraction [GO:0006936]; negative regulation of calcium ion transport [GO:0051926]; neuron projection development [GO:0031175]; positive regulation of GTPase activity [GO:0043547]; regulation of heart contraction [GO:0008016]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to hydrogen peroxide [GO:0042542]; response to morphine [GO:0043278]dcorticotropin-releasing hormone receptor 1 binding [GO:0051430]; G-protein beta/gamma-subunit complex binding [GO:0031683]; G-protein coupled serotonin receptor binding [GO:0031821]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mu-type opioid receptor binding [GO:0031852]; signal transducer activity [GO:0004871]~dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14.Q8IYE1CCD13(Coiled-coil domain-containing protein 13SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24816561}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24816561}.cellular response to DNA damage stimulus [GO:0006974]; cytoplasmic microtubule organization [GO:0031122]; nonmotile primary cilium assembly [GO:0035058]Xcell projection [GO:0042995]; centriolar satellite [GO:0034451]; centrosome [GO:0005813]FUNCTION: Required for primary cilia formation and promotes the localization of the ciliopathy protein BBS4 to both centriolar satellites and cilia. {ECO:0000269|PubMed:24816561}.P17813EGLNEndoglinartery morphogenesis [GO:0048844]; BMP signaling pathway [GO:0030509]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; cell migration involved in endocardial cushion formation [GO:0003273]; cell motility [GO:0048870]; central nervous system vasculogenesis [GO:0022009]; chronological cell aging [GO:0001300]; detection of hypoxia [GO:0070483]; extracellular matrix disassembly [GO:0022617]; heart looping [GO:0001947]; intracellular signal transduction [GO:0035556]; negative regulation of cell migration [GO:0030336]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of nitric-oxide synthase activity [GO:0051001]; negative regulation of pathway-restricted SMAD protein phosphorylation [GO:0060394]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; patterning of blood vessels [GO:0001569]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell adhesion [GO:0030155]; regulation of cell proliferation [GO:0042127]; regulation of phosphorylation [GO:0042325]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to hypoxia [GO:0001666]; smooth muscle tissue development [GO:0048745]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vasculogenesis [GO:0001570]; venous blood vessel morphogenesis [GO:0048845]; wound healing [GO:0042060]/activin binding [GO:0048185]; galactose binding [GO:0005534]; glycosaminoglycan binding [GO:0005539]; protein homodimerization activity [GO:0042803]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor, cytoplasmic mediator activity [GO:0005072]; transmembrane signaling receptor activity [GO:0004888]; type II transforming growth factor beta receptor binding [GO:0005114]; type I transforming growth factor beta receptor binding [GO:0034713]Kcell surface [GO:0009986]; cytoplasm [GO:0005737]; endothelial microparticle [GO:0072563]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; receptor complex [GO:0043235]; transforming growth factor beta receptor homodimeric complex [GO:0070022]FUNCTION: Major glycopro< tein of vascular endothelium. Involved in the regulation of angiogenesis. May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGF-beta1 signaling through SMAD3. {ECO:0000269|PubMed:21737454, ECO:0000269|PubMed:23300529}.Q9Y2E5MA2B2%Epididymis-specific alpha-mannosidaseBextracellular exosome [GO:0070062]; vacuolar membrane [GO:0005774]Q8TE73DYH5Dynein heavy chain 5, axonemal>SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. cilium assembly [GO:0042384]; cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; lateral ventricle development [GO:0021670]; left/right axis specification [GO:0070986]; outer dynein arm assembly [GO:0036158]; sperm motility [GO:0030317]Maxoneme [GO:0005930]; microtubule [GO:0005874]; outer dynein arm [GO:0036157]AFUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.Q92995UBP13(Ubiquitin carboxyl-terminal hydrolase 13autophagy [GO:0006914]; cell proliferation [GO:0008283]; melanocyte differentiation [GO:0030318]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; regulation of autophagy [GO:0010506]; regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903069]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of transcription, DNA-templated [GO:0006355]BAT3 complex binding [GO:1904288]; chaperone binding [GO:0051087]; cysteine-type endopeptidase activity [GO:0004197]; omega peptidase activity [GO:0008242]; proteasome binding [GO:0070628]; ubiquitin binding [GO:0043130]; ubiquitin-like protein ligase binding [GO:0044389]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. {ECO:0000269|PubMed:17653289, ECO:0000269|PubMed:21571647, ECO:0000269|PubMed:21659512, ECO:0000269|PubMed:21811243, ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:22216260}.Q9Y2U8MAN1#Inner nuclear membrane protein Man1SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:15647271}; Multi-pass membrane protein {ECO:0000269|PubMed:15647271}.blood vessel endothelial cell migration involved in intussusceptive angiogenesis [GO:0002044]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; nucleus organization [GO:0006997]; regulation of cell cycle [GO:0051726]; regulation of extracellular matrix organization [GO:1903053]; skeletal muscle cell differentiation [GO:0035914]9DNA binding [GO:0003677]; nucleotide binding [GO:0000166]integral component of membrane [GO:0016021]; integral component of nuclear inner membrane [GO:0005639]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]FUNCTION: Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest. {ECO:0000269|PubMed:15601644, ECO:0000269|PubMed:15647271}.P56545CTBP2C-terminal-binding protein 2RSUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction, synapse {ECO:0000250}.negative regulation of cell proliferation [GO:0008285]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of chromatin binding [GO:0035563]; positive regulation of retinoic acid receptor signaling pathway [GO:0048386]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]; viral genome replication [GO:0019079]; white fat cell differentiation [GO:0050872]chromatin binding [GO:0003682]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]}cell junction [GO:0030054]; nucleus [GO:0005634]; ribbon synapse [GO:0097470]; transcriptional repressor complex [GO:0017053]FUNCTION: Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation (By similarity). {ECO:0000250}.; FUNCTION: Isoform 2 probably acts as a scaffold for specialized synapses.O00468AGRINAgrin SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space, extracellular matrix. Note=Synaptic basal lamina at the neuromuscular junction. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell junction, synapse. Cell membrane; Single-pass type II membrane protein.axon guidance [GO:0007411]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate metabolic process [GO:0030204]; clustering of voltage-gated sodium channels [GO:0045162]; extracellular matrix organization [GO:0030198]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; neuromuscular junction development [GO:0007528]; neurotransmitter receptor metabolic process [GO:0045213]; phototransduction, visible light [GO:0007603]; plasma membrane organization [GO:0007009]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of synaptic growth at neuromuscular junction [GO:0045887]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; receptor clustering [GO:0043113]; retinoid metabolic process [GO:0001523]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synapse organization [GO:0050808]; synaptic transmission [GO:0007268]Macetylcholine receptor regulator activity [GO:0030548]; calcium ion binding [GO:0005509]; chondroitin sulfate binding [GO:0035374]; dystroglycan binding [GO:0002162]; heparan sulfate proteoglycan binding [GO:0043395]; laminin binding [GO:0043236]; sialic acid binding [GO:0033691]; structural constituent of cytoskeleton [GO:0005200]basal lamina [GO:0005605]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extr< acellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; integral component of membrane [GO:0016021]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; synapse [GO:0045202] FUNCTION: Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.; FUNCTION: Isoform 2: transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; FUNCTION: Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.; FUNCTION: Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.; FUNCTION: Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250}.; FUNCTION: Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.P67809YBOX1,Nuclease-sensitive element-binding protein 1[SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic granule {ECO:0000269|PubMed:25229427}. Secreted. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells. Cytotoxic stress and DNA damage enhance translocation to the nucleus. Localized with DDX1, MBNL1 and TIAL1 in stress granules upon stress. Secreted by mesangial and monocytic cells after inflammatory challenges. Translocates from the cytoplasm to the nucleus after and colocalizes with APEX1 in nuclear speckles after genotoxic stress.WCRD-mediated mRNA stabilization [GO:0070934]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of striated muscle cell differentiation [GO:0051154]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell division [GO:0051781]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription from RNA polymerase II promoter [GO:0006366]6chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; GTPase binding [GO:0051020]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; extracellular exosome [GO:0070062]; histone pre-mRNA 3'end processing complex [GO:0071204]; intracellular membrane-bounded organelle [GO:0043231]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; U12-type spliceosomal complex [GO:0005689]9FUNCTION: Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Regulates the transcription of numerous genes. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds preferentially to the 5'-[CU]CUGCG-3' motif in vitro. {ECO:0000250}.; FUNCTION: The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation.Q8TEA7TBCK1TBC domain-containing protein kinase-like protein$protein phosphorylation [GO:0006468]>ATP binding [GO:0005524]; protein kinase activity [GO:0004672]Q9BW60ELOV13Elongation of very long chain fatty acids protein 1~SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255}.Kalpha-linolenic acid metabolic process [GO:0036109]; cellular lipid metabolic process [GO:0044255]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, saturated fatty acid [GO:0019367]; linoleic acid metabolic process [GO:0043651]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; triglyceride biosynthetic process [GO:0019432]; unsaturated fatty acid metabolic process [GO:0033559]; very long-chain fatty acid biosynthetic process [GO:0042761]=FUNCTION: Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs. {ECO:0000269|PubMed:20166112, ECO:0000269|PubMed:20937905}.P51858HDGFHepatoma-derived growth factordcell proliferation [GO:0008283]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; negative regulation of transcription from RNA polymerase II< promoter [GO:0000122]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; heparin binding [GO:0008201]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA polymerase II transcription corepressor activity [GO:0001106]; transcription corepressor binding [GO:0001222]cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; transcriptional repressor complex [GO:0017053]FUNCTION: Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor. {ECO:0000269|PubMed:17974029}.Q9BXW6OSBL1+Oxysterol-binding protein-related protein 1SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:16176980}. Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cholesterol metabolic process [GO:0008203]; lipid transport [GO:0006869]; vesicle-mediated transport [GO:0016192]Ccholesterol binding [GO:0015485]; phospholipid binding [GO:0005543]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (By similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A (PubMed:16176980). Binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000250, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17428193}.O15431COPT1%High affinity copper uptake protein 1SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Localizes to the apical membrane in intestinal epithelial cells. {ECO:0000250}.cellular copper ion homeostasis [GO:0006878]; cellular response to cisplatin [GO:0072719]; copper ion import into cell [GO:1902861]; copper ion transport [GO:0006825]; drug transmembrane transport [GO:0006855]; transmembrane transport [GO:0055085]ycopper ion transmembrane transporter activity [GO:0005375]; copper uptake transmembrane transporter activity [GO:0015088]integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]wFUNCTION: High-affinity, saturable copper transporter involved in dietary copper uptake. {ECO:0000269|PubMed:11734551}.P62699YPEL5Protein yippee-like 5Q14974IMB1Importin subunit beta-1nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}. Nucleus envelope {ECO:0000269|PubMed:11891849}.Zapoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cytokine-mediated signaling pathway [GO:0019221]; intracellular transport of virus [GO:0075733]; NLS-bearing protein import into nucleus [GO:0006607]; programmed cell death [GO:0012501]; protein import into nucleus [GO:0006606]; protein import into nucleus, translocation [GO:0000060]; ribosomal protein import into nucleus [GO:0006610]; small molecule metabolic process [GO:0044281]; viral life cycle [GO:0019058]; viral process [GO:0016032]enzyme binding [GO:0019899]; nuclear localization sequence binding [GO:0008139]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; protein transporter activity [GO:0008565]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum tubular network [GO:0071782]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]FUNCTION: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus. {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:9687515}.Q9HD42CHM1A&Charged multivesicular body protein 1aySUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus matrix. Note=The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On overexpression, it localizes to nuclear bodies characterized by nuclease-resistant condensed chromatin.cell division [GO:0051301]; cell separation after cytokinesis [GO:0000920]; gene silencing [GO:0016458]; mitotic chromosome condensation [GO:0007076]; mitotic metaphase plate congression [GO:0007080]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription by glucose [GO:0045014]; nucleus organization [GO:0006997]; protein transport [GO:0015031]; proteolysis [GO:0006508]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; transcription, DNA-templated [GO:0006351]; vacuolar transport [GO:0007034]; vesicle-mediated transport [GO:0016192]metallopeptidase activity [GO:0008237]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]condensed nuclear chromosome [GO:0000794]; early endosome [GO:0005769]; endomembrane system [GO:0012505]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815]; nuclear matrix [GO:0016363]FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condense< d chromatin. May play a role in stable cell cycle progression and in PcG gene silencing. {ECO:0000269|PubMed:11559747, ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:23045692}.P07355ANXA2 Annexin A2SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism.jangiogenesis [GO:0001525]; body fluid secretion [GO:0007589]; collagen fibril organization [GO:0030199]; fibrinolysis [GO:0042730]; membrane budding [GO:0006900]; membrane raft assembly [GO:0001765]; negative regulation of catalytic activity [GO:0043086]; negative regulation of low-density lipoprotein particle receptor catabolic process [GO:0032804]; negative regulation of receptor binding [GO:1900121]; negative regulation of receptor internalization [GO:0002091]; osteoclast development [GO:0036035]; positive regulation of binding [GO:0051099]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor activity [GO:2000273]; positive regulation of vesicle fusion [GO:0031340]; protein heterotetramerization [GO:0051290]; protein targeting to plasma membrane [GO:0072661]8calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phospholipase A2 inhibitor activity [GO:0019834]; poly(A) RNA binding [GO:0044822]; S100 protein binding [GO:0044548]basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell surface [GO:0009986]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of plasma membrane [GO:0019897]; late endosome membrane [GO:0031902]; lipid particle [GO:0005811]; lysosomal membrane [GO:0005765]; macropinosome [GO:0044354]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; myelin sheath adaxonal region [GO:0035749]; nucleus [GO:0005634]; PCSK9-AnxA2 complex [GO:1990667]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; sarcolemma [GO:0042383]; Schmidt-Lanterman incisure [GO:0043220]; vesicle [GO:0031982]FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640). {ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640, ECO:0000269|PubMed:24808179}.Q9BXW7CECR5*Cat eye syndrome critical region protein 5Q9BT22ALG15Chitobiosyldiphosphodolichol beta-mannosyltransferaseZcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; lipopolysaccharide biosynthetic process [GO:0009103]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279]vchitobiosyldiphosphodolichol beta-mannosyltransferase activity [GO:0004578]; mannosyltransferase activity [GO:0000030]FUNCTION: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER. {ECO:0000269|PubMed:10704531}.P57737CORO7 Coronin-7#SUBCELLULAR LOCATION: Golgi apparatus membrane. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic structures and on the cis-Golgi. Not associated with actin filaments.tactin filament polymerization [GO:0030041]; Golgi to endosome transport [GO:0006895]; protein transport [GO:0015031]cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology. {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}.Q9H583HEAT1 HEAT repeat-containing protein 1maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; positive regulation of transcription from RNA polymerase I promoter [GO:0045943]90S preribosome [GO:0030686]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]; t-UTP complex [GO:0034455]FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis (By similarity). {ECO:0000250}.Q8IYM9TRI22"E3 ubiquitin-protein ligase TRIM22SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus {ECO:0000269|PubMed:17156811}. Nucleus speckle. Nucleus, Cajal body. Note=Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies.cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; immune response [GO:0006955]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of nucleic acid-templated transcription [GO:1903507]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein trimerization [GO:0070206]; protein ubiquitination [GO:0016567]; regulation of transcription, DNA-templated [GO:0006355]; response to virus [GO:0009615]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]ligase activity [GO:0016874]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:18656448, ECO:0000269|PubMed:19218198, ECO:0000269|PubMed:19585648}.O95785WIZ Protein Wizpositive regulation of nuclear cell cycle DNA replication [GO:0010571]; protein heterotrimerization [GO:0070208]; protein stabilization [GO:0050821]FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarit< y). {ECO:0000250}.Q8TD26CHD6+Chromodomain-helicase-DNA-binding protein 6sSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17027977}. Note=Enriched at sites of mRNA synthesis.chromatin modification [GO:0016568]; positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress [GO:0036091]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent helicase activity [GO:0008026]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; transcription cofactor binding [GO:0001221]FUNCTION: Probable chromatin-remodeling protein with a DNA-dependent ATPase activity. May play a role in transcription regulation, activating for instance, the transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000269|PubMed:16314513}.Q86W42THOC6THO complex subunit 6 homologkSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23621916}. Nucleus speckle {ECO:0000305|PubMed:23621916}.apoptotic process [GO:0006915]; central nervous system development [GO:0007417]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; negative regulation of apoptotic process [GO:0043066]; RNA splicing [GO:0008380]; viral mRNA export from host cell nucleus [GO:0046784]nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; THO complex [GO:0000347]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346]FUNCTION: Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Plays a role in apoptosis negative control involved in brain development. {ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:23621916}.Q14690RRP5Protein RRP5 homologSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:14624448, ECO:0000269|PubMed:17654514}.:mRNA processing [GO:0006397]; rRNA processing [GO:0006364]Kpoly(A) RNA binding [GO:0044822]; transcription factor binding [GO:0008134]icytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040] FUNCTION: Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.; FUNCTION: Involved in the biogenesis of rRNA. {ECO:0000250}.O94925GLSK)Glutaminase kidney isoform, mitochondrialeSUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion.lcellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; gene expression [GO:0010467]; glutamate biosynthetic process [GO:0006537]; glutamate secretion [GO:0014047]; glutamine catabolic process [GO:0006543]; neurotransmitter secretion [GO:0007269]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by neurological system process [GO:0002087]; small molecule metabolic process [GO:0044281]; suckling behavior [GO:0001967]; synaptic transmission [GO:0007268]; transcription initiation from RNA polymerase II promoter [GO:0006367]!glutaminase activity [GO:0004359]FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.Q8NI27THOC2THO complex subunit 2KSUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000305}.mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; poly(A)+ mRNA export from nucleus [GO:0016973]; RNA splicing [GO:0008380]; viral mRNA export from host cell nucleus [GO:0046784]nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; THO complex [GO:0000347]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346]UFUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains. Required for NXF1 localization to the nuclear rim. {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23222130}.Q9GZL7WDR12!Ribosome biogenesis protein WDR12?SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.Ecell proliferation [GO:0008283]; maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000466]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; Notch signaling pathway [GO:0007219]; ribosomal large subunit biogenesis [GO:0042273]nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; PeBoW complex [GO:0070545]; preribosome, large subunit precursor [GO:0030687]FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03029, ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:17353269}.Q9Y6M5ZNT1Zinc transporter 1]SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. cadmium ion transmembrane transport [GO:0070574]; calcium ion import [GO:0070509]; cellular calcium ion homeostasis [GO:0006874]; cellular zinc ion homeostasis [GO:0006882]; detoxification of cadmium ion [GO:0071585]; in utero embryonic development [GO:0001701]; negative regulation of calcium ion import [GO:0090281]; negative regulation of neurotransmitter secretion [GO:0046929]; negative regulation of zinc ion transmembrane import [GO:0071584]; transmembrane transport [GO:0055085]; zinc II ion transport [GO:0006829]icalcium channel inhibitor activity [GO:0019855]; zinc ion transmembrane transporter activity [GO:0005385]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]<FUNCTION: May be involved in zinc transport out of the cell.Q7Z5Q1CPEB25Cytoplasmic polyadenylation element-binding protein 2Dorso-ventral axis formation$mRNA polyadenylation factor(PC00146)cellular response to arsenic-containing substance [GO:0071243]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of cytoplasmic translational elongation [GO:1900248]; negative regulation of GTPase activity [GO:0< 034260]; translation [GO:0006412]GTPase inhibitor activity [GO:0005095]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly-pyrimidine tract binding [GO:0008187]; ribosomal large subunit binding [GO:0043023]; ribosomal small subunit binding [GO:0043024]; ribosome binding [GO:0043022]; translation factor activity, RNA binding [GO:0008135]; translation repressor activity, nucleic acid binding [GO:0000900]cytoplasm [GO:0005737]; messenger ribonucleoprotein complex [GO:1990124]; neuron projection [GO:0043005]; nucleus [GO:0005634]; polysome [GO:0005844]; synapse [GO:0045202]FUNCTION: May play a role in translational regulation of stored mRNAs in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA oligomers (By similarity). {ECO:0000250}.Q96ST3SIN3A&Paired amphipathic helix protein Sin3aSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, ECO:0000269|PubMed:16820529}. Nucleus, nucleolus {ECO:0000269|PubMed:16820529}. Note=Recruited to the nucleolus by SAP30L.activation of innate immune response [GO:0002218]; blood coagulation [GO:0007596]; cellular lipid metabolic process [GO:0044255]; cellular protein localization [GO:0034613]; cellular response to glucose stimulus [GO:0071333]; DNA replication [GO:0006260]; gene expression [GO:0010467]; hematopoietic progenitor cell differentiation [GO:0002244]; histone deacetylation [GO:0016575]; in utero embryonic development [GO:0001701]; negative regulation of apoptotic process [GO:0043066]; negative regulation of circadian rhythm [GO:0042754]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of histone H3-K27 acetylation [GO:1901675]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription regulatory region DNA binding [GO:2000678]; positive regulation of chromatin silencing [GO:0031937]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein deacetylation [GO:0006476]; regulation of gene expression, epigenetic [GO:0040029]; response to methylglyoxal [GO:0051595]; rhythmic process [GO:0048511]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]jchromatin binding [GO:0003682]; protein deacetylase activity [GO:0033558]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II transcription corepressor activity [GO:0001106]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region sequence-specific DNA binding [GO:0000976])chromatin [GO:0000785]; cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Sin3 complex [GO:0016580]; transcriptional repressor complex [GO:0017053]; transcription factor complex [GO:0005667]BFUNCTION: Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:12150998}.Q8N6S5AR6P6<ADP-ribosylation factor-like protein 6-interacting protein 6Q96EY4TMA16+Translation machinery-associated protein 16Q9Y4F5C170B(Centrosomal protein of 170 kDa protein BBFUNCTION: Plays a role in microtubule organization. {ECO:0000250}.P49591SYSC Serine--tRNA ligase, cytoplasmic Aminoacyl-tRNA biosynthesisgene expression [GO:0010467]; selenocysteinyl-tRNA(Sec) biosynthetic process [GO:0097056]; seryl-tRNA aminoacylation [GO:0006434]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]; tRNA processing [GO:0008033]\ATP binding [GO:0005524]; RNA binding [GO:0003723]; serine-tRNA ligase activity [GO:0004828]FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:9431993}.Q96I15SCLYSelenocysteine lyase2cellular amino acid metabolic process [GO:0006520]Mselenocysteine lyase activity [GO:0009000]; transferase activity [GO:0016740]mFUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium. {ECO:0000250}.O43896KIF1CKinesin-like protein KIF1Ccytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; motor activity [GO:0003774]; poly(A) RNA binding [GO:0044822]xendoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]FUNCTION: Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:9685376}.Q7Z4H8KDEL2KDEL motif-containing protein 2Q70UQ0IKIP>Inhibitor of nuclear factor kappa-B kinase-interacting proteinlSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15389287}; Single-pass membrane protein {ECO:0000269|PubMed:15389287}. Note=Isoform 4 deletion of the hydrophobic, or transmembrane region between AA 45-63 results in uniform distribution throughout the cell, suggesting that this region is responsible for endoplasmic reticulum localization.response to X-ray [GO:0010165]XFUNCTION: Target of p53/TP53 with pro-apoptotic function. {ECO:0000269|PubMed:15389287}.Q15075EEA1Early endosome antigen 1early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; synaptic vesicle to endosome fusion [GO:0016189]; vesicle fusion [GO:0006906]1-phosphatidylinositol binding [GO:0005545]; calmodulin binding [GO:0005516]; GTP-dependent protein binding [GO:0030742]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270]Saxonal spine [GO:0044308]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; extrinsic component of plasma membrane [GO:0019897]; membrane [GO:0016020]; serine-pyruvate aminotransferase complex [GO:0005969]|FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.P62136PP1A@Serine/threonine-protein phosphatase PP1-alpha catalytic subunit PP1C1a/b/cxSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.branching morphogenesis of an epithelial tube [GO:0048754]; cell cycle [GO:0007049]; cell division [GO:0051301]; circadian regulation of gene expression [GO:0032922]; dephosphorylation [GO:0016311]; entrainment of circadian clock by photoperiod [GO:0043153]; glycogen metabolic process [GO:0005977]; lung development [GO:0030324]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation o< f extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein dephosphorylation [GO:0006470]; regulation of circadian rhythm [GO:0042752]; regulation of glycogen biosynthetic process [GO:0005979]; regulation of glycogen catabolic process [GO:0005981]; regulation of translational initiation by eIF2 alpha dephosphorylation [GO:0036496]; small molecule metabolic process [GO:0044281]; transforming growth factor beta receptor signaling pathway [GO:0007179]; triglyceride catabolic process [GO:0019433]metal ion binding [GO:0046872]; phosphatase activity [GO:0016791]; protein serine/threonine phosphatase activity [GO:0004722]; ribonucleoprotein complex binding [GO:0043021]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glycogen granule [GO:0042587]; MLL5-L complex [GO:0070688]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; protein phosphatase type 1 complex [GO:0000164]; PTW/PP1 phosphatase complex [GO:0072357]FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.O00629IMA3Importin subunit alpha-3cytokine-mediated signaling pathway [GO:0019221]; NLS-bearing protein import into nucleus [GO:0006607]; response to hydrogen peroxide [GO:0042542]FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.Q8IY33MILK2MICAL-like protein 2SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.actin cytoskeleton reorganization [GO:0031532]; actin filament polymerization [GO:0030041]; adherens junction assembly [GO:0034333]; bicellular tight junction assembly [GO:0070830]; endocytic recycling [GO:0032456]; neuron projection development [GO:0031175]; positive regulation of protein targeting to mitochondrion [GO:1903955]; substrate adhesion-dependent cell spreading [GO:0034446]`actin filament binding [GO:0051015]; filamin binding [GO:0031005]; zinc ion binding [GO:0008270]bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; stress fiber [GO:0001725]FUNCTION: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity). {ECO:0000250}.Q9Y613FHOD1#FH1/FH2 domain-containing protein 1pSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, bleb. Note=Predominantly cytoplasmic.positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]qbleb [GO:0032059]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing. {ECO:0000269|PubMed:14576350, ECO:0000269|PubMed:15878344, ECO:0000269|PubMed:18694941}.P11117PPALLysosomal acid phosphatasephosphatases(2)SUBCELLULAR LOCATION: Lysosome membrane; Single-pass membrane protein; Lumenal side. Lysosome lumen. Note=The soluble form arises by proteolytic processing of the membrane-bound form.autophagic cell death [GO:0048102]; dephosphorylation [GO:0016311]; lysosome organization [GO:0007040]; response to organic substance [GO:0010033]; skeletal system development [GO:0001501]Xacid phosphatase activity [GO:0003993]; phosphoprotein phosphatase activity [GO:0004721]cytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; neuron projection [GO:0043005]Q7L099RUFY3 Protein RUFY3SUBCELLULAR LOCATION: Cell projection {ECO:0000250}. Note=Enriched in F-actin enriched filopodia and lamellipodia of growth cones of axons and minor processes of hippocampal neurons in culture. {ECO:0000250}.bnegative regulation of axonogenesis [GO:0050771]; positive regulation of axonogenesis [GO:0050772]|axon [GO:0030424]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]FUNCTION: Implicated in the formation of a single axon by developing neurons. May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). {ECO:0000250}.O75569PRKRAMInterferon-inducible double-stranded RNA-dependent protein kinase activator A?SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm.cellular response to oxidative stress [GO:0034599]; gene expression [GO:0010467]; immune response [GO:0006955]; middle ear morphogenesis [GO:0042474]; negative regulatio< n of cell proliferation [GO:0008285]; outer ear morphogenesis [GO:0042473]; positive regulation of catalytic activity [GO:0043085]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; pre-miRNA processing [GO:0031054]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; production of siRNA involved in RNA interference [GO:0030422]; protein phosphorylation [GO:0006468]; response to virus [GO:0009615]; skeletal system morphogenesis [GO:0048705]double-stranded RNA binding [GO:0003725]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]JFUNCTION: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250}.Q7Z422SZRD1SUZ domain-containing protein 1Q8IVL1NAV2Neuron navigator 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12214280}.Gglossopharyngeal nerve development [GO:0021563]; locomotory behavior [GO:0007626]; optic nerve development [GO:0021554]; regulation of systemic arterial blood pressure by baroreceptor feedback [GO:0003025]; sensory perception of smell [GO:0007608]; sensory perception of sound [GO:0007605]; vagus nerve development [GO:0021564]VATP binding [GO:0005524]; helicase activity [GO:0004386]; heparin binding [GO:0008201]:interstitial matrix [GO:0005614]; nucleoplasm [GO:0005654]FUNCTION: Possesses 3' to 5' helicase activity and exonuclease activity. Involved in neuronal development, specifically in the development of different sensory organs. {ECO:0000269|PubMed:12214280, ECO:0000269|PubMed:15158073}.Q96S82UBL7Ubiquitin-like protein 7Q96MG7MAGG1Melanoma-associated antigen G1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:18086888}. Chromosome, telomere {ECO:0000305|PubMed:18086888}.cellular protein metabolic process [GO:0044267]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of protein ubiquitination [GO:0031398]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of growth [GO:0040008]{chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; Smc5-Smc6 complex [GO:0030915]SFUNCTION: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest. {ECO:0000269|PubMed:20864041}.Q16740CLPP=ATP-dependent Clp protease proteolytic subunit, mitochondrialISUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10525407}.qprotein homooligomerization [GO:0051260]; proteolysis involved in cellular protein catabolic process [GO:0051603]Ppeptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]eendopeptidase Clp complex [GO:0009368]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782}.Q9UKC9FBXL2F-box/LRR-repeat protein 2iSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15893726}; Lipid-anchor {ECO:0000269|PubMed:15893726}.vcellular protein modification process [GO:0006464]; protein monoubiquitination [GO:0006513]; protein ubiquitination [GO:0016567]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regulation of phosphatidylinositol 3-kinase signaling [GO:0014066]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; viral process [GO:0016032]phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; protein phosphatase binding [GO:0019903]; ubiquitin-protein transferase activity [GO:0004842]Xcytoplasm [GO:0005737]; membrane [GO:0016020]; SCF ubiquitin ligase complex [GO:0019005]pFUNCTION: Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0) (PubMed:22020328, PubMed:22323446). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy (PubMed:23604317). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant (By similarity). {ECO:0000250|UniProtKB:Q8BH16, ECO:0000269|PubMed:22020328, ECO:0000269|PubMed:22323446, ECO:0000269|PubMed:23604317}.Q12851M4K27Mitogen-activated protein kinase kinase kinase kinase 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.activation of JUN kinase activity [GO:0007257]; activation of MAPKKK activity [GO:0000185]; immune response [GO:0006955]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; positive regulation of JNK cascade [GO:0046330]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; vesicle targeting [GO:0006903]ATP binding [GO:0005524]; MAP kinase kinase kinase kinase activity [GO:0008349]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; protein serine/threonine kinase activity [GO:0004674]]basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]FUNCTION: Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extend of the p38 MAPKs signaling pathway. Required for the efficient activation of JNKs by TRAF6-dependent stimuli, including pathogen-associated molecular patterns (PAMPs) such as polyinosine-polycytidine (poly(< IC)), lipopolysaccharides (LPS), lipid A, peptidoglycan (PGN), or bacterial flagellin. To a lesser degree, IL-1 and engagement of CD40 also stimulate MAP4K2-mediated JNKs activation. The requirement for MAP4K2/GCK is most pronounced for LPS signaling, and extends to LPS stimulation of c-Jun phosphorylation and induction of IL-8. Enhances MAP3K1 oligomerization, which may relieve N-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. Mediates also the SAP/JNK signaling pathway and the p38 MAPKs signaling pathway through activation of the MAP3Ks MAP3K10/MLK2 and MAP3K11/MLK3. May play a role in the regulation of vesicle targeting or fusion. regulation of vesicle targeting or fusion. {ECO:0000269|PubMed:11784851, ECO:0000269|PubMed:15456887, ECO:0000269|PubMed:17584736, ECO:0000269|PubMed:7477268, ECO:0000269|PubMed:7515885, ECO:0000269|PubMed:9712898}.Q6ZMP0THSD41Thrombospondin type-1 domain-containing protein 4#elastic fiber assembly [GO:0048251]*metalloendopeptidase activity [GO:0004222]<extracellular exosome [GO:0070062]; microfibril [GO:0001527]4FUNCTION: Promotes FBN1 matrix assembly. Attenuates TGFB signaling, possibly by accelerating the sequestration of large latent complexes of TGFB or active TGFB by FBN1 microfibril assembly, thereby negatively regulating the expression of TGFB regulatory targets, such as POSTN (By similarity). {ECO:0000250}.Q7Z3E2CC186)Coiled-coil domain-containing protein 186P49356FNTB(Protein farnesyltransferase subunit betaZnegative regulation of cell proliferation [GO:0008285]; phototransduction, visible light [GO:0007603]; positive regulation of cell cycle [GO:0045787]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; protein farnesylation [GO:0018343]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; response to cytokine [GO:0034097]; response to inorganic substance [GO:0010035]; response to organic cyclic compound [GO:0014070]; rhodopsin mediated signaling pathway [GO:0016056]; wound healing [GO:0042060]drug binding [GO:0008144]; farnesyltranstransferase activity [GO:0004311]; isoprenoid binding [GO:0019840]; peptide binding [GO:0042277]; protein farnesyltransferase activity [GO:0004660]; zinc ion binding [GO:0008270]scytosol [GO:0005829]; microtubule associated complex [GO:0005875]; protein farnesyltransferase complex [GO:0005965]FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. {ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009, ECO:0000269|PubMed:8494894}.Q8N8A2ANR44JSerine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit BFUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates.P13196HEM165-aminolevulinate synthase, nonspecific, mitochondrialIcellular lipid metabolic process [GO:0044255]; heme biosynthetic process [GO:0006783]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; porphyrin-containing compound metabolic process [GO:0006778]; protoporphyrinogen IX biosynthetic process [GO:0006782]; small molecule metabolic process [GO:0044281]Z5-aminolevulinate synthase activity [GO:0003870]; pyridoxal phosphate binding [GO:0030170]ocytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]Q9P1Y6PHRF1/PHD and RING finger domain-containing protein 1XmRNA processing [GO:0006397]; transcription from RNA polymerase II promoter [GO:0006366]BRNA polymerase binding [GO:0070063]; zinc ion binding [GO:0008270]O14558HSPB6Heat shock protein beta-6-regulation of muscle contraction [GO:0006937]_protein homodimerization activity [GO:0042803]; structural constituent of eye lens [GO:0005212]Q6IN84MRM1'rRNA methyltransferase 1, mitochondrialUFUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:25074936}.Q9HCM4E41L5Band 4.1-like protein 5SUBCELLULAR LOCATION: Cytoplasm. Cell junction, adherens junction. Note=Associated with the plasma membrane. Colocalizes with CTNNB1, an adherens junction marker (By similarity). {ECO:0000250}.actomyosin structure organization [GO:0031032]; apical constriction [GO:0003383]; axial mesoderm morphogenesis [GO:0048319]; cellular response to transforming growth factor beta stimulus [GO:0071560]; ectoderm development [GO:0007398]; embryonic foregut morphogenesis [GO:0048617]; endoderm development [GO:0007492]; epithelial to mesenchymal transition [GO:0001837]; in utero embryonic development [GO:0001701]; left/right axis specification [GO:0070986]; mesoderm migration involved in gastrulation [GO:0007509]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of protein binding [GO:0032091]; neural plate morphogenesis [GO:0001839]; paraxial mesoderm development [GO:0048339]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of protein binding [GO:0032092]; posttranscriptional regulation of gene expression [GO:0010608]; regulation of establishment of protein localization [GO:0070201]; somite rostral/caudal axis specification [GO:0032525]; substrate-dependent cell migration, cell attachment to substrate [GO:0006931]; unidimensional cell growth [GO:0009826]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extrinsic component of membrane [GO:0019898]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: May contribute to the correct positioning of tight junctions during the establishment of polarity in epithelial cells. {ECO:0000269|PubMed:17920587}.Q13131AAPK195'-AMP-activated protein kinase catalytic subunit alpha-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15866171}. Nucleus {ECO:0000269|PubMed:15866171}. Note=In response to stress, recruited by p53/TP53 to specific promoters.activation of MAPK activity [GO:0000187]; autophagy [GO:0006914]; cell cycle arrest [GO:0007050]; cellular response to ethanol [GO:0071361]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to nutrient levels [GO:0031669]; cellular response to prostaglandin E stimulus [GO:0071380]; cholesterol biosynthetic process [GO:0006695]; cold acclimation [GO:0009631]; fatty acid biosynthetic process [GO:0006633]; fatty acid homeostasis [GO:0055089]; fatty acid oxidation [GO:0019395]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; histone-serine phosphorylation [GO:0035404]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; lipid biosynthetic process [GO:0008610]; negative regulation of apoptotic process [GO:0043066]; negative regulation of glucose import in response to insulin stimulus [GO:2001274]; negative regulation of glucosylceramide biosynthetic process [GO:0046318]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of TOR signaling [GO:0032007]; positive regulation of autophagy [GO:0010508]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of gene expression [GO:0010628]; positive regulation of glycolytic process [GO:0045821]; positive regulation < of skeletal muscle tissue development [GO:0048643]; protein heterooligomerization [GO:0051291]; protein phosphorylation [GO:0006468]; regulation of circadian rhythm [GO:0042752]; regulation of energy homeostasis [GO:2000505]; regulation of peptidyl-serine phosphorylation [GO:0033135]; regulation of transcription, DNA-templated [GO:0006355]; regulation of vesicle-mediated transport [GO:0060627]; response to activity [GO:0014823]; response to caffeine [GO:0031000]; response to camptothecin [GO:1901563]; response to gamma radiation [GO:0010332]; response to hypoxia [GO:0001666]; response to UV [GO:0009411]; rhythmic process [GO:0048511]; signal transduction [GO:0007165]; transcription initiation from RNA polymerase II promoter [GO:0006367]; Wnt signaling pathway [GO:0016055][acetyl-CoA carboxylase] kinase activity [GO:0050405]; [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity [GO:0047322]; AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; chromatin binding [GO:0003682]; histone serine kinase activity [GO:0035174]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; tau-protein kinase activity [GO:0050321]AMP-activated protein kinase complex [GO:0031588]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]w FUNCTION: Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. {ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17486097, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076, ECO:0000269|PubMed:21205641}.O43504LTOR5!Ragulator complex protein LAMTOR5*SUBCELLULAR LOCATION: Cytoplasm. Lysosome.cellular response to amino acid stimulus [GO:0071230]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of GTPase activity [GO:0043547]; positive regulation of TOR signaling [GO:0032008]; protein localization to lysosome [GO:0061462]; regulation of cell size [GO:0008361]; response to virus [GO:0009615]; viral genome replication [GO:0019079]Kcytosol [GO:0005829]; lysosome [GO:0005764]; Ragulator complex [GO:0071986]IFUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication. {ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:22980980}.Q96B49TOM62Mitochondrial import receptor subunit TOM6 homologQSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18331822}.Ymitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]Q9BZQ6EDEM39ER degradation-enhancing alpha-mannosidase-like protein 3cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; glycoprotein ERAD pathway [GO:0097466]; mannose trimming involved in glycoprotein ERAD pathway [GO:1904382]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein folding [GO:0006457]; protein N-linked glycosylation via asparagine [GO:0018279]calcium ion binding [GO:0005509]; glycoprotein endo-alpha-1,2-mannosidase activity [GO:0004569]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571]yendoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]7FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:25092655}.Q8N2G8GHDCGH3 domain-containing proteinLSUBCELLULAR LOCATION: Endoplasmic reticulum. Nucleus envelope {ECO:0000250}.Xendoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; nuclear envelope [GO:0005635]Q9UBU8MO4L1!Mortality factor 4-like protein 1cell proliferation [GO:0008283]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; chromatin silencing [GO:0006342]; double-strand break repair via homologous recombination [GO:0000724]; histone deacetylation [GO:0016575]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; regulation of growth [GO:0040008]; transcription, DNA-templated [GO:0006351]Gchromatin binding [GO:0003682]; protein N-terminus binding [GO:0047485]hNuA4 histone acetyltransferase complex [GO:0035267]; nucleoplasm [GO:0005654]; Sin3 complex [GO:0016580]FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved < in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the mSin3A complex which acts to repress transcription by deacetylation of nucleosomal histones. Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:20332121}.Q6ZTN6AN13D,Ankyrin repeat domain-containing protein 13DSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22298428}. Late endosome {ECO:0000269|PubMed:22298428}. Note=Interaction with EGFR may enhance association with the cell membrane.8late endosome [GO:0005770]; plasma membrane [GO:0005886]7FUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane. {ECO:0000269|PubMed:22298428}.P33993MCM7%DNA replication licensing factor MCM70cell proliferation [GO:0008283]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to xenobiotic stimulus [GO:0071466]; DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA unwinding involved in DNA replication [GO:0006268]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; regulation of phosphorylation [GO:0042325]; response to drug [GO:0042493]fATP binding [GO:0005524]; DNA helicase activity [GO:0003678]; single-stranded DNA binding [GO:0003697]chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; MCM complex [GO:0042555]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for S-phase checkpoint activation upon UV-induced damage. {ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:15538388, ECO:0000269|PubMed:9305914}.Q99707METHMethionine synthaseRcellular nitrogen compound metabolic process [GO:0034641]; cellular response to nitric oxide [GO:0071732]; cobalamin metabolic process [GO:0009235]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; nervous system development [GO:0007399]; pteridine-containing compound metabolic process [GO:0042558]; response to axon injury [GO:0048678]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]; xenobiotic metabolic process [GO:0006805]cobalamin binding [GO:0031419]; methionine synthase activity [GO:0008705]; S-adenosylmethionine-homocysteine S-methyltransferase activity [GO:0008898]; zinc ion binding [GO:0008270]FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity). {ECO:0000250}.O14497ARI1A0AT-rich interactive domain-containing protein 1AbSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:11318604}.androgen receptor signaling pathway [GO:0030521]; ATP-dependent chromatin remodeling [GO:0043044]; cardiac chamber development [GO:0003205]; cardiac muscle cell differentiation [GO:0055007]; chromatin-mediated maintenance of transcription [GO:0048096]; chromatin remodeling [GO:0006338]; forebrain development [GO:0030900]; glucocorticoid receptor signaling pathway [GO:0042921]; intracellular estrogen receptor signaling pathway [GO:0030520]; maintenance of chromatin silencing [GO:0006344]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neural tube closure [GO:0001843]; nucleosome disassembly [GO:0006337]; nucleosome mobilization [GO:0042766]; optic cup formation involved in camera-type eye development [GO:0003408]; placenta blood vessel development [GO:0060674]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; toxin transport [GO:1901998]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; ligand-dependent nuclear receptor binding [GO:0016922]; transcription coactivator activity [GO:0003713]nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.Q9BQK8LPIN3Phosphatidate phosphatase LPIN3dephosphorylation [GO:0016311]; fatty acid catabolic process [GO:0009062]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid metabolic process [GO:0006644]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]`phosphatidate phosphatase activity [GO:0008195]; transcription coactivator activity [GO:0003713]Aendoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]FUNCTION: Regulates fatty acid metabolism. Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis (By similarity). {ECO:0000250}.Q00587BORG5Cdc42 effector protein 1SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:10430899}; Peripheral membran< e protein {ECO:0000269|PubMed:10430899}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10430899}.actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]FUNCTION: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. {ECO:0000269|PubMed:10430899}.P15291B4GT1 Beta-1,4-galactosyltransferase 1}SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:1714903}.; SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:1714903}.; SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1: Secreted. Note=Soluble form found in body fluids.acute inflammatory response [GO:0002526]; angiogenesis involved in wound healing [GO:0060055]; binding of sperm to zona pellucida [GO:0007339]; branching morphogenesis of an epithelial tube [GO:0048754]; carbohydrate metabolic process [GO:0005975]; cell adhesion [GO:0007155]; cellular protein metabolic process [GO:0044267]; development of secondary sexual characteristics [GO:0045136]; epithelial cell development [GO:0002064]; extracellular matrix organization [GO:0030198]; galactose metabolic process [GO:0006012]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; lactose biosynthetic process [GO:0005989]; leukocyte migration [GO:0050900]; mammary gland development [GO:0030879]; multicellular organism reproduction [GO:0032504]; negative regulation of cell proliferation [GO:0008285]; Notch signaling pathway [GO:0007219]; oligosaccharide biosynthetic process [GO:0009312]; penetration of zona pellucida [GO:0007341]; positive regulation of apoptotic process involved in mammary gland involution [GO:0060058]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]; regulation of acrosome reaction [GO:0060046]; regulation of cellular component movement [GO:0051270]; single fertilization [GO:0007338]; small molecule metabolic process [GO:0044281]alpha-tubulin binding [GO:0043014]; beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; beta-tubulin binding [GO:0048487]; galactosyltransferase activity [GO:0008378]; lactose synthase activity [GO:0004461]; manganese ion binding [GO:0030145]; N-acetyllactosamine synthase activity [GO:0003945]; protein homodimerization activity [GO:0042803]; UDP-galactosyltransferase activity [GO:0035250]basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; desmosome [GO:0030057]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; glycocalyx [GO:0030112]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]-FUNCTION: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.; FUNCTION: The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.Q6WCQ1MPRIP*Myosin phosphatase Rho-interacting proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14506264, ECO:0000269|PubMed:16257966}. Note=Colocalizes with F-actin.Tactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells. {ECO:0000250|UniProtKB:P97434, ECO:0000269|PubMed:15545284, ECO:0000269|PubMed:16257966}.P24385CCND1G1/S-specific cyclin-D13SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9106657}. Cytoplasm {ECO:0000269|PubMed:9106657}. Membrane {ECO:0000269|PubMed:9106657}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members. {ECO:0000250}.canonical Wnt signaling pathway [GO:0060070]; cell division [GO:0051301]; cellular response to DNA damage stimulus [GO:0006974]; chromatin organization [GO:0006325]; endoplasmic reticulum unfolded protein response [GO:0030968]; fat cell differentiation [GO:0045444]; G1/S transition of mitotic cell cycle [GO:0000082]; lactation [GO:0007595]; Leydig cell differentiation [GO:0033327]; liver development [GO:0001889]; mammary gland alveolus development [GO:0060749]; mammary gland epithelial cell proliferation [GO:0033598]; mitotic cell cycle [GO:0000278]; mitotic G1 DNA damage checkpoint [GO:0031571]; negative regulation of cell cycle arrest [GO:0071157]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; Notch signaling pathway [GO:0007219]; organ regeneration [GO:0031100]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of mammary gland epithelial cell proliferation [GO:0033601]; positive regulation of protein phosphorylation [GO:0001934]; re-entry into mitotic cell cycle [GO:0000320]; response to calcium ion [GO:0051592]; response to corticosterone [GO:0051412]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to iron ion [GO:0010039]; response to magnesium ion [GO:0032026]; response to organonitrogen compound [GO:0010243]; response to UV-A [GO:0070141]; response to vitamin E [GO:0033197]; response to X-ray [GO:0010165]; transcription, DNA-templated [GO:0006351]hcyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; proline-rich region binding [GO:0070064]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]bicellular tight junction [GO:0005923]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytosol [GO:0005829]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]7FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F comp< lex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:9106657}.O75044SRGP2)SLIT-ROBO Rho GTPase-activating protein 2G-protein modulator(PC00022)SUBCELLULAR LOCATION: Cell membrane. Cell projection, dendritic spine. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Cell projection, lamellipodium. Cytoplasmic vesicle, phagosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates from nucleus to cytoplasm during development. {ECO:0000250}.actin filament severing [GO:0051014]; axon guidance [GO:0007411]; dendritic spine development [GO:0060996]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; filopodium assembly [GO:0046847]; lamellipodium assembly involved in ameboidal cell migration [GO:0003363]; negative regulation of neuron migration [GO:2001223]; neuron projection morphogenesis [GO:0048812]; positive regulation of GTPase activity [GO:0043547]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; substrate adhesion-dependent cell spreading [GO:0034446]wGTPase activator activity [GO:0005096]; protein homodimerization activity [GO:0042803]; Rac GTPase binding [GO:0048365] cell junction [GO:0030054]; cytosol [GO:0005829]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]FUNCTION: RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia. {ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21148482, ECO:0000269|PubMed:22559944}.O14662STX16 Syntaxin-16SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein.; SUBCELLULAR LOCATION: Isoform C: Cytoplasm.Golgi ribbon formation [GO:0090161]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]FUNCTION: SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.O14791APOL1Apolipoprotein L1^chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; cholesterol metabolic process [GO:0008203]; cytolysis [GO:0019835]; innate immune response [GO:0045087]; killing of cells of other organism [GO:0031640]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; receptor-mediated endocytosis [GO:0006898]Bchloride channel activity [GO:0005254]; lipid binding [GO:0008289]blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intrinsic component of membrane [GO:0031224]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver.Q30201HFE"Hereditary hemochromatosis proteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9465039}; Single-pass type I membrane protein {ECO:0000305|PubMed:8696333}.acute-phase response [GO:0006953]; BMP signaling pathway [GO:0030509]; cellular iron ion homeostasis [GO:0006879]; cellular response to iron ion starvation [GO:0010106]; female pregnancy [GO:0007565]; hormone biosynthetic process [GO:0042446]; immune response [GO:0006955]; iron ion import into cell [GO:0097459]; liver regeneration [GO:0097421]; multicellular organismal iron ion homeostasis [GO:0060586]; negative regulation of antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:1904283]; negative regulation of CD8-positive, alpha-beta T cell activation [GO:2001186]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000059]; negative regulation of receptor binding [GO:1900121]; negative regulation of T cell antigen processing and presentation [GO:0002626]; negative regulation of T cell cytokine production [GO:0002725]; positive regulation of gene expression [GO:0010628]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; protein complex assembly [GO:0006461]; response to iron ion starvation [GO:1990641]beta-2-microglobulin binding [GO:0030881]; co-receptor binding [GO:0039706]; receptor binding [GO:0005102]; transferrin receptor binding [GO:1990459]apical part of cell [GO:0045177]; basal part of cell [GO:0045178]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; HFE-transferrin receptor complex [GO:1990712]; integral component of plasma membrane [GO:0005887]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; terminal web [GO:1990357]FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. {ECO:0000269|PubMed:9465039}.P35237SPB6 Serpin B6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14670919, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8486644}.cellular response to osmotic stress [GO:0071470]; negative regulation of endopeptidase activity [GO:0010951]; sensory perception of sound [GO:0007605]Xprotease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; protein complex [GO:0043234]FUNCTION: May be involved in the regulation of serine proteinases present in the brain or extravasated from the blood (By similarity). Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an important role in the inner< ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss. {ECO:0000250, ECO:0000269|PubMed:10068683, ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8136380, ECO:0000269|PubMed:8415716}.Q5VUE5CA053Uncharacterized protein C1orf53Q02224CENPECentromere-associated protein ESUBCELLULAR LOCATION: Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Associates with kinetochores during congression (as early as prometaphase), relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; blood coagulation [GO:0007596]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; kinetochore assembly [GO:0051382]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic metaphase plate congression [GO:0007080]; multicellular organismal development [GO:0007275]; positive regulation of protein kinase activity [GO:0045860]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; small GTPase mediated signal transduction [GO:0007264]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; kinetochore binding [GO:0043515]; microtubule motor activity [GO:0003777]chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; nucleus [GO:0005634]FUNCTION: Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end-directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule-dependent motor activity of CENPE serves to power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1, MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle. {ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:7889940}.P52789HXK2 Hexokinase-2SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}. Note=Its hydrophobic N-terminal sequence may be involved in membrane binding. {ECO:0000250}.apoptotic mitochondrial changes [GO:0008637]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; cellular glucose homeostasis [GO:0001678]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glucose transport [GO:0015758]; glycolytic process [GO:0006096]; hexose transport [GO:0008645]; lactation [GO:0007595]; negative regulation of mitochondrial membrane permeability [GO:0035795]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; regulation of glucose import [GO:0046324]; response to ischemia [GO:0002931]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]Vcytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]O75970MPDZMultiple PDZ domain proteinSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection, dendrite. Cell junction, tight junction. Cell junction, synapse. Cell junction, synapse, synaptosome. Note=Associated with membranes. Colocalizes with HTR2C on the apical membrane of epithelial choroid plexus cells. Highly enriched in postsynaptic densities (PSD). Localized to punctae on dendrites of hippocampal neurons and colocalizes with the synaptic marker DLG4. Localized mainly in the Schmidt-Lanterman incisures of myelinating Schwann cells (By similarity). In the retina, localizes to the sub-apical region adjacent to the adherens junction complex at the outer limiting membrane. Enriched at the tight junctions of epithelial cells. Association to the tight junctions depends on CXADR. {ECO:0000250}.6cell adhesion [GO:0007155]; viral process [GO:0016032]7apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Schmidt-Lanterman incisure [GO:0043220]4FUNCTION: Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. {ECO:0000250, ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:15312654}.Q9UHR4BI2L1KBrain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19366662}. Note=Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; insulin receptor signaling pathway [GO:0008286]; plasma membrane organization [GO:0007009]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of actin filament polymerization [GO:0030838]; regulation of insulin receptor signaling pathway [GO:0046626]; response to bacterium [GO:0009617]Tcytoskeletal adaptor activity [GO:0008093]; proline-rich region binding [GO:0070064]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:22921828}.Q16720AT2B3-Plasma membrane calcium-transporting ATPase 3blood coagulation [GO:0007596]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]; transport [GO:0006810]extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]P19105ML12A!Myosin regulatory light chain 12Aaxon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; muscle contraction [GO:0006936]; platelet aggregation [GO:0070527]; protein targeting to plasma membrane [GO:0072661]; regulation of cell shape [GO:0008360]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myosin II complex [GO:0016460]; stress fiber [GO:0001725]; Z disc [GO:0030018]FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). {ECO:0000250}.P51965UB2E1"Ubiquitin-conjugating enzyme E2 E1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18845142}.fanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cytokine-mediated signaling pathway [GO:0019221]; histon< e H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; ISG15-protein conjugation [GO:0032020]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; ubiquitin-dependent protein catabolic process [GO:0006511]ATP binding [GO:0005524]; ISG15 transferase activity [GO:0042296]; ligase activity [GO:0016874]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]kcytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]gFUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination. {ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386}.P0DI83NARR(Ras-related protein Rab-34, isoform NARRSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21586586}. Nucleus, nucleolus {ECO:0000269|PubMed:21586586}. Note=Colocalizes with rDNA clusters.Q8IZ07AN13A,Ankyrin repeat domain-containing protein 13AQ96RK0CICProtein capicua homologlung alveolus development [GO:0048286]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]mFUNCTION: Transcriptional repressor which may play a role in development of the central nervous system (CNS).Q96CM8ACSF22Acyl-CoA synthetase family member 2, mitochondrial6ATP binding [GO:0005524]; ligase activity [GO:0016874]FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation. {ECO:0000269|PubMed:16380219, ECO:0000269|PubMed:17762044}.P35908K22E)Keratin, type II cytoskeletal 2 epidermalepidermis development [GO:0008544]; keratinization [GO:0031424]; keratinocyte activation [GO:0032980]; keratinocyte migration [GO:0051546]; keratinocyte proliferation [GO:0043616]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Probably contributes to terminal cornification. Associated with keratinocyte activation, proliferation and keratinization. {ECO:0000269|PubMed:12598329, ECO:0000269|PubMed:1380918}.P78346RPP30"Ribonuclease P protein subunit p30Fpoly(A) RNA binding [GO:0044822]; ribonuclease P activity [GO:0004526]O15382BCAT29Branched-chain-amino-acid aminotransferase, mitochondrial\SUBCELLULAR LOCATION: Isoform A: Mitochondrion.; SUBCELLULAR LOCATION: Isoform B: Cytoplasm.branched-chain amino acid biosynthetic process [GO:0009082]; branched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; isoleucine catabolic process [GO:0006550]; leucine metabolic process [GO:0006551]; regulation of hormone levels [GO:0010817]; small molecule metabolic process [GO:0044281]; valine metabolic process [GO:0006573]FUNCTION: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.Q9BQC6RT63#Ribosomal protein 63, mitochondrial&mitochondrial translation [GO:0032543]#mitochondrial ribosome [GO:0005761]Q8N653LZTR1/Leucine-zipper-like transcriptional regulator 1hanatomical structure morphogenesis [GO:0009653]; regulation of transcription, DNA-templated [GO:0006355][FUNCTION: Probable transcriptional regulator that may play a crucial role in embryogenesis.Q13075BIRC1+Baculoviral IAP repeat-containing protein 1Linflammatory response [GO:0006954]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; protein ubiquitination [GO:0016567]; regulation of signal transduction [GO:0009966]; response to amino acid [GO:0043200]; response to axon injury [GO:0048678]ATP binding [GO:0005524]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; ubiquitin-protein transferase activity [GO:0004842]basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perikaryon [GO:0043204]FUNCTION: Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.; FUNCTION: Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila.Q9UBS3DNJB9!DnaJ homolog subfamily B member 9cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; IRE1-mediated unfolded protein response [GO:0036498]&misfolded protein binding [GO:0051787]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein. {ECO:0000269|PubMed:18400946}.Q8WXA9SREK13Splicing regulatory glutamine/lysine-rich protein 1FUNCTION: Participates in the regulation of alternative splicing by modulating the activity of other splice facors. Inhibits the splicing activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of SFRS3 (By similarity). {ECO:0000250}.Q3B726RPA43+DNA-directed RNA polymerase I subunit RPA431DNA-directed RNA polymerase activity [GO:0003899]DNA-directed RNA polymerase I complex [GO:0005736]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634];FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Through its association with RRN3/TIF-IA may be involved in recruitment of Pol I< to rDNA promoters.Q96GX2A7L3B!Putative ataxin-7-like protein 3BP17302CXA1Gap junction alpha-1 proteinSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22411987}; Multi-pass membrane protein {ECO:0000269|PubMed:22411987}. Cell junction, gap junction {ECO:0000269|PubMed:22411987}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}.Iapoptotic process [GO:0006915]; ATP transport [GO:0015867]; atrial cardiac muscle cell action potential [GO:0086014]; cell-cell signaling [GO:0007267]; cell communication by electrical coupling [GO:0010644]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular response to mechanical stimulus [GO:0071260]; chronic inflammatory response [GO:0002544]; endothelium development [GO:0003158]; gap junction assembly [GO:0016264]; heart development [GO:0007507]; ion transmembrane transport [GO:0034220]; membrane organization [GO:0061024]; muscle contraction [GO:0006936]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of DNA biosynthetic process [GO:2000279]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of wound healing [GO:0061045]; neuron projection morphogenesis [GO:0048812]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of cell communication by chemical coupling [GO:0010652]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of glomerular filtration [GO:0003104]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of vasoconstriction [GO:0045907]; positive regulation of vasodilation [GO:0045909]; protein oligomerization [GO:0051259]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of calcium ion transport [GO:0051924]; response to fluid shear stress [GO:0034405]; response to glucose [GO:0009749]; response to peptide hormone [GO:0043434]; response to pH [GO:0009268]; signal transduction [GO:0007165]; transport [GO:0006810]; vascular transport [GO:0010232]Igap junction channel activity [GO:0005243]; gap junction channel activity involved in cardiac conduction electrical coupling [GO:0086075]; gap junction channel activity involved in cell communication by electrical coupling [GO:1903763]; ion transmembrane transporter activity [GO:0015075]; signal transducer activity [GO:0004871]Tconnexon complex [GO:0005922]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; gap junction [GO:0005921]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle membrane [GO:0030660]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; intercalated disc [GO:0014704]; lysosome [GO:0005764]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]wFUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). {ECO:0000250}.Q9H0A0NAT10N-acetyltransferase 10SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:19303003}. Note=Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase.eATP binding [GO:0005524]; N-acetyltransferase activity [GO:0008080]; poly(A) RNA binding [GO:0044822]SFUNCTION: Has protein acetyltransferase activity in vitro. Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division. {ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19303003}.P11310ACADM;Medium-chain specific acyl-CoA dehydrogenase, mitochondrialcarnitine biosynthetic process [GO:0045329]; carnitine metabolic process, CoA-linked [GO:0019254]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]; medium-chain fatty acid catabolic process [GO:0051793]; medium-chain fatty acid metabolic process [GO:0051791]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]tacyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; medium-chain-acyl-CoA dehydrogenase activity [GO:0070991]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]axon [GO:0030424]; extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]DFUNCTION: This enzyme is specific for acyl chain lengths of 4 to 16.O94763RMP*Unconventional prefoldin RPB5 interactor 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cell projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion. cellular response to growth factor stimulus [GO:0071363]; cellular response to steroid hormone stimulus [GO:0071383]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of phosphatase activity [GO:0010923]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of cell growth [GO:0001558]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to virus [GO:0009615]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; phosphatase inhibitor activity [GO:0019212]; protein phosphatase inhibitor activity [GO:0004864]; RNA polymerase II transcription corepressor activity [GO:0001106]cytoplasm [GO:0005737]; dendrite [GO:0030425]; DNA-directed RNA polymerase II, core complex [GO:0005665]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFD< s and proteins with roles in transcription and ubiquitination.Q96C11FGGY2FGGY carbohydrate kinase domain-containing proteinScarbohydrate phosphorylation [GO:0046835]; neuron cellular homeostasis [GO:0070050]akinase activity [GO:0016301]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]Q9GZU8F192AProtein FAM192AQ7Z3D6CN159(UPF0317 protein C14orf159, mitochondrialP15927RFA2$Replication protein A 32 kDa subunitSUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner.base-excision repair [GO:0006284]; cellular response to heat [GO:0034605]; DNA damage response, detection of DNA damage [GO:0042769]; DNA recombinase assembly [GO:0000730]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; G1/S transition of mitotic cell cycle [GO:0000082]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; mitotic G1 DNA damage checkpoint [GO:0031571]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA gap filling [GO:0006297]; regulation of cellular response to heat [GO:1900034]; regulation of DNA damage checkpoint [GO:2000001]; regulation of double-strand break repair via homologous recombination [GO:0010569]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]damaged DNA binding [GO:0003684]; enzyme binding [GO:0019899]; protein phosphatase binding [GO:0019903]; single-stranded DNA binding [GO:0003697]; ubiquitin protein ligase binding [GO:0031625]chromatin [GO:0000785]; DNA replication factor A complex [GO:0005662]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]YFUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.P55055NR1H2Oxysterols receptor LXR-betaESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.Ocellular lipid metabolic process [GO:0044255]; cholesterol homeostasis [GO:0042632]; gene expression [GO:0010467]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of interferon-gamma-mediated signaling pathway [GO:0060336]; negative regulation of lipid transport [GO:0032369]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; negative regulation of pinocytosis [GO:0048550]; negative regulation of proteolysis [GO:0045861]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol transport [GO:0032376]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of high-density lipoprotein particle assembly [GO:0090108]; positive regulation of lipid storage [GO:0010884]; positive regulation of lipoprotein lipase activity [GO:0051006]; positive regulation of pancreatic juice secretion [GO:0090187]; positive regulation of secretion of lysosomal enzymes [GO:0090340]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of cholesterol homeostasis [GO:2000188]; retinoic acid receptor signaling pathway [GO:0048384]; transcription initiation from RNA polymerase II promoter [GO:0006367]apolipoprotein A-I receptor binding [GO:0034191]; ATPase binding [GO:0051117]; DNA binding [GO:0003677]; ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0004879]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity [GO:0001133]; steroid hormone receptor activity [GO:0003707]; zinc ion binding [GO:0008270]FUNCTION: Nuclear receptor. Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:25661920}.Q9H6Q4NARFL,Cytosolic Fe-S cluster assembly factor NARFLhematopoietic progenitor cell differentiation [GO:0002244]; iron-sulfur cluster assembly [GO:0016226]; oxygen homeostasis [GO:0032364]; regulation of transcription, DNA-templated [GO:0006355]; response to hypoxia [GO:0001666]; small molecule metabolic process [GO:0044281]w4 iron, 4 sulfur cluster binding [GO:0051539]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872].CIA complex [GO:0097361]; cytosol [GO:0005829]eFUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect. {ECO:0000269|PubMed:16956324, ECO:0000269|PubMed:18270200}.O75400PR40A'Pre-mRNA-processing factor 40 homolog ASUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000269|PubMed:16391387}. Note=Colocalizes with AKAP8L in the nuclear matrix. {ECO:0000250}.cell cycle [GO:0007049]; cell division [GO:0051301]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; mRNA processing [GO:0006397]; regulation of cell shape [GO:0008360]; regulation of cytokinesis [GO:0032465]; RNA splicing [GO:0008380]cytoplasm [GO:0005737]; membrane [G< O:0016020]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. {ECO:0000250, ECO:0000269|PubMed:21834987}.Q96L92SNX27Sorting nexin-27SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein. Cytoplasm, cytosol. Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products. endosomal transport [GO:0016197]; establishment of natural killer cell polarity [GO:0001770]; intracellular protein transport [GO:0006886]; response to drug [GO:0042493]; retrograde transport, endosome to plasma membrane [GO:1990126]; signal transduction [GO:0007165]5phosphatidylinositol-3-phosphate binding [GO:0032266]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; immunological synapse [GO:0001772]; nucleoplasm [GO:0005654]oFUNCTION: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes. {ECO:0000269|PubMed:17351151, ECO:0000269|PubMed:20733053, ECO:0000269|PubMed:21300787, ECO:0000269|PubMed:21303929, ECO:0000269|PubMed:21602791, ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:22411990, ECO:0000269|PubMed:23563491}.Q8WYP3RIN2Ras and Rab interactor 2endocytosis [GO:0006897]; positive regulation of GTPase activity [GO:0043547]; regulation of catalytic activity [GO:0050790]; small GTPase mediated signal transduction [GO:0007264]GTPase activator activity [GO:0005096]; GTPase regulator activity [GO:0030695]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]-FUNCTION: Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP. {ECO:0000269|PubMed:11733506}.Q9NXS2QPCTL0Glutaminyl-peptide cyclotransferase-like proteinSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18486145}; Single-pass type I membrane protein {ECO:0000269|PubMed:18486145}.gpeptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase [GO:0017186]Xglutaminyl-peptide cyclotransferase activity [GO:0016603]; zinc ion binding [GO:0008270]FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. {ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}.Q13671RIN1Ras and Rab interactor 1Ras/RIN1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11784866}. Membrane {ECO:0000269|PubMed:11784866}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11784866}. Note=Some amount is membrane-associated.associative learning [GO:0008306]; endocytosis [GO:0006897]; memory [GO:0007613]; negative regulation of synaptic plasticity [GO:0031914]; signal transduction [GO:0007165]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]kFUNCTION: Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis. {ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9208849}.Q8IWL3HSC20<Iron-sulfur cluster co-chaperone protein HscB, mitochondrialkSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20668094}. Mitochondrion {ECO:0000269|PubMed:20668094}.miron-sulfur cluster assembly [GO:0016226]; protein folding [GO:0006457]; protein oligomerization [GO:0051259]>chaperone binding [GO:0051087]; metal ion binding [GO:0046872]icentrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]pFUNCTION: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. {ECO:0000269|PubMed:20668094}.Q6NUQ1RINT1RAD50-interacting protein 1]SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein.cell cycle [GO:0007049]; Golgi vesicle transport [GO:0048193]; protein transport [GO:0015031]; regulation of ER to Golgi vesicle-mediated transport [GO:0060628]; regulation of signal transduction involved in mitotic G2 DNA damage checkpoint [GO:1902504]kDsl1p complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]FUNCTION: Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control (PubMed:11096100). Essential for telomere length control (PubMed:16600870). {ECO:0000269|PubMed:11096100, ECO:0000269|PubMed:16600870, ECO:0000305}.P49116NR2C2-Nuclear receptor subfamily 2 group C member 2SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:15302918}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cell differentiation [GO:0030154]; cerebellum development [GO:0021549]; gene expression [GO:0010467]; meiotic cell cycle [GO:0051321]; nervous system development [GO:0007399]; p38MAPK cascade [GO:0038066]; positive regulation of behavior [GO:0048520]; positive regulation of embryonic development [GO:0040019]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; spermatogenesis [GO:0007283]; transcription initiation from RNA polymerase II promoter [GO:0006367]Fprotein heterodimerization activity [GO:0046982]; receptor activity [GO:0004872]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; steroid hormone receptor activity [GO:0003707]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]^FUNCTION: Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consens< us sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior (By similarity). Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation. {ECO:0000250, ECO:0000269|PubMed:10347174, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:17974920, ECO:0000269|PubMed:7779113, ECO:0000269|PubMed:9556573}.O15514RPB4+DNA-directed RNA polymerase II subunit RPB47-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; mRNA export from nucleus in response to heat stress [GO:0031990]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of translational initiation [GO:0045948]; positive regulation of viral transcription [GO:0050434]; recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex [GO:0034402]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]DNA-directed RNA polymerase activity [GO:0003899]; nucleotide binding [GO:0000166]; translation initiation factor binding [GO:0031369]cytoplasmic mRNA processing body [GO:0000932]; DNA-directed RNA polymerase II, core complex [GO:0005665]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). {ECO:0000250}.Q6IA86ELP2Elongator complex protein 2chromatin organization [GO:0006325]; regulation of JAK-STAT cascade [GO:0046425]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription elongation from RNA polymerase II promoter [GO:0006368]cytoplasm [GO:0005737]; Elongator holoenzyme complex [GO:0033588]; histone acetyltransferase complex [GO:0000123]; transcription elongation factor complex [GO:0008023]FUNCTION: Regulates the ligand-dependent activation of STAT3. {ECO:0000250}.; FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576}.Q8N9B5JMY*Junction-mediating and -regulatory proteinwSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19287377}. Note=Localizes to the nucleus in most cell types. Accumulates in nucleus under DNA damage conditions, increasing p53/TP53 transcription response and reducing its influence on cell motility (By similarity). In primary neutrophils, it colocalizes with actin filaments at the leading edge and is excluded from the nucleus. Localization correlates with motility, because it moves from the nucleus to the cytoplasmic compartment when cells are differentiated from nonmotile cells into highly motile neutrophil-like cells. {ECO:0000250}.de novo' actin filament nucleation [GO:0070060]; actin polymerization-dependent cell motility [GO:0070358]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cell cycle arrest [GO:0007050]; DNA repair [GO:0006281]; positive regulation of apoptotic process [GO:0043065]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; regulation of transcription from RNA polymerase II promoter [GO:0006357]cell junction [GO:0030054]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location (By similarity). {ECO:0000250}.Q9UID3VPS516Vacuolar protein sorting-associated protein 51 homologJSUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20685960}. Recycling endosome {ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex (PubMed:25799061). {ECO:0000269|PubMed:25799061}.autophagy [GO:0006914]; endocytic recycling [GO:0032456]; lipid transport [GO:0006869]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]EARP complex [GO:1990745]; GARP complex [GO:0000938]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; recycling endosome [GO:0055037]>FUNCTION: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN (PubMed:20685960). Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061). {ECO:0000269|PubMed:20685960, ECO:0000269|PubMed:25799061}.Q9H9Y6RPA2*DNA-directed RNA polymerase I subunit RPA2GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11250903}.embryo implantation [GO:0007566]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleologenesis [GO:0017126]; regulation of gene expression, epigenetic [GO:0040029]; rRNA transcription [GO:0009303]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; ribonucleoside binding [GO:0032549]|cytoplasm [GO:0005737]; DNA-directed RNA polymerase I complex [GO< :0005736]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]<FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}.P15586GNSN-acetylglucosamine-6-sulfatase sulfatases(7)carbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; small molecule metabolic process [GO:0044281]metal ion binding [GO:0046872]; N-acetylglucosamine-6-sulfatase activity [GO:0008449]; sulfuric ester hydrolase activity [GO:0008484]@extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]P61812TGFB2!Transforming growth factor beta-2activation of protein kinase activity [GO:0032147]; angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; blood vessel remodeling [GO:0001974]; cardiac epithelial to mesenchymal transition [GO:0060317]; cardiac muscle cell proliferation [GO:0060038]; cardioblast differentiation [GO:0010002]; cartilage condensation [GO:0001502]; catagen [GO:0042637]; cell-cell junction organization [GO:0045216]; cell-cell signaling [GO:0007267]; cell cycle arrest [GO:0007050]; cell death [GO:0008219]; cell development [GO:0048468]; cell growth [GO:0016049]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; cell proliferation [GO:0008283]; collagen fibril organization [GO:0030199]; dopamine biosynthetic process [GO:0042416]; embryo development [GO:0009790]; embryonic digestive tract development [GO:0048566]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix organization [GO:0030198]; extrinsic apoptotic signaling pathway [GO:0097191]; eye development [GO:0001654]; face morphogenesis [GO:0060325]; generation of neurons [GO:0048699]; glial cell migration [GO:0008347]; hair follicle development [GO:0001942]; hair follicle morphogenesis [GO:0031069]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; heart valve morphogenesis [GO:0003179]; hemopoiesis [GO:0030097]; negative regulation of alkaline phosphatase activity [GO:0010693]; negative regulation of cartilage development [GO:0061037]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of immune response [GO:0050777]; negative regulation of macrophage cytokine production [GO:0010936]; neuron development [GO:0048666]; neuron fate commitment [GO:0048663]; neutrophil chemotaxis [GO:0030593]; odontogenesis [GO:0042476]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of activation-induced cell death of T cells [GO:0070237]; positive regulation of cardioblast differentiation [GO:0051891]; positive regulation of catagen [GO:0051795]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell division [GO:0051781]; positive regulation of cell growth [GO:0030307]; positive regulation of cell proliferation [GO:0008284]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of gene expression [GO:0010628]; positive regulation of heart contraction [GO:0045823]; positive regulation of immune response [GO:0050778]; positive regulation of integrin biosynthetic process [GO:0045726]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of ossification [GO:0045778]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein secretion [GO:0050714]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein phosphorylation [GO:0006468]; regulation of extracellular matrix organization [GO:1903053]; regulation of transforming growth factor beta2 production [GO:0032909]; response to drug [GO:0042493]; response to hypoxia [GO:0001666]; response to progesterone [GO:0032570]; response to wounding [GO:0009611]; salivary gland morphogenesis [GO:0007435]; signal transduction by protein phosphorylation [GO:0023014]; SMAD protein import into nucleus [GO:0007184]; SMAD protein signal transduction [GO:0060395]; somatic stem cell division [GO:0048103]; transforming growth factor beta receptor signaling pathway [GO:0007179]; uterine wall breakdown [GO:0042704]; wound healing [GO:0042060]beta-amyloid binding [GO:0001540]; cytokine activity [GO:0005125]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; receptor signaling protein serine/threonine kinase activity [GO:0004702]; transforming growth factor beta receptor binding [GO:0005160]; type III transforming growth factor beta receptor binding [GO:0034714]; type II transforming growth factor beta receptor binding [GO:0005114]axon [GO:0030424]; endosome [GO:0005768]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; platelet alpha granule lumen [GO:0031093]VFUNCTION: TGF-beta 2 has suppressive effects on interleukin-2 dependent T-cell growth.Q13257MD2L11Mitotic spindle assembly checkpoint protein MAD2ASUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Note=Recruited by MAD1L1 to unattached kinetochores (Probable). Recruited to the nuclear pore complex by TPR during interphase. Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2. Kinetochore association is repressed by UBD. {ECO:0000305}.vanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of APC-Cdc20 complex activity [GO:0060564]; negative regulation of apoptotic process [GO:0043066]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small GTPase mediated signal transduction [GO:0007264]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle pole [GO:0000922]FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:10700282, ECO:0000269|PubMed:11804586, ECO:0000269|PubMed:15024386}.P02042HBD< Hemoglobin subunit deltablood coagulation [GO:0007596]Wblood microparticle [GO:0072562]; cytosol [GO:0005829]; hemoglobin complex [GO:0005833]O14908GIPC1#PDZ domain-containing protein GIPC1GSUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.endothelial cell migration [GO:0043542]; glutamate secretion [GO:0014047]; G-protein coupled receptor signaling pathway [GO:0007186]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; positive regulation of cytokinesis [GO:0032467]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; protein targeting [GO:0006605]; regulation of protein stability [GO:0031647]; regulation of synaptic plasticity [GO:0048167]; synaptic transmission [GO:0007268]actin binding [GO:0003779]; myosin binding [GO:0017022]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]ibrush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; synaptic vesicle [GO:0008021]; vesicle membrane [GO:0012506]8FUNCTION: May be involved in G protein-linked signaling.Q0IIM8TBC8BTBC1 domain family member 8BP23368MAOM)NAD-dependent malic enzyme, mitochondrialXmalate metabolic process [GO:0006108]; regulation of NADP metabolic process [GO:1902031]electron carrier activity [GO:0009055]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malic enzyme activity [GO:0004470]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; oxaloacetate decarboxylase activity [GO:0008948]tintracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]Q9ULW3ABT1"Activator of basal transcription 1NSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.pendonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000472]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; small-subunit processome assembly [GO:0034462]; spinal cord motor neuron differentiation [GO:0021522]; transcription from RNA polymerase II promoter [GO:0006366]DNA binding [GO:0003677]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]Wnucleolus [GO:0005730]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Could be a novel TATA-binding protein (TBP) which can function as a basal transcription activator. Can act as a regulator of basal transcription for class II genes (By similarity). {ECO:0000250}.Q9Y6V0PCLOProtein piccoloSUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250}. Note=Concentrated at the presynaptic side of synaptic junctions. {ECO:0000250}.cAMP-mediated signaling [GO:0019933]; cytoskeleton organization [GO:0007010]; insulin secretion [GO:0030073]; regulation of exocytosis [GO:0017157]; synapse assembly [GO:0007416]; synaptic vesicle exocytosis [GO:0016079]tcalcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; profilin binding [GO:0005522]cell junction [GO:0030054]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; postsynaptic density [GO:0014069]; presynaptic cytoskeletal matrix assembled at active zones [GO:0048788]; synapse [GO:0045202]FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking. {ECO:0000250|UniProtKB:Q9QYX7}.O00461GOLI4!Golgi integral membrane protein 4SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Note=Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and distal compartments like endosome.cis-Golgi network [GO:0005801]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi lumen [GO:0005796]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. {ECO:0000269|PubMed:15331763}.P98170XIAP E3 ubiquitin-protein ligase XIAPVSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=TLE3 promotes its nuclear localization. apoptotic process [GO:0006915]; cellular response to DNA damage stimulus [GO:0006974]; copper ion homeostasis [GO:0055070]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein linear polyubiquitination [GO:1902530]; positive regulation of protein ubiquitination [GO:0031398]; programmed cell death [GO:0012501]; protein ubiquitination [GO:0016567]; regulation of BMP signaling pathway [GO:0030510]; regulation of cell proliferation [GO:0042127]; regulation of inflammatory response [GO:0050727]; regulation of innate immune response [GO:0045088]; regulation of nucleotide-binding oligomerization domain containing signaling pathway [GO:0070424]; Wnt signaling pathway [GO:0016055]cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; ligase activity [GO:0016874]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270], FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptio< nal coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. {ECO:0000269|PubMed:11447297, ECO:0000269|PubMed:12121969, ECO:0000269|PubMed:14645242, ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:17560374, ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:20154138, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22103349, ECO:0000269|PubMed:22304967, ECO:0000269|PubMed:9230442}.Q9BSJ2GCP2!Gamma-tubulin complex component 2centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; spindle pole [GO:0000922]P61225RAP2BRas-related protein Rap-2bSUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000269|PubMed:16540189}; Lipid-anchor {ECO:0000269|PubMed:16540189}; Cytoplasmic side {ECO:0000269|PubMed:16540189}. Note=Associated with red blood cells-released vesicles.Enegative regulation of cell migration [GO:0030336]; platelet activation [GO:0030168]; platelet aggregation [GO:0070527]; positive regulation of protein autophosphorylation [GO:0031954]; Rap protein signal transduction [GO:0032486]; regulation of protein tyrosine kinase activity [GO:0061097]; signal transduction [GO:0007165]2GDP binding [GO:0019003]; GTP binding [GO:0005525]bicellular tight junction [GO:0005923]; cell-cell contact zone [GO:0044291]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]FUNCTION: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells. {ECO:0000269|PubMed:11877431, ECO:0000269|PubMed:15143162, ECO:0000269|PubMed:16540189}.P12694ODBA;2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity [GO:0003863]; alpha-ketoacid dehydrogenase activity [GO:0003826]; carboxy-lyase activity [GO:0016831]; metal ion binding [GO:0046872]Q9UPT8ZC3H4,Zinc finger CCCH domain-containing protein 4Q9Y5M8SRPRB1Signal recognition particle receptor subunit beta]cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; IRE1-mediated unfolded protein response [GO:0036498]; small GTPase mediated signal transduction [GO:0007264]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]LFUNCTION: Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR (By similarity). {ECO:0000250}.Q9NQG6MID51$Mitochondrial dynamics protein MID51SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}; Single-pass membrane protein {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}.mitochondrial fission [GO:0000266]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein targeting to membrane [GO:0090314]ZADP binding [GO:0043531]; GDP binding [GO:0019003]; identical protein binding [GO:0042802]FUNCTION: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L. {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:24515348}.Q15386UBE3CUbiquitin-protein ligase E3Cprotein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]icytoplasm [GO:0005737]; intracellular [GO:0005622]; nucleus [GO:0005634]; proteasome complex [GO:0000502].FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo. {ECO:0000269|PubMed:11278995, ECO:0000269|PubMed:12692129, ECO:0000269|PubMed:16341092, ECO:0000269|PubMed:16601690}.Q969H6POP5'Ribonuclease P/MRP protein subunit POP5)SUBCELLULAR LOCATION: Nucleus, nucleolus.-nucleolar ribonuclease P complex [GO:0005655]FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. {ECO:0000269|PubMed:11413139}.Q15438CYH1 Cytohesin-1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17398095}; Peripheral membrane protein {ECO:0000269|PubMed:17398095}. Cytoplasm, cytosol {ECO:0000250}.establishment of epithelial cell polarity [GO:0090162]; positive regulation of GTPase activity [GO:0043547]; regulation of ARF protein signal transduction [GO:0032012]; regulation of cell adhesion [GO:0030155]; vesicle-mediated transport [GO:0016192]WARF guanyl-nucleotide exchange factor activity [GO:0005086]; lipid binding [GO:0008289]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; plasma membrane [GO:0005886]FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. {ECO:0000269|PubMed:10652308, ECO:0000269|PubMed:9653114}.O94829IPO13 Importin-13aFUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of the paired homeobox family. Also mediates nuclear export of eIF-1A, and the cytoplasmic release of eIF-1A is triggered by the loading of import substrates onto IPO13. {ECO:0000250, ECO:0000269|PubMed:11447110, ECO:0000269|PubMed:15143176}.Q9Y5Z9UBIA12UbiA prenyltransferase domain-containing< protein 1 Quinol/quinone metabolismSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Mitochondrion membrane. Cytoplasm. Nucleus.menaquinone biosynthetic process [GO:0009234]; ubiquinone biosynthetic process [GO:0006744]; vitamin K biosynthetic process [GO:0042371]Jantioxidant activity [GO:0016209]; prenyltransferase activity [GO:0004659]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of Golgi membrane [GO:0030173]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform present at high concentrations in the brain, kidney and pancreas, and is required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosyntetic enzyme: coenzyme Q10, also named ubiquinone, plays a important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress. {ECO:0000269|PubMed:20953171, ECO:0000269|PubMed:23374346}.P41440S19A1Folate transporter 1folic acid metabolic process [GO:0046655]; folic acid transport [GO:0015884]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]}folic acid binding [GO:0005542]; folic acid transporter activity [GO:0008517]; methotrexate transporter activity [GO:0015350]FUNCTION: Transporter for the intake of folate. Uptake of folate in human placental choriocarcinoma cells occurs by a novel mechanism called potocytosis which functionally couples three components, namely the folate receptor, the folate transporter, and a V-type H(+)-pump.Q15283RASA2Ras GTPase-activating protein 2?SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.intracellular signal transduction [GO:0035556]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]cytoplasm [GO:0005737]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; perinuclear region of cytoplasm [GO:0048471]eFUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4).Q96B23CR025 Uncharacterized protein C18orf25Q9NQE9HINT3,Histidine triad nucleotide-binding protein 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17870088}. Nucleus {ECO:0000269|PubMed:17870088}. Note=Localized as aggregates in the cytoplasm and the nucleus.ncytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]bFUNCTION: Hydrolyzes phosphoramidate and acyl-adenylate substrates. {ECO:0000269|PubMed:17870088}.Q9P0J1PDP1K[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialcellular metabolic process [GO:0044237]; peptidyl-threonine dephosphorylation [GO:0035970]; pyruvate metabolic process [GO:0006090]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; small molecule metabolic process [GO:0044281][pyruvate dehydrogenase (lipoamide)] phosphatase activity [GO:0004741]; metal ion binding [GO:0046872]; protein serine/threonine phosphatase activity [GO:0004722]FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. {ECO:0000250}.O14713ITBP1!Integrin beta-1-binding protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium. Cell projection, ruffle. Note=Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in a integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen.activation of protein kinase B activity [GO:0032148]; biomineral tissue development [GO:0031214]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; myoblast migration [GO:0051451]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of protein binding [GO:0032091]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein targeting to membrane [GO:0090315]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; Notch signaling pathway [GO:0007219]; positive regulation of cell division [GO:0051781]; positive regulation of cell proliferation [GO:0008284]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein transport [GO:0015031]; receptor clustering [GO:0043113]; regulation of blood vessel size [GO:0050880]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of GTPase activity [GO:0043087]; regulation of integrin-mediated signaling pathway [GO:2001044]; transcription, DNA-templated [GO:0006351]; tube formation [GO:0035148]GDP-dissociation inhibitor activity [GO:0005092]; integrin binding [GO:0005178]; protein complex binding [GO:0032403]; protein transporter activity [GO:0008565]2cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA < by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin-and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter. {ECO:0000269|PubMed:11741838, ECO:0000269|PubMed:11807099, ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:15703214, ECO:0000269|PubMed:17916086, ECO:0000269|PubMed:20616313, ECO:0000269|PubMed:21768292, ECO:0000269|Ref.18}.Q9Y5S1TRPV2@Transient receptor potential cation channel subfamily V member 2fSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Translocates from the cytoplasm to the plasma membrane upon ligand stimulation (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250}.scalcium ion transmembrane transport [GO:0070588]; ion transmembrane transport [GO:0034220]; positive regulation of axon extension [GO:0045773]; positive regulation of calcium ion import [GO:0090280]; response to heat [GO:0009408]; response to temperature stimulus [GO:0009266]; sensory perception [GO:0007600]; transmembrane transport [GO:0055085]; transport [GO:0006810]calcium channel activity [GO:0005262]; cation channel activity [GO:0005261]; ion channel activity [GO:0005216]; ion transmembrane transporter activity [GO:0015075]axonal growth cone [GO:0044295]; cell body [GO:0044297]; cell surface [GO:0009986]; growth cone membrane [GO:0032584]; integral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]; plasma membrane [GO:0005886]fFUNCTION: Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. {ECO:0000269|PubMed:10201375}.Q99447PCY2+Ethanolamine-phosphate cytidylyltransferaseglycerophospholipid biosynthetic process [GO:0046474]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid biosynthetic process [GO:0008654]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]Aethanolamine-phosphate cytidylyltransferase activity [GO:0004306]FUNCTION: Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine.Q96A54ADR1Adiponectin receptor protein 1ADIPO-Ligand-receptorsSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}; Multi-pass membrane protein {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000269|PubMed:12802337}..adiponectin-activated signaling pathway [GO:0033211]; fatty acid oxidation [GO:0019395]; glucose homeostasis [GO:0042593]; G-protein coupled receptor signaling pathway [GO:0007186]; hormone-mediated signaling pathway [GO:0009755]; leptin-mediated signaling pathway [GO:0033210]; negative regulation of cell growth [GO:0030308]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of JAK-STAT cascade [GO:0046427]; regulation of glucose metabolic process [GO:0010906]; regulation of lipid metabolic process [GO:0019216]adipokinetic hormone receptor activity [GO:0097003]; adiponectin binding [GO:0055100]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; receptor activity [GO:0004872]integral component of membrane [GO:0016021]; intrinsic component of plasma membrane [GO:0031226]; membrane [GO:0016020]; plasma membrane [GO:0005886]uFUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:25855295, PubMed:12802337). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity). {ECO:0000250|UniProtKB:Q91VH1, ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.Q9C0H5RHG39 Rho GTPase-activating protein 39axon guidance [GO:0007411]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]Ecytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]Q12797ASPH%Aspartyl/asparaginyl beta-hydroxylaseSUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056}.; SUBCELLULAR LOCATION: Isoform 4: Sarcoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000305|PubMed:15485681}.; SUBCELLULAR LOCATION: Isoform 8: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000269|PubMed:22586105}.activation of cysteine-type endopeptidase activity [GO:0097202]; activation of store-operated calcium channel activity [GO:0032237]; calcium ion transmembrane transport [GO:0070588]; cellular response to calcium ion [GO:0071277]; detection of calcium ion [GO:0005513]; face morphogenesis [GO:0060325]; limb morphogenesis [GO:0035108]; muscle contraction [GO:0006936]; negative regulation of cell proliferation [GO:0008285]; palate development [GO:0060021]; pattern specification process [GO:0007389]; peptidyl-aspartic acid hydroxylation [GO:0042264]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of proteolysis [GO:0045862]; positive regulation of ryanodine-sensitive calcium-release channel activity [GO:0060316]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cell communication by electrical coupling [GO:0010649]; regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0031585]; regulation of protein depolymerization [GO:1901879]; regulation of protein stability [GO:0031647]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; response to ATP [GO:0033198]calcium ion binding [GO:0005509]; electron carrier activity [GO:0009055]; ion channel binding [GO:0044325]; peptide-aspartate beta-dioxygenase activity [GO:0004597]; structural constituent of muscle [GO:0008307]; structural molecule activity [GO:0005198]calcium channel complex [GO:0034704]; cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789< ]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; junctional sarcoplasmic reticulum membrane [GO:0014701]; plasma membrane [GO:0005886]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]FUNCTION: Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. {ECO:0000269|PubMed:11773073}.; FUNCTION: Isoform 8: membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. {ECO:0000269|PubMed:22586105}.Q16563SYPL1Synaptophysin-like protein 1,SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Cytoplasmic transport vesicles (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250}."synaptic transmission [GO:0007268]%cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; integral component of synaptic vesicle membrane [GO:0030285]; melanosome [GO:0042470]; secretory granule [GO:0030141]Q9P086MED116Mediator of RNA polymerase II transcription subunit 11nRNA polymerase II transcription cofactor activity [GO:0001104]; ubiquitin protein ligase activity [GO:0061630]Dmediator complex [GO:0016592]; ubiquitin ligase complex [GO:0000151]P08962CD63 CD63 antigen$major lysosomal membrane proteins(6)SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Endosome, multivesicular body. Melanosome. Note=Also found in Weibel-Palade bodies of endothelial cells. Located in platelet dense granules. Detected in a subset of pre-melanosomes. Detected on intralumenal vesicles (ILVs) within multivesicular bodies.Tblood coagulation [GO:0007596]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cellular protein localization [GO:0034613]; endosome to melanosome transport [GO:0035646]; pigment granule maturation [GO:0048757]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of receptor internalization [GO:0002092]; protein transport [GO:0015031]; regulation of rubidium ion transport [GO:2000680]; regulation of vascular endothelial growth factor signaling pathway [GO:1900746]cell surface [GO:0009986]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; intrinsic component of plasma membrane [GO:0031226]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; multivesicular body, internal vesicle [GO:0097487]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088]RFUNCTION: Functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. {ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:21803846, ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027, ECO:0000269|PubMed:24635319}.Q96E11RRFM(Ribosome-recycling factor, mitochondrialFUNCTION: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity). {ECO:0000250}.Q96IU4ABHEB2Alpha/beta hydrolase domain-containing protein 14BISUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic.Qpositive regulation of transcription from RNA polymerase II promoter [GO:0045944]~cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription. {ECO:0000269|PubMed:14672934}.P28340DPOD1&DNA polymerase delta catalytic subunitbase-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; cellular response to UV [GO:0034644]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication proofreading [GO:0045004]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA synthesis involved in DNA repair [GO:0000731]; fatty acid homeostasis [GO:0055089]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; response to UV [GO:0009411]; small molecule metabolic process [GO:0044281]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]/3'-5'-exodeoxyribonuclease activity [GO:0008296]; 4 iron, 4 sulfur cluster binding [GO:0051539]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]aggresome [GO:0016235]; cytoplasm [GO:0005737]; delta DNA polymerase complex [GO:0043625]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleotide-excision repair complex [GO:0000109]; nucleus [GO:0005634]FUNCTION: Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.O00124UBXN8UBX domain-containing protein 8SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21949850}; Multi-pass membrane protein {ECO:0000269|PubMed:21949850}.kER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; single fertilization [GO:0007338]FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction. {ECO:0000269|PubMed:21949850}.P55017S12A3!Solute carrier family 12 member 3cell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; ion transport [GO:0006811]; potassium ion homeostasis [GO:0055075]; potassium ion import [GO:0010107]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085]; transport [GO:0006810],potassium:chloride symporter activity [GO:0015379];< potassium ion symporter activity [GO:0022820]; sodium:chloride symporter activity [GO:0015378]; sodium:potassium:chloride symporter activity [GO:0008511]; sodium ion transmembrane transporter activity [GO:0015081]; transporter activity [GO:0005215]apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Key mediator of sodium and chloride reabsorption in this nephron segment, accounting for a significant fraction of renal sodium reabsorption. {ECO:0000269|PubMed:8528245}.Q96KR1ZFRZinc finger RNA-binding protein[SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons. Colocalizes with STAU2 in several cytosolic RNA granules (By similarity). {ECO:0000250}.YDNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]Ichromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA (By similarity). {ECO:0000250}.P55199ELL'RNA polymerase II elongation factor ELLhSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, Cajal body. Note=Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes.gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; negative regulation of phosphatase activity [GO:0010923]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase III promoter [GO:0045945]; positive regulation of viral transcription [GO:0050434]; snRNA transcription from RNA polymerase III promoter [GO:0042796]; snRNA transcription from RNA polymerase II promoter [GO:0042795]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]Cajal body [GO:0015030]; histone locus body [GO:0035363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; transcriptionally active chromatin [GO:0035327]; transcription elongation factor complex [GO:0008023]FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (PubMed:23932780). ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. {ECO:0000269|PubMed:16006523, ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:22252557, ECO:0000269|PubMed:23932780, ECO:0000269|PubMed:8596958}.Q9UQ90SPG7 ParapleginSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:9635427}; Multi-pass membrane protein {ECO:0000269|PubMed:9635427}.anterograde axon cargo transport [GO:0008089]; mitochondrion organization [GO:0007005]; nervous system development [GO:0007399]; proteolysis [GO:0006508]ATP binding [GO:0005524]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270]6FUNCTION: Putative ATP-dependent zinc metalloprotease.P55268LAMB2Laminin subunit beta-2SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.astrocyte development [GO:0014002]; axon extension involved in regeneration [GO:0048677]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; metanephric glomerular basement membrane development [GO:0072274]; metanephric glomerular visceral epithelial cell development [GO:0072249]; neuromuscular junction development [GO:0007528]; retina development in camera-type eye [GO:0060041]; Schwann cell development [GO:0014044]; visual perception [GO:0007601]basal lamina [GO:0005605]; basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; laminin-11 complex [GO:0043260]; laminin-3 complex [GO:0005608]; synapse [GO:0045202]Q8IY18SMC5/Structural maintenance of chromosomes protein 5SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, telomere. Note=Associates with chromatin. Localizes to PML nuclear bodies in ALT cell lines.cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; cellular senescence [GO:0090398]; double-strand break repair via homologous recombination [GO:0000724]; mitotic nuclear division [GO:0007067]; positive regulation of maintenance of mitotic sister chromatid cohesion [GO:0034184]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; telomere maintenance via recombination [GO:0000722]cell junction [GO:0030054]; chromosome, telomeric region [GO:0000781]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Smc5-Smc6 complex [GO:0030915]GFUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526, ECO:0000269|PubMed:19502785}.Q92979NEP12Ribosomal RNA small subunit methyltransferase NEP1GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11935223}.lribosomal small subunit biogenesis [GO:0042274]; rRNA methylation [GO:0031167]; rRNA processing [GO:0006364]poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; rRNA (pseudouridine) methyltransferase activity [GO:0070037]; rRNA binding [GO:0019843]FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position (PubMed:20047967). Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). {ECO:0000250|UniProtKB:Q06287, ECO:0000269|PubMed:20047967}.Q53LP3SWAHC/Ankyrin repeat domain-containing protein SOWAHCQ9NRR3C42S2CDC42 small effector protein < 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Lipid-anchor. Cell projection, phagocytic cup. Note=Recruited to the activated TCR prior actin polymerization. Localizes at the phagocytic cup of macrophages.phagocytosis [GO:0006909]; regulation of cell shape [GO:0008360]; regulation of signal transduction [GO:0009966]; signal transduction [GO:0007165]cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. {ECO:0000269|PubMed:10816584, ECO:0000269|PubMed:15840583}.Q9NQ75CASS4'Cas scaffolding protein family member 4SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18256281}. Cell junction, focal adhesion {ECO:0000269|PubMed:18256281}.0phosphorelay sensor kinase activity [GO:0000155]ecytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; membrane [GO:0016020]FUNCTION: Docking protein that plays a role in tyrosine kinase-based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading. {ECO:0000269|PubMed:18256281}.Q86W92LIPB1 Liprin-beta-19focal adhesion [GO:0005925]; plasma membrane [GO:0005886]FUNCTION: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A. {ECO:0000269|PubMed:9624153}.Q5QJ74TBCEL2Tubulin-specific chaperone cofactor E-like proteinRFUNCTION: Acts as a regulator of tubulin stability. {ECO:0000269|PubMed:15728251}.Q15746MYLK(Myosin light chain kinase, smooth muscleSUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium. Cleavage furrow. Cytoplasm, cytoskeleton. Note=Localized to stress fibers during interphase and to the cleavage furrow during mitosis.actin filament organization [GO:0007015]; activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; aorta smooth muscle tissue morphogenesis [GO:0060414]; bleb assembly [GO:0032060]; cellular hypotonic response [GO:0071476]; muscle contraction [GO:0006936]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cell migration [GO:0030335]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of wound healing [GO:0090303]; protein phosphorylation [GO:0006468]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle contraction [GO:0006939]; tonic smooth muscle contraction [GO:0014820]ATP binding [GO:0005524]; calmodulin-dependent protein kinase activity [GO:0004683]; metal ion binding [GO:0046872]; myosin light chain kinase activity [GO:0004687]cell-cell junction [GO:0005911]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; stress fiber [GO:0001725]4 FUNCTION: Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. {ECO:0000269|PubMed:11113114, ECO:0000269|PubMed:11976941, ECO:0000269|PubMed:15020676, ECO:0000269|PubMed:15825080, ECO:0000269|PubMed:16284075, ECO:0000269|PubMed:16723733, ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:18710790, ECO:0000269|PubMed:19826488, ECO:0000269|PubMed:20139351, ECO:0000269|PubMed:20181817, ECO:0000269|PubMed:20375339, ECO:0000269|PubMed:20453870}.Q7Z569BRAPBRCA1-associated protein MAPK=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9497340}.MAPK cascade [GO:0000165]; negative regulation of signal transduction [GO:0009968]; protein ubiquitination [GO:0016567]; Ras protein signal transduction [GO:0007265]ligase activity [GO:0016874]; nuclear localization sequence binding [GO:0008139]; nucleotide binding [GO:0000166]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]\cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; ubiquitin ligase complex [GO:0000151]FUNCTION: Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport. {ECO:0000269|PubMed:14724641, ECO:0000303|PubMed:10777491}.Q49A88CCD14(Coiled-coil domain-containing protein 14)substantia nigra development [GO:0021762]Q96CG8CTHR11Collagen triple helix repeat-containing protein 1:cell migration [GO:0016477]; cochlea morphogenesis [GO:0090103]; establishment of planar polarity involved in neural tube closure [GO:0090177]; inner ear receptor stereocilium organization [GO:0060122]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; ossification involved in bone remodeling [GO:0043932]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of protein binding [GO:0032092]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]collagen trimer [GO:0005581]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]WFUNCTION: May act as a nega< tive regulator of collagen matrix deposition. {ECO:0000250}.Q6ZRS2SRCAPHelicase SRCAPbSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:10702287}.histone acetylation [GO:0016573]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone acetyltransferase activity [GO:0004402]; transcription coactivator activity [GO:0003713]Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]FUNCTION: Catalytic component of the SRCAP complex which mediates the ATP-dependent exchange of histone H2AZ/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling. Acts as a coactivator for CREB-mediated transcription, steroid receptor-mediated transcription, and Notch-mediated transcription. {ECO:0000269|PubMed:10347196, ECO:0000269|PubMed:11522779, ECO:0000269|PubMed:14500758, ECO:0000269|PubMed:16024792, ECO:0000269|PubMed:16634648, ECO:0000269|PubMed:17617668}.Q8NHQ9DDX55 ATP-dependent RNA helicase DDX55,FUNCTION: Probable ATP-binding RNA helicase.Q9Y4W2LAS1L"Ribosomal biogenesis protein LAS1LSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20647540}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Localizes mainly to the granular component, the region implicated in the later steps of rRNA processing and subunit assembly and export. {ECO:0000250}.cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; MLL1 complex [GO:0071339]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:20647540, ECO:0000269|PubMed:22872859}.O14874BCKDI[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrialXSUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion {ECO:0000269|PubMed:24449431}.branched-chain amino acid catabolic process [GO:0009083]; cellular amino acid catabolic process [GO:0009063]; phosphorylation [GO:0016310]; protein phosphorylation [GO:0006468][3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity [GO:0047323]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine/threonine kinase activity [GO:0004674]`mitochondrial alpha-ketoglutarate dehydrogenase complex [GO:0005947]; mitochondrion [GO:0005739](FUNCTION: Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex. {ECO:0000269|PubMed:24449431}.Q96GM5SMRD1]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1HSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8804307, ECO:0000305}.%cellular response to fatty acid [GO:0071398]; chromatin-mediated maintenance of transcription [GO:0048096]; chromatin remodeling [GO:0006338]; nervous system development [GO:0007399]; nucleosome disassembly [GO:0006337]; regulation of transcription from RNA polymerase II promoter [GO:0006357]vchromatin binding [GO:0003682]; protein complex scaffold [GO:0032947]; transcription coactivator activity [GO:0003713]SnBAF complex [GO:0071565]; npBAF complex [GO:0071564]; SWI/SNF complex [GO:0016514]FUNCTION: Involved in chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE). May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation. {ECO:0000250, ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:14698202, ECO:0000269|PubMed:8804307}.O00478BT3A3"Butyrophilin subfamily 3 member A3SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.%T cell mediated immunity [GO:0002456]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]jFUNCTION: Plays a role in T-cell responses in the adaptive immune response. {ECO:0000269|PubMed:22767497}.Q8N9N2ASCC12Activating signal cointegrator 1 complex subunit 1[cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; transcription factor complex [GO:0005667]FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. {ECO:0000269|PubMed:19074642}.P18440ARY1Arylamine N-acetyltransferase 1Xsmall molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]3arylamine N-acetyltransferase activity [GO:0004060]FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.Q9Y2G2CARD8/Caspase recruitment domain-containing protein 8eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15030775}. Nucleus {ECO:0000269|PubMed:15030775}.Pactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of interleukin-1 beta secretion [GO:0050718]cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; NACHT domain binding [GO:0032089]; protein homodimerization activity [GO:0042803]ocytoplasm [GO:0005737]; NLRP3 inflammasome complex [GO:0072559]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]TFUNCTION: Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.P48740MASP1'Mannan-binding lectin serine protease 1=SUBCELLULAR LOCATION: Secreted {ECO:0< 000269|PubMed:11485744}.complement activation [GO:0006956]; complement activation, lectin pathway [GO:0001867]; innate immune response [GO:0045087]; negative regulation of complement activation [GO:0045916]; receptor-mediated endocytosis [GO:0006898]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; peptidase activity [GO:0008233]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252]zFUNCTION: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. {ECO:0000269|PubMed:11485744}.Q9UHP3UBP25(Ubiquitin carboxyl-terminal hydrolase 25SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16501887, ECO:0000269|PubMed:19440361}.; SUBCELLULAR LOCATION: Isoform USP25m: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Some transient punctuate nuclear location in myotubes during myocyte development. {ECO:0000250}.cellular protein modification process [GO:0006464]; negative regulation of ERAD pathway [GO:1904293]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of proteasomal protein catabolic process [GO:0061136] ATPase binding [GO:0051117]; cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233]; SUMO binding [GO:0032183]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]FUNCTION: Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.; FUNCTION: The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.Q15262PTPRK0Receptor-type tyrosine-protein phosphatase kappakSUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane; Single-pass type I membrane protein.cell adhesion [GO:0007155]; cell migration [GO:0016477]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV [GO:0034644]; focal adhesion assembly [GO:0048041]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of transcription, DNA-templated [GO:0045892]; peptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]; protein localization to cell surface [GO:0034394]; signal transduction [GO:0007165]; transforming growth factor beta receptor signaling pathway [GO:0007179]beta-catenin binding [GO:0008013]; gamma-catenin binding [GO:0045295]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]Tadherens junction [GO:0005912]; axon [GO:0030424]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; dendrite [GO:0030425]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; leading edge membrane [GO:0031256]; neuronal cell body [GO:0043025]; photoreceptor outer segment [GO:0001750]ZFUNCTION: Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa. {ECO:0000269|PubMed:19836242}.P61009SPCS3"Signal peptidase complex subunit 3endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; signal peptidase complex [GO:0005787]Q8WUH2TGFA1=Transforming growth factor-beta receptor-associated protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278302}. Early endosome {ECO:0000269|PubMed:25266290}. Note=Colocalizes with TGF-beta receptors in the absence of signaling.$endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transforming growth factor beta receptor signaling pathway [GO:0007179]XSMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]2early endosome [GO:0005769]; membrane [GO:0016020]FUNCTION: Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2. {ECO:0000269|PubMed:11278302, ECO:0000269|PubMed:9545258}.; FUNCTION: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:25266290). Functions predominantly in APPL1-containing endosomes and in degradative but not recycling trafficking of endocytosed cargo (PubMed:25266290). {ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}.P081954F2$4F2 cell-surface antigen heavy chainSSUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localized to the plasma membrane when associated with SLC7A5 or SLC7A8. Localized to the placental apical membrane. Located selectively at cell-cell adhesion sites (By similarity). Colocalized with SLC7A8/LAT2 at the basolateral membrane of kidney proximal tubules and small intestine epithelia. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). {ECO:0000250}.amino acid transport [GO:0006865]; blood coagulation [GO:0007596]; calcium ion transport [GO:0006816]; carbohydrate metabolic process [GO:0005975]; cell growth [GO:0016049]; ion transport [GO:0006811]; leucine import [GO:0060356]; leukocyte migration [GO:0050900]; response to exogenous dsRNA [GO:0043330]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]; tryptophan transport [GO:0015827]calcium:sodium antiporter activity [GO:0005432]; catalytic activity [GO:0003824]; cation binding [GO:0043169]; double-stranded RNA binding [GO:0003725]; neutral amino acid transmembrane transporter activity [GO:0015175]; poly(A) RNA binding [GO:0044822]%apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Required for the func< tion of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier. {ECO:0000269|PubMed:10903140, ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:9751058, ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.Q8TB72PUM2Pumilio homolog 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19168546}. Cytoplasmic granule {ECO:0000269|PubMed:25340845}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19168546}. Note=The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules. Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ cells. {ECO:0000269|PubMed:25340845}.positive regulation of gene silencing by miRNA [GO:2000637]; positive regulation of RIG-I signaling pathway [GO:1900246]; regulation of gene silencing by miRNA [GO:0060964]; regulation of translation [GO:0006417]; stress granule assembly [GO:0034063]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]iFUNCTION: Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE) (, PubMed:21397187). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation (PubMed:22955276). Also mediates deadenylation-independent repression by promoting accessibility of miRNAs (PubMed:18776931, PubMed:22345517). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (PubMed:22345517). Plays a role in cytoplasmic sensing of viral infection (PubMed:25340845). May regulate DCUN1D3 mRNA levels (PubMed:25349211). May support proliferation and self-renewal of stem cells. {ECO:0000269|PubMed:18776931, ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:22345517, ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845, ECO:0000269|PubMed:25349211}.Q92499DDX1ATP-dependent RNA helicase DDX1wSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule. Note=Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF) after IR treatment, a process that depends on the presence of chromosomal DNA and/or RNA-DNA duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an ATM-dependent manner after IR treatment. Colocalized with RELA in the nucleus upon TNF-alpha induction. Relocalized to the cytoplasm with a perinuclear staining pattern in avian infectious bronchitis virus (IBV)-infected cells. Required for proper localization of HIV-1 Rev. Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264). {ECO:0000269|PubMed:24608264}.=DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; multicellular organismal development [GO:0007275]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translational initiation [GO:0006446]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RNA secondary structure unwinding [GO:0010501]; spliceosomal complex assembly [GO:0000245]; transcription, DNA-templated [GO:0006351]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]ATP binding [GO:0005524]; ATP-dependent helicase activity [GO:0008026]; ATP-dependent RNA helicase activity [GO:0004004]; chromatin binding [GO:0003682]; DNA/RNA helicase activity [GO:0033677]; DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; exonuclease activity [GO:0004527]; nuclease activity [GO:0004518]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; RNA helicase activity [GO:0003724]; transcription cofactor activity [GO:0003712]cleavage body [GO:0071920]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; tRNA-splicing ligase complex [GO:0072669]:FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Required for HIV-1 Rev function as well as for HIV-1 replication. Binds to the RRE sequence of HIV-1 mRNAs. {ECO:0000269|PubMed:12183465, ECO:0000269|PubMed:15567440, ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:18710941, ECO:0000269|PubMed:20573827, ECO:0000269|PubMed:24870230}.Q9NPB8GPCP1.Glycerophosphocholine phosphodiesterase GPCPD1glycerophospholipid biosynthetic process [GO:0046474]; phospholipid metabolic process [GO:0006644]; skeletal muscle tissue development [GO:0007519]; small molecule metabolic process [GO:0044281]Zglycerophosphocholine phosphodiesterase activity [GO:0047389]; starch binding [GO:2001070]FUNCTION: May be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity. {ECO:0000250}.A3KMH1VWA83von Willebrand factor A domai< n-containing protein 8=extracellular region [GO:0005576]; mitochondrion [GO:0005739]P50454SERPH Serpin H1_chondrocyte development involved in endochondral bone morphogenesis [GO:0003433]; collagen biosynthetic process [GO:0032964]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; negative regulation of endopeptidase activity [GO:0010951]; protein maturation [GO:0051604]; response to unfolded protein [GO:0006986]zcollagen binding [GO:0005518]; poly(A) RNA binding [GO:0044822]; serine-type endopeptidase inhibitor activity [GO:0004867]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]sFUNCTION: Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.O95391SLU7Pre-mRNA-splicing factor SLU7 Complex C(7)SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules.&alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to heat [GO:0034605]; intracellular protein transport [GO:0006886]; mRNA 3'-splice site recognition [GO:0000389]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing, via transesterification reactions [GO:0000375]pre-mRNA 3'-splice site binding [GO:0030628]; second spliceosomal transesterification activity [GO:0000386]; zinc ion binding [GO:0008270]4catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]BFUNCTION: Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:10647016, ECO:0000269|PubMed:12764196, ECO:0000269|PubMed:15728250}.Q99685MGLLMonoglyceride lipaseSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35678}. Membrane {ECO:0000250|UniProtKB:O35678}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35678}.acylglycerol acyl-chain remodeling [GO:0036155]; acylglycerol catabolic process [GO:0046464]; arachidonic acid metabolic process [GO:0019369]; blood coagulation [GO:0007596]; fatty acid biosynthetic process [GO:0006633]; glycerophospholipid biosynthetic process [GO:0046474]; inflammatory response [GO:0006954]; lipid metabolic process [GO:0006629]; phospholipid metabolic process [GO:0006644]; platelet activation [GO:0030168]; regulation of endocannabinoid signaling pathway [GO:2000124]; regulation of inflammatory response [GO:0050727]; regulation of sensory perception of pain [GO:0051930]; regulation of signal transduction [GO:0009966]; small molecule metabolic process [GO:0044281]; triglyceride catabolic process [GO:0019433]acylglycerol lipase activity [GO:0047372]; lysophospholipase activity [GO:0004622]; protein homodimerization activity [GO:0042803]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (By similarity). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333). {ECO:0000250|UniProtKB:O35678, ECO:0000269|PubMed:20079333}.O60512B4GT3 Beta-1,4-galactosyltransferase 3carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate metabolic process [GO:0042339]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.O94966UBP19(Ubiquitin carboxyl-terminal hydrolase 19SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}.ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of skeletal muscle tissue development [GO:0048642]; positive regulation of cell cycle process [GO:0090068]; protein deubiquitination [GO:0016579]; regulation of cellular response to hypoxia [GO:1900037]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein stability [GO:0031647]; response to endoplasmic reticulum stress [GO:0034976]cysteine-type endopeptidase activity [GO:0004197]; Hsp90 protein binding [GO:0051879]; metal ion binding [GO:0046872]; ubiquitin-specific protease activity [GO:0004843]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]&FUNCTION: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.Q8NHZ8CDC26(Anaphase-promoting complex subunit CDC26)FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex. {ECO:0000269|PubMed:1< 8485873}.Q9H7F4T185BTransmembrane protein 185BO00584RNT2Ribonuclease T2SUBCELLULAR LOCATION: Secreted. Lysosome lumen. Endoplasmic reticulum lumen. Note=Subcellular fractionation of transfected ovarian cancer cells reveals full-length RNASET2 in the endoplasmic reticulum fraction and the 2 smaller RNASET2 proteolytic products in the lysosome fraction.RNA catabolic process [GO:0006401]; RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]endoribonuclease activity [GO:0004521]; ribonuclease activity [GO:0004540]; ribonuclease T2 activity [GO:0033897]; RNA binding [GO:0003723]endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]/FUNCTION: Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism. {ECO:0000250, ECO:0000269|PubMed:16620762, ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:22735700}.Q9GZQ8MLP3B4Microtubule-associated proteins 1A/1B light chain 3BwSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endomembrane system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:23459205}. Note=LC3-II binds to the autophagic membranes. Localizes also to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250}.autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; membrane fusion [GO:0061025]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; regulation of mitochondrion degradation [GO:1903146]{autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of membrane [GO:0019898]; intracellular [GO:0005622]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; organelle membrane [GO:0031090]; pre-autophagosomal structure [GO:0000407]FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. {ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295, ECO:0000269|PubMed:24089205}.Q9Y365PCTLPCTP-like protein]SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:17561512}. Membrane {ECO:0000269|PubMed:17561512}. Note=In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm (By similarity). Mainly cytosolic. {ECO:0000250}.bile acid secretion [GO:0032782]; positive regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035360]mcytosol [GO:0005829]; intercellular canaliculus [GO:0046581]; membrane [GO:0016020]; microvillus [GO:0005902]FUNCTION: May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. {ECO:0000250, ECO:0000269|PubMed:15911624}.Q9UJS0CMC25Calcium-binding mitochondrial carrier protein Aralar2SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10642534}; Multi-pass membrane protein {ECO:0000269|PubMed:10642534}.aspartate transport [GO:0015810]; ATP biosynthetic process [GO:0006754]; carbohydrate metabolic process [GO:0005975]; cellular respiration [GO:0045333]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; L-aspartate transmembrane transport [GO:0089712]; L-glutamate transmembrane transport [GO:0089711]; L-glutamate transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]calcium ion binding [GO:0005509]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]; transporter activity [GO:0005215]yintegral component of plasma membrane [GO:0005887]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]Q15035TRAM21Translocating chain-associated membrane protein 2Jcollagen biosynthetic process [GO:0032964]; protein transport [GO:0015031]FUNCTION: Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. {ECO:0000269|PubMed:14749390}.P55789ALR!FAD-linked sulfhydryl oxidase ALRzSUBCELLULAR LOCATION: Isoform 1: Mitochondrion intermembrane space.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Secreted.flavin adenine dinucleotide binding [GO:0050660]; protein disulfide oxidoreductase activity [GO:0015035]; thiol oxidase activity [GO:0016972]cytoplasm [GO:0005737]; extracellular region [GO:0005576]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]_FUNCTION: Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.; FUNCTION: Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.P42336PK3CANPhosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoformxactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]; adaptive immune response [GO:0002250]; adipose tissue development [GO:0060612]; angiogenesis [GO:0001525]; blood coagulation [GO:0007596]; cardiac muscle contraction [GO:0060048]; cell chemotaxis [GO:0060326]; cellular response to glucose stimulus [GO:0071333]; endothelial cell migration [GO:0043542]; energy homeostasis [GO:0097009]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glucose metabolic process [GO:0006006]; hypomethylation of CpG island [GO:0044029]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; insulin receptor signaling pathway via phosphatidylinositol 3-kinase [GO:0038028]; leukocyte migration [GO:0050900]; liver development [GO:0001889]; negative regulation of anoikis [GO:2000811]; negative regulation of fibroblast apoptotic process [GO:2000270]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphati< dylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; platelet activation [GO:0030168]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; regulation of cellular respiration [GO:0043457]; regulation of genetic imprinting [GO:2000653]; regulation of multicellular organism growth [GO:0040014]; small molecule metabolic process [GO:0044281]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vasculature development [GO:0001944]1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphatidylinositol 3-kinase activity [GO:0035004]; phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; plasma membrane [GO:0005886]FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS. {ECO:0000269|PubMed:21708979}.Q9P219DAPLE Protein Daple>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25062847}.protein destabilization [GO:0031648]; protein homooligomerization [GO:0051260]; regulation of protein phosphorylation [GO:0001932]; stress-activated protein kinase signaling cascade [GO:0031098]; Wnt signaling pathway [GO:0016055]FPDZ domain binding [GO:0030165]; protein self-association [GO:0043621]FUNCTION: Negative regulator of the canonical Wnt signaling pathway, acting downstream of DVL to inhibit CTNNB1/Beta-catenin stabilization (By similarity). May also activate the JNK signaling pathway (PubMed:25062847). {ECO:0000250|UniProtKB:Q6VGS5, ECO:0000269|PubMed:25062847}.P43080GUC1A%Guanylyl cyclase-activating protein 1phototransduction, visible light [GO:0007603]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; rhodopsin mediated signaling pathway [GO:0016056]; signal transduction [GO:0007165]; visual perception [GO:0007601]ecalcium ion binding [GO:0005509]; calcium sensitive guanylate cyclase activator activity [GO:0008048]pphotoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886] FUNCTION: Stimulates guanylyl cyclase 1 (GC1) when free calcium ions concentration is low and inhibits GC1 when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of GC is a key event in recovery of the dark state of rod photoreceptors following light exposure.P62318SMD3%Small nuclear ribonucleoprotein Sm D3gene expression [GO:0010467]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; protein methylation [GO:0006479]; RNA splicing [GO:0008380]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]henzyme binding [GO:0019899]; histone pre-mRNA DCP binding [GO:0071208]; poly(A) RNA binding [GO:0044822]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; pICln-Sm protein complex [GO:0034715]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U4 snRNP [GO:0005687]; U7 snRNP [GO:0005683]9FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:18984161}.P78524ST5'Suppression of tumorigenicity 5 proteinnpositive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]6FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May be involved in cytoskeletal organization and tumorogenicity. Isoform 1 seems to be involved in a signaling transduction pathway leading to activation of MAPK1/ERK2. Isoform 3 may block ERK2 activation stimulated by ABL1. Isoform 3 may alter cell morphology and cell growth. {ECO:0000269|PubMed:10229203, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9632734}.Q13237KGP2cGMP-dependent protein kinase 2sSUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:8636133}; Lipid-anchor {ECO:0000269|PubMed:8636133}.blood coagulation [GO:0007596]; circadian regulation of gene expression [GO:0032922]; nitric oxide metabolic process [GO:0046209]; peptidyl-serine autophosphorylation [GO:0036289]; protein phosphorylation [GO:0006468]; protein targeting to plasma membrane [GO:0072661]; regulation of nitric-oxide synthase activity [GO:0050999]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; cGMP binding [GO:0030553]; cGMP-dependent protein kinase activity [GO:0004692]; protein kinase activity [GO:0004672]Xapical plasma membrane [GO:0016324]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]Q9H425CA198 Uncharacterized protein C1orf198Q96N67DOCK7"Dedicator of cytokinesis protein 7SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:16982419}. Note=Enriched in the developing axons of hippocampal neurons.activation of GTPase activity [GO:0090630]; axonogenesis [GO:0007409]; establishment of neuroblast polarity [GO:0045200]; hematopoietic progenitor cell differentiation [GO:0002244]; interkinetic nuclear migration [GO:0022027]; microtubule cytoskeleton organization [GO:0000226]; neuron projection development [GO:0031175]; pigmentation [GO:0043473]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of neurogenesis [GO:0050767]; small GTPase mediated signal transduction [GO:0007264]Xguanyl-nucleotide exchange factor activity [GO:0005085]; Rac GTPase binding [GO:0048365]axon [GO:0030< 424]; basal part of cell [GO:0045178]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; intracellular [GO:0005622]; neuron projection [GO:0043005]FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity). {ECO:0000250|UniProtKB:Q8R1A4, ECO:0000269|PubMed:16982419}.P40616ARL1&ADP-ribosylation factor-like protein 1SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11303027}; Peripheral membrane protein {ECO:0000269|PubMed:11303027}; Cytoplasmic side {ECO:0000269|PubMed:11303027}.Dactivation of phospholipase D activity [GO:0031584]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; protein localization to Golgi apparatus [GO:0034067]; retrograde transport, endosome to Golgi [GO:0042147]; small GTPase mediated signal transduction [GO:0007264]; toxin metabolic process [GO:0009404]enzyme activator activity [GO:0008047]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802] FUNCTION: GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus. {ECO:0000269|PubMed:9624189}.P22234PUR6Multifunctional protein ADE2Pde novo' IMP biosynthetic process [GO:0006189]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphoribosylaminoimidazole carboxylase activity [GO:0004638]; phosphoribosylaminoimidazolesuccinocarboxamide synthase activity [GO:0004639]Q9UPT5EXOC7Exocyst complex component 7SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates, as a preformed complex with SEC6 and SEC8, to the plasma membrane in response to insulin through the activation of ARHQ. {ECO:0000250}.cellular protein metabolic process [GO:0044267]; exocytosis [GO:0006887]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]; regulation of entry of bacterium into host cell [GO:2000535]centriolar satellite [GO:0034451]; cytosol [GO:0005829]; exocyst [GO:0000145]; growth cone membrane [GO:0032584]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]LFUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). {ECO:0000250}.Q13049TRI32"E3 ubiquitin-protein ligase TRIM32hSUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic bodies, often located around the nucleus.3actin ubiquitination [GO:0007014]; axon development [GO:0061564]; fat cell differentiation [GO:0045444]; innate immune response [GO:0045087]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of viral release from host cell [GO:1902187]; negative regulation of viral transcription [GO:0032897]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell motility [GO:2000147]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of neurogenesis [GO:0050769]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of proteolysis [GO:0045862]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of tumor necrosis factor-mediated signaling pathway [GO:1903265]; positive regulation of type I interferon production [GO:0032481]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of type I interferon production [GO:0032479]; response to tumor necrosis factor [GO:0034612]; response to UV [GO:0009411]; tissue homeostasis [GO:0001894]ligase activity [GO:0016874]; myosin binding [GO:0017022]; protein self-association [GO:0043621]; RNA binding [GO:0003723]; Tat protein binding [GO:0030957]; transcription coactivator activity [GO:0003713]; translation initiation factor binding [GO:0031369]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]vcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; striated muscle myosin thick filament [GO:0005863]FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:22500027}.Q9NWM3CUED1CUE domain-containing protein 1Q9UBL3ASH2L8Set1/Ash2 histone methyltransferase complex subunit ASH2<SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17355966}.cellular response to DNA damage stimulus [GO:0006974]; chromatin organization [GO:0006325]; hemopoiesis [GO:0030097]; histone H3-K4 methylation [GO:0051568]; positive regulation of cell proliferation [GO:0008284]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; response to estrogen [GO:0043627]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]DNA binding [GO:0003677]; euchromatin binding [GO:1990188]; metal ion binding [GO:0046872]; transcription regulatory region DNA binding [GO:0044212]histone methyltransferase complex [GO:0035097]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]FUNCTION: Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis. {ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:19556245}.Q9BPX7CG025UPF0415 protein C7orf25Q96C36P5CR2#Pyrroline-5-carboxylate reductase 2=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2722838}.+L-proline biosynthetic process [GO:0055129]7pyrroline-5-carboxylate reductase activity [GO:00047< 35]VFUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH. {ECO:0000269|PubMed:2722838, ECO:0000269|PubMed:6894153}.O00560SDCB1 Syntenin-1SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Melanosome. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Note=Mainly membrane-associated. Localized to adherens junctions, focal adhesions and endoplasmic reticulum. Colocalized with actin stress fibers. Also found in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.Iactin cytoskeleton organization [GO:0030036]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; intracellular signal transduction [GO:0035556]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphorylation [GO:0042327]; protein targeting to membrane [GO:0006612]; Ras protein signal transduction [GO:0007265]; substrate-dependent cell migration, cell extension [GO:0006930]; synaptic transmission [GO:0007268]cytoskeletal adaptor activity [GO:0008093]; frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; interleukin-5 receptor binding [GO:0005137]; protein heterodimerization activity [GO:0046982]; protein N-terminus binding [GO:0047485]; syndecan binding [GO:0045545]adherens junction [GO:0005912]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; focal adhesion [GO:0005925]; interleukin-5 receptor complex [GO:0005895]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway. {ECO:0000269|PubMed:10230395, ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:11498591}.Q9BWS9CHID1%Chitinase domain-containing protein 1eSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16357325}. Lysosome {ECO:0000269|PubMed:16357325}.carbohydrate metabolic process [GO:0005975]; chitin catabolic process [GO:0006032]; innate immune response [GO:0045087]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]bchitinase activity [GO:0004568]; chitin binding [GO:0008061]; oligosaccharide binding [GO:0070492]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802] FUNCTION: Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro). {ECO:0000269|PubMed:20724479}.Q9P0V3SH3B4SH3 domain-binding protein 4SUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus {ECO:0000305}. Note=Specifically associated with transferrin receptor-containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus.cellular response to amino acid stimulus [GO:0071230]; endocytosis [GO:0006897]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of GTPase activity [GO:0034260]; negative regulation of TOR signaling [GO:0032007]; positive regulation of autophagy [GO:0010508]; protein localization to lysosome [GO:0061462]; regulation of catalytic activity [GO:0050790]yGDP-dissociation inhibitor activity [GO:0005092]; identical protein binding [GO:0042802]; Ras GTPase binding [GO:0017016]clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]\FUNCTION: May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may acts as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy. {ECO:0000269|PubMed:16325581, ECO:0000269|PubMed:22575674}.Q9NS91RAD18!E3 ubiquitin-protein ligase RAD186DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; negative regulation of DNA recombination [GO:0045910]; postreplication repair [GO:0006301]; protein monoubiquitination [GO:0006513]; response to UV [GO:0009411]; spermatogenesis [GO:0007283]; translesion synthesis [GO:0019985]=damaged DNA binding [GO:0003684]; ligase activity [GO:0016874]; polyubiquitin binding [GO:0031593]; single-stranded DNA-dependent ATPase activity [GO:0043142]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; Y-form DNA binding [GO:0000403]; zinc ion binding [GO:0008270]chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505]; replication fork [GO:0005657]; XY body [GO:0001741]FUNCTION: E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. {ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:21659603}.Q5VTR2BRE1A!E3 ubiquitin-protein ligase BRE1AYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19037095, ECO:0000305|PubMed:16337599}.histone H2B ubiquitination [GO:0033523]; histone monoubiquitination [GO:0010390]; negative regulation of cell migration [GO:0030336]; negative regulation of mRNA polyadenylation [GO:1900364]; positive regulation of histone H2B ubiquitination [GO:2001168]; positive regulation of histone methylation [GO:0031062]; positive regulation of transcription, DNA-templated [GO:0045893]; protein polyubiquitination [GO:0000209]; regulation of transcription, DNA-templated [GO:0006355]; ubiquitin-dependent protein catabolic process [GO:0006511]Jchromatin binding [GO:0003682]; histone binding [GO:0042393]; ligase activity [GO:0016874]; mRNA 3'-UTR binding [GO:0003730]; p53 binding [GO:0002039]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]HULC complex [GO:0033503]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex< in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation. {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:19410543}.P18074ERCC2=TFIIH basal transcription factor complex helicase XPD subunit57-methylguanosine mRNA capping [GO:0006370]; aging [GO:0007568]; apoptotic process [GO:0006915]; bone mineralization [GO:0030282]; cell proliferation [GO:0008283]; central nervous system myelin formation [GO:0032289]; chromosome segregation [GO:0007059]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; embryonic cleavage [GO:0040016]; erythrocyte maturation [GO:0043249]; extracellular matrix organization [GO:0030198]; gene expression [GO:0010467]; hair cell differentiation [GO:0035315]; hair follicle maturation [GO:0048820]; hematopoietic stem cell differentiation [GO:0060218]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA incision [GO:0033683]; positive regulation of DNA binding [GO:0043388]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; post-embryonic development [GO:0009791]; protein phosphorylation [GO:0006468]; regulation of gene expression, epigenetic [GO:0040029]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; spinal cord development [GO:0021510]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; UV protection [GO:0009650]; viral process [GO:0016032][4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; metal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]core TFIIH complex [GO:0000439]; cytoplasm [GO:0005737]; holo TFIIH complex [GO:0005675]; MMXD complex [GO:0071817]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the core-TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:15494306, ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:8413672}.Q9NQT5EXOS3Exosome complex component RRP40CUT catabolic process [GO:0071034]; DNA deamination [GO:0045006]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; gene expression [GO:0010467]; isotype switching [GO:0045190]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear polyadenylation-dependent tRNA catabolic process [GO:0071038]; nuclear retention of pre-mRNA with aberrant 3'-ends at the site of transcription [GO:0071049]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; positive regulation of isotype switching [GO:0045830]; rRNA processing [GO:0006364]; U4 snRNA 3'-end processing [GO:0034475]E3'-5'-exoribonuclease activity [GO:0000175]; RNA binding [GO:0003723]nFUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:21255825}.Q13310PABP4Polyadenylate-binding protein 4yblood coagulation [GO:0007596]; RNA catabolic process [GO:0006401]; RNA processing [GO:0006396]; translation [GO:0006412]nucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]}cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity). {ECO:0000250}.Q9HCN3TMM8ATransmembrane protein 8Aextracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]rFUNCTION: May be a cell surface adhesion molecule. May be involved in the maintenance of the resting T-cell state.Q5VZF2MBNL2Muscleblind-like protein 2&SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Greater concentration in the nucleus. Expressed in or near large cytoplasmic adhesion plaques. Location in the cytoplasm is microtubule-dependent. In both DM1 and DM2 patients, colocalizes with nuclear foci of retained expanded-repeat transcripts.`mRNA processing [GO:0006397]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]9FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts either < as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. RNA-binding protein that binds to 5'ACACCC-3' core sequence, termed zipcode, within the 3'UTR of ITGA3. Binds to CUG triplet repeat expansion in myotonic dystrophy muscle cells by sequestering the target RNAs. Seems to regulate expression and localization of ITGA3 by transporting it from the nucleus to cytoplasm at adhesion plaques. May play a role in myotonic dystrophy pathophysiology (DM). {ECO:0000269|PubMed:15257297, ECO:0000269|PubMed:16273094, ECO:0000269|PubMed:16946708}.Q9BXI6TB10ATBC1 domain family member 10ASUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000269|PubMed:16923811}. Note=Localizes to the microvilli-rich region of the syncytiotrophoblast. In melanocytes, located at the periphery of cells.activation of cysteine-type endopeptidase activity [GO:0097202]; positive regulation of proteolysis [GO:0045862]; retrograde transport, endosome to Golgi [GO:0042147]GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; PDZ domain binding [GO:0030165]vextracellular exosome [GO:0070062]; intracellular [GO:0005622]; microvillus [GO:0005902]; plasma membrane [GO:0005886]{FUNCTION: Acts as GTPase-activating protein for RAB27A, but not for RAB2A, RAB3A, nor RAB4A. {ECO:0000269|PubMed:16923811}.Q96EM0T3HPD$Trans-L-3-hydroxyproline dehydratasemetabolic process [GO:0008152]]hydro-lyase activity [GO:0016836]; trans-L-3-hydroxyproline dehydratase activity [GO:0050346]%FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it. {ECO:0000269|PubMed:22528483}.P11279LAMP1+Lysosome-associated membrane glycoprotein 1ISUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. Colocalizes with OSBPL1A at the late endosome.autophagic cell death [GO:0048102]; autophagy [GO:0006914]; establishment of protein localization to organelle [GO:0072594]; Golgi to lysosome transport [GO:0090160]; granzyme-mediated apoptotic signaling pathway [GO:0008626]; positive regulation of natural killer cell degranulation [GO:0043323]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; protein stabilization [GO:0050821]; regulation of organelle transport along microtubule [GO:1902513]; viral process [GO:0016032]halveolar lamellar body [GO:0097208]; cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane [GO:0016020]; multivesicular body [GO:0005771]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; phagolysosome membrane [GO:0061474]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; synaptic vesicle [GO:0008021]_FUNCTION: Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.A5D8V6VP37C/Vacuolar protein sorting-associated protein 37CSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000305|PubMed:15509564}; Peripheral membrane protein {ECO:0000305|PubMed:15509564}. Note=Probably associates with membranes. Recruited to the plasma membrane by HIV-1.endosomal transport [GO:0016197]; intracellular transport of virus [GO:0075733]; membrane organization [GO:0061024]; protein transport [GO:0015031]; viral life cycle [GO:0019058]; viral process [GO:0016032]; viral protein processing [GO:0019082]; virion assembly [GO:0019068]endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15509564}.Q9UQE7SMC3/Structural maintenance of chromosomes protein 3eSUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. The phosphorylated form at Ser-1083 is preferentially associated with unsynapsed chromosomal regions (By similarity). {ECO:0000250}.[cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; DNA repair [GO:0006281]; meiotic nuclear division [GO:0007126]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid cohesion [GO:0007064]; mitotic spindle organization [GO:0007052]; negative regulation of DNA endoreduplication [GO:0032876]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of DNA replication [GO:0006275]; signal transduction [GO:0007165]; sister chromatid cohesion [GO:0007062]; stem cell maintenance [GO:0019827]ATP binding [GO:0005524]; chromatin binding [GO:0003682]; dynein binding [GO:0045502]; microtubule motor activity [GO:0003777]; protein heterodimerization activity [GO:0046982]basement membrane [GO:0005604]; chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; cohesin core heterodimer [GO:0008280]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lateral element [GO:0000800]; meiotic cohesin complex [GO:0030893]; nuclear matrix [GO:0016363]; nuclear meiotic cohesin complex [GO:0034991]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]5FUNCTION: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:19907496}.Q03701CEBPZ#CCAAT/enhancer-binding protein zetapositive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription from RNA polymerase II promoter [GO:0006366]ADNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077];FUNCTION: Stimulates transcription from the HSP70 promoter.Q13136LIPA1Liprin-alpha-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7796809}. Note=Colocalizes with PTPRF at the ends of focal adhesions most proximal to the cell nucleus.Kcell-matrix adhesion [GO:0007160]; glutamate secretion [GO:0014047]; negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; negative regulation of stress fiber assembly [GO:0051497]; neurotransmitter secretion [GO:0007269]; signal transduction [GO:0007165]; synaptic transmission [GO:0007< 268]ocytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; presynaptic active zone [GO:0048786]+FUNCTION: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. {ECO:0000269|PubMed:7796809}.P47893OR3A2Olfactory receptor 3A22detection of chemical stimulus involved in sensory perception [GO:0050907]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; G-protein coupled receptor signaling pathway [GO:0007186]; sensory perception of chemical stimulus [GO:0007606]; signal transduction [GO:0007165]zG-protein coupled receptor activity [GO:0004930]; olfactory receptor activity [GO:0004984]; receptor activity [GO:0004872]*FUNCTION: Odorant receptor. {ECO:0000305}.Q14147DHX34)Probable ATP-dependent RNA helicase DHX34negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; RNA processing [GO:0006396]Q6PCE3PGM2L!Glucose 1,6-bisphosphate synthaseDglucose metabolic process [GO:0006006]; phosphorylation [GO:0016310]glucose-1,6-bisphosphate synthase activity [GO:0047933]; intramolecular transferase activity, phosphotransferases [GO:0016868]; metal ion binding [GO:0046872]FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities. {ECO:0000269|PubMed:17804405, ECO:0000269|PubMed:18927083}.Q9BTE7DCNL5DCN1-like protein 5O00148DX39A!ATP-dependent RNA helicase DDX39ASUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21859714}. Cytoplasm {ECO:0000269|PubMed:21859714}. Note=Can translocate to the cytoplasm in the presence of MX1.cellular response to DNA damage stimulus [GO:0006974]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; regulation of gene expression [GO:0010468]; RNA secondary structure unwinding [GO:0010501]fcytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Isoform 1: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus. {ECO:0000269|PubMed:15047853, ECO:0000269|PubMed:17548965}.Q9BQ15SOSB1SOSS complex subunit B1Other related(25)SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment.cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; mitotic cell cycle checkpoint [GO:0007093]; response to ionizing radiation [GO:0010212]acytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SOSS complex [GO:0070876]FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. {ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.Q6P1N9TATD1!Putative deoxyribonuclease TATDN1"DNA catabolic process [GO:0006308]deoxyribonuclease activity [GO:0004536]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; metal ion binding [GO:0046872]:intracellular organelle [GO:0043229]; nucleus [GO:0005634]4FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.Q08J23NSUN2*tRNA (cytosine(34)-C(5))-methyltransferaseSUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Note=Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; spermatid development [GO:0007286]; tRNA methylation [GO:0030488]wpoly(A) RNA binding [GO:0044822]; tRNA (cytosine-5-)-methyltransferase activity [GO:0016428]; tRNA binding [GO:0000049]xchromatoid body [GO:0033391]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819]/FUNCTION: RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors. May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity. {ECO:0000269|PubMed:17071714, ECO:0000269|PubMed:19596847, ECO:0000269|PubMed:22995836}.Q8TDX7NEK7$Serine/threonine-protein kinase Nek7-SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Present at centrosome throughout the cell cycle. Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody.cytokinesis [GO:0000910]; protein phosphorylation [GO:0006468]; regulation of mitotic cell cycle [GO:0007346]; spindle assembly [GO:0051225]oATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; spindle pole [GO:0000922]<FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1. {ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473, ECO:0000269|PubMed:19414596}.Q6IAA8LTOR1!Ragulator complex protein LAMTOR1SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor; Cytoplasmic side. Lysosome membrane; Lipid-anchor; Cytoplasmic side. Cell membrane.cell growth [GO:0016049]; cellular protein localization [GO:0034613]; cellular response to amino acid stimulus [GO:0071230]; cholesterol homeostasis [GO:0042632]; endosome localization [GO:0032439]; endosome organization [GO:0007032]; lysosome localization [GO:0032418]; lysosome organization [GO:0007040]; positive regulation of GTPase activity [GO:0043547]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of TOR signaling [GO:0032008]; regulation of cholesterol efflux [GO:0010874]; regulation of cholesterol esterification [GO:0010872]; regulation of cholesterol import [GO:0060620]; regulation of receptor recycling [GO:0001919].extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; Ragulator complex [GO:0071986]=FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cel< l growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation. {ECO:0000269|PubMed:19654316, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:20544018, ECO:0000269|PubMed:22980980}.Q92791SC65!Synaptonemal complex protein SC65SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8862517}. Chromosome {ECO:0000269|PubMed:8862517}. Note=Localized uniformly throughout the granular component of the nucleolus and on the surface of chromosomes during mitosis.*synaptonemal complex assembly [GO:0007130]dcondensed nuclear chromosome [GO:0000794]; nucleolus [GO:0005730]; synaptonemal complex [GO:0000795]Q15334L2GL1(Lethal(2) giant larvae protein homolog 1SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12725730, ECO:0000269|PubMed:7542763}. Note=Localized to the lateral membrane during the polarization and formation cell-cell contacts. Enriched in developping axons (By similarity). {ECO:0000250}.axonogenesis [GO:0007409]; cortical actin cytoskeleton organization [GO:0030866]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; positive regulation of GTPase activity [GO:0043547]; protein complex assembly [GO:0006461]vGTPase activator activity [GO:0005096]; protein kinase binding [GO:0019901]; structural molecule activity [GO:0005198]axon [GO:0030424]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; early endosome membrane [GO:0031901]; Golgi cis cisterna [GO:0000137]; trans-Golgi network membrane [GO:0032588]FUNCTION: Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane. {ECO:0000269|PubMed:15735678, ECO:0000269|PubMed:16170365}.Q9UKK3PARP4Poly [ADP-ribose] polymerase 4Base excision repair (BER)(30)SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Also found in the nucleus, associated with mitotic spindles.cell death [GO:0008219]; cellular protein modification process [GO:0006464]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; protein ADP-ribosylation [GO:0006471]; response to drug [GO:0042493]; transport [GO:0006810]hDNA binding [GO:0003677]; enzyme binding [GO:0019899]; NAD+ ADP-ribosyltransferase activity [GO:0003950]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; spindle microtubule [GO:0005876]Q8IWT6LRC8A-Volume-regulated anion channel subunit LRRC8ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24725410, ECO:0000269|PubMed:24782309, ECO:0000269|PubMed:24790029}; Multi-pass membrane protein {ECO:0000269|PubMed:24725410, ECO:0000269|PubMed:24782309, ECO:0000269|PubMed:24790029}.anion transmembrane transport [GO:0098656]; anion transport [GO:0006820]; cell volume homeostasis [GO:0006884]; pre-B cell differentiation [GO:0002329]; response to osmotic stress [GO:0006970]pcell surface [GO:0009986]; ion channel complex [GO:0034702]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. It is unclear whether LRRC8A constitutes a pore-forming subunit or whether it is closely associated with the pore and mediates channel properties such as ion selectivity. Involved in B-cell development: required for the pro-B cell to pre-B cell transition. Also required for T-cell development. {ECO:0000269|PubMed:14660746, ECO:0000269|PubMed:24725410, ECO:0000269|PubMed:24790029}.Q9H329E41LBBand 4.1-like protein 4B.actomyosin structure organization [GO:0031032]apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extrinsic component of membrane [GO:0019898]A9YTQ3AHRR#Aryl hydrocarbon receptor repressor2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}. Note=Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment.negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; response to xenobiotic stimulus [GO:0009410]; transcription, DNA-templated [GO:0006351]vDNA binding [GO:0003677]; RNA polymerase II transcription factor binding transcription repressor activity [GO:0001191]EFUNCTION: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site. {ECO:0000269|PubMed:17890447, ECO:0000269|PubMed:18172554}.O00159MYO1CUnconventional myosin-IcSUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:22736583}. Nucleus {ECO:0000269|PubMed:22736583}. Note=Colocalizes with RNA polymerase II. Absent from nucleoli and does not colocalize with RNA polymerase I. Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, stereocilium membrane {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm. Nucleus, nucleolus. Nucleus, nuclear pore complex. Note=Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli (By similarity). In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contac< t with RNP particles. Colocalizes with RPS6 at the nuclear pore level. {ECO:0000250}.wFc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; membrane organization [GO:0061024]; mRNA transport [GO:0051028]; positive regulation of cell migration [GO:0030335]; positive regulation of cell migration by vascular endothelial growth factor signaling pathway [GO:0038089]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; protein targeting [GO:0006605]; protein targeting to membrane [GO:0006612]; regulation of bicellular tight junction assembly [GO:2000810]actin-dependent ATPase activity [GO:0030898]; ATP binding [GO:0005524]; motor activity [GO:0003774]; Ral GTPase binding [GO:0017160]; receptor binding [GO:0005102]`basal plasma membrane [GO:0009925]; brush border [GO:0005903]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; membrane raft [GO:0045121]; microvillus [GO:0005902]; mitochondrion [GO:0005739]; myosin I complex [GO:0045160]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; stereocilium membrane [GO:0060171]; unconventional myosin complex [GO:0016461]%FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. {ECO:0000269|PubMed:24636949}.; FUNCTION: Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation (By similarity). {ECO:0000250}.Q6P9B6TLDC1TLD domain-containing protein 1P25685DNJB1!DnaJ homolog subfamily B member 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1586970}. Nucleus {ECO:0000269|PubMed:1586970}. Nucleus, nucleolus {ECO:0000269|PubMed:1586970}. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.zcellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0070389]; chaperone mediated protein folding requiring cofactor [GO:0051085]; negative regulation of inclusion body assembly [GO:0090084]; positive regulation of ATPase activity [GO:0032781]; regulation of cellular response to heat [GO:1900034]; response to unfolded protein [GO:0006986]ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; chaperone binding [GO:0051087]; Hsp70 protein binding [GO:0030544]; unfolded protein binding [GO:0051082]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]wFUNCTION: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.P49770EI2BB1Translation initiation factor eIF-2B subunit beta/cellular protein metabolic process [GO:0044267]; cellular response to stimulus [GO:0051716]; central nervous system development [GO:0007417]; gene expression [GO:0010467]; myelination [GO:0042552]; oligodendrocyte development [GO:0014003]; ovarian follicle development [GO:0001541]; positive regulation of GTPase activity [GO:0043547]; regulation of translational initiation [GO:0006446]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to peptide hormone [GO:0043434]; translation [GO:0006412]; translational initiation [GO:0006413]gATP binding [GO:0005524]; GTP binding [GO:0005525]; translation initiation factor activity [GO:0003743]O95347SMC2/Structural maintenance of chromosomes protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.cell division [GO:0051301]; kinetochore organization [GO:0051383]; meiotic chromosome condensation [GO:0010032]; meiotic chromosome segregation [GO:0045132]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]JATP binding [GO:0005524]; protein heterodimerization activity [GO:0046982]condensed chromosome [GO:0000793]; condensin complex [GO:0000796]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.P32322P5CR12Pyrroline-5-carboxylate reductase 1, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19648921}.cellular amino acid biosynthetic process [GO:0008652]; cellular nitrogen compound metabolic process [GO:0034641]; cellular response to oxidative stress [GO:0034599]; L-proline biosynthetic process [GO:0055129]; negative regulation of hydrogen peroxide-induced cell death [GO:1903206]; proline biosynthetic process [GO:0006561]; regulation of mitochondrial membrane potential [GO:0051881]; small molecule metabolic process [GO:0044281]_identical protein binding [GO:0042802]; pyrroline-5-carboxylate reductase activity [GO:0004735]FUNCTION: Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress. {ECO:0000269|PubMed:16730026, ECO:0000269|PubMed:19648921}.Q9H944MED206Mediator of RNA polymerase II transcription subunit 20gene expression [GO:0010467]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]DNA-directed RNA polymerase activity [GO:0003899]; RNA polymerase II transcription cofactor activity [GO:0001104]; ubiquitin protein ligase activity [GO:0061630]^mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; ubiquitin ligase complex [GO:0000151]Q8N6G5CGAT27Chondroitin sulfate N-acetylgalactosaminyltransferase 2carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate metabolic process [GO:0030204]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0050653]; dermatan sulfate proteoglycan biosynthetic process [GO:< 0050651]; dermatan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0050652]; glycosaminoglycan metabolic process [GO:0030203]; proteoglycan biosynthetic process [GO:0030166]; small molecule metabolic process [GO:0044281]acetylgalactosaminyltransferase activity [GO:0008376]; glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity [GO:0047237]; metal ion binding [GO:0046872]Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of Golgi membrane [GO:0030173]; membrane [GO:0016020]-FUNCTION: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. {ECO:0000269|PubMed:12433924, ECO:0000269|PubMed:12446672}.Q5VWJ9SNX30Sorting nexin-30Cendosome [GO:0005768]; extrinsic component of membrane [GO:0019898]Q14011CIRBP"Cold-inducible RNA-binding proteinSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11574538}. Cytoplasm {ECO:0000269|PubMed:11574538}. Note=Translocates from the nucleus to the cytoplasm after exposure to UV radiation. Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. Its recruitment into stress granules occurs in the absence of TIAR proteins (By similarity). {ECO:0000250}.mRNA stabilization [GO:0048255]; negative regulation of translation [GO:0017148]; positive regulation of translation [GO:0045727]; response to cold [GO:0009409]; response to UV [GO:0009411]; stress granule assembly [GO:0034063]mRNA 3'-UTR binding [GO:0003730]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; small ribosomal subunit rRNA binding [GO:0070181]; translation repressor activity [GO:0030371]ocytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]GFUNCTION: Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed. {ECO:0000250, ECO:0000269|PubMed:11574538, ECO:0000269|PubMed:16513844}.O00470MEIS1Homeobox protein Meis1:angiogenesis [GO:0001525]; definitive hemopoiesis [GO:0060216]; lens morphogenesis in camera-type eye [GO:0002089]; locomotory behavior [GO:0007626]; megakaryocyte development [GO:0035855]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of neuron differentiation [GO:0045665]chromatin binding [GO:0003682]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]?nucleus [GO:0005634]; transcription factor complex [GO:0005667]KFUNCTION: Acts as a transcriptional regulator of PAX6. Acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias. {ECO:0000269|PubMed:12609849}.P62330ARF6ADP-ribosylation factor 6SUBCELLULAR LOCATION: Golgi apparatus. Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Recycling endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Cell projection, filopodium membrane; Lipid-anchor. Midbody {ECO:0000250}. Cytoplasm {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Distributed throughout the cytoplasm during metaphase. Transiently detected at the ingressing cleavage furrow during mitotic cytokinesis. Recruited to the midbody at later stages of cytokinesis; this requires interaction with KIF23 (By similarity). Recruited to the cell membrane in association with CYTH2 and ARL4C. Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles. {ECO:0000250}.5cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; establishment of epithelial cell polarity [GO:0090162]; hepatocyte apoptotic process [GO:0097284]; liver development [GO:0001889]; movement of cell or subcellular component [GO:0006928]; myeloid cell apoptotic process [GO:0033028]; negative regulation of dendrite development [GO:2000171]; negative regulation of receptor-mediated endocytosis [GO:0048261]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; protein localization to cell surface [GO:0034394]; protein localization to endosome [GO:0036010]; protein transport [GO:0015031]; regulation of dendritic spine development [GO:0060998]; regulation of filopodium assembly [GO:0051489]; regulation of Rac protein signal transduction [GO:0035020]; ruffle organization [GO:0031529]; small GTPase mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192]YGTPase activity [GO:0003924]; GTP binding [GO:0005525]; thioesterase binding [GO:0031996]cell cortex [GO:0005938]; cleavage furrow [GO:0032154]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; midbody [GO:0030496]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; ruffle [GO:0001726]FUNCTION: GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers. May also modulate vesicle budding and uncoating within the Golgi apparatus. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. {ECO:0000269|PubMed:11266366, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16099990, ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:18400762, ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:7589240}.O95997PTTG1Securinanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell division [GO:0051301]; chromosome organization [GO:0051276]; chromosome segregation [GO:0007059]; DNA repair [GO:0006281]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of endopeptidase activity [GO:0010951]; regulation of transcription, DNA-templated [GO:0006355]; spermatogenesis [GO:0007283]; transcription from RNA polymerase II promoter [GO:0006366]cysteine-type endopeptidase inhibitor activity [GO:0004869]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional ac< tivity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11238996, ECO:0000269|PubMed:11371342, ECO:0000269|PubMed:12355087}.O15460P4HA2$Prolyl 4-hydroxylase subunit alpha-2Bpeptidyl-proline hydroxylation to 4-hydroxy-L-proline [GO:0018401]0electron carrier activity [GO:0009055]; iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; procollagen-proline 4-dioxygenase activity [GO:0004656]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; procollagen-proline 4-dioxygenase complex [GO:0016222]Q8IXM6NRMNurimSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}; Multi-pass membrane protein {ECO:0000269|PubMed:10402458, ECO:0000269|PubMed:15542857, ECO:0000269|PubMed:23092226}.integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q7Z304MAMC2MAM domain-containing protein 2jendoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; proteinaceous extracellular matrix [GO:0005578]Q8NFV4ABHDB1Alpha/beta hydrolase domain-containing protein 11Q96SB3NEB2 Neurabin-2 SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse. Cell junction, adherens junction {ECO:0000250}. Cytoplasm. Cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle membrane. Note=Enriched at synapse and cadherin-based cell-cell adhesion sites. In neurons, both cytosolic and membrane-associated, and highly enriched in the postsynaptic density apposed to exitatory synapses. Colocalizes with PPP1R2 at actin-rich adherens junctions in epithelial cells and in dendritic spines (By similarity). Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. {ECO:0000250}.hcell cycle arrest [GO:0007050]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to morphine [GO:0071315]; filopodium assembly [GO:0046847]; negative regulation of catalytic activity [GO:0043086]; negative regulation of cell growth [GO:0030308]; nervous system development [GO:0007399]; regulation of cell growth by extracellular stimulus [GO:0001560]; regulation of cell proliferation [GO:0042127]; regulation of exit from mitosis [GO:0007096]; regulation of opioid receptor signaling pathway [GO:2000474]; regulation of synaptic transmission [GO:0050804]; RNA splicing [GO:0008380]_protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]Aadherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein phosphatase type 1 complex [GO:0000164]; ruffle membrane [GO:0032587]; synapse [GO:0045202]FUNCTION: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1 (By similarity). Required for hepatocyte growth factor (HGF)-induced cell migration. {ECO:0000250, ECO:0000269|PubMed:19151759}.Q69YN4VIRProtein virilizer homologDSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24100041}.VmRNA methylation [GO:0080009]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]6FUNCTION: Required for N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and processing (PubMed:24981863). Involved in mRNA splicing regulation, probably via its function in m6A methylation (Probable). {ECO:0000269|PubMed:24981863, ECO:0000305}.Q01658NC2B Protein Dr1chromatin organization [GO:0006325]; histone H3 acetylation [GO:0043966]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; sequence-specific DNA binding [GO:0043565]; TBP-class protein binding [GO:0017025]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]QAda2/Gcn5/Ada3 transcription activator complex [GO:0005671]; nucleus [GO:0005634]FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:8670811}.P07947YESTyrosine-protein kinase YesSUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytosol. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway.axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cellular protein modification process [GO:0006464]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; ephrin receptor signaling pathway [GO:0048013]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; glucose transport [GO:0015758]; innate immune response [GO:0045087]; leukocyte migration [GO:0050900]; peptidyl-tyrosine autophosphorylation [GO:0038083]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell proliferation [GO:0042127]; regulation of vascular permeability [GO:0043114]; T cell costimulation [GO:0031295]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]ATP binding [GO:0005524]; enzyme binding [GO:0019899]; ion channel binding [GO:0044325]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102];actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal < adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule organizing center [GO:0005815]; plasma membrane [GO:0005886]FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. {ECO:0000269|PubMed:11901164, ECO:0000269|PubMed:18479465, ECO:0000269|PubMed:19276087, ECO:0000269|PubMed:21566460, ECO:0000269|PubMed:21713032}.Q9BRK4LZTS2*Leucine zipper putative tumor suppressor 2SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localized to the centrosome throughout the cell cycle. Localized to the midbody in cells undergoing cytokinesis.cytokinesis [GO:0000910]; kidney development [GO:0001822]; microtubule severing [GO:0051013]; mitotic nuclear division [GO:0007067]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell proliferation [GO:0008285]; negative regulation of protein localization to nucleus [GO:1900181]; nuclear export [GO:0051168]; positive regulation of cell death [GO:0010942]; spindle midzone assembly [GO:0051255]; Wnt signaling pathway [GO:0016055]_centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; midbody [GO:0030496]FUNCTION: Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. May negatively regulate axonal outgrowth by preventing the formation of microtubule bundles that are necessary for transport within the elongating axon. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin. {ECO:0000255|HAMAP-Rule:MF_03026, ECO:0000269|PubMed:17000760, ECO:0000269|PubMed:17351128, ECO:0000269|PubMed:17950943, ECO:0000269|PubMed:18490357}.Q8TCD5NT5C,5'(3')-deoxyribonucleotidase, cytosolic typedephosphorylation [GO:0016311]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide catabolic process [GO:0006195]; pyrimidine deoxyribonucleotide catabolic process [GO:0009223]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside catabolic process [GO:0046135]; small molecule metabolic process [GO:0044281]5'-nucleotidase activity [GO:0008253]; metal ion binding [GO:0046872]; nucleotidase activity [GO:0008252]; pyrimidine nucleotide binding [GO:0019103]FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.P54764EPHA4Ephrin type-A receptor 4 Receptor/RTKwSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Early endosome {ECO:0000250}. Note=Clustered upon activation and targeted to early endosome. {ECO:0000250}.adult walking behavior [GO:0007628]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; corticospinal tract morphogenesis [GO:0021957]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]; fasciculation of sensory neuron axon [GO:0097155]; glial cell migration [GO:0008347]; motor neuron axon guidance [GO:0008045]; negative regulation of axon regeneration [GO:0048681]; nephric duct morphogenesis [GO:0072178]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of Rho guanyl-nucleotide exchange factor activity [GO:2001108]; protein autophosphorylation [GO:0046777]; regulation of astrocyte differentiation [GO:0048710]; regulation of axonogenesis [GO:0050770]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of GTPase activity [GO:0043087]ATP binding [GO:0005524]; DH domain binding [GO:0097161]; GPI-linked ephrin receptor activity [GO:0005004]; PH domain binding [GO:0042731]; protein kinase activity [GO:0004672]; transmembrane-ephrin receptor activity [GO:0005005]Uaxon [GO:0030424]; axonal growth cone [GO:0044295]; axon terminus [GO:0043679]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; mitochondrial outer membrane [GO:0005741]; neuromuscular junction [GO:0031594]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]=FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. {ECO:0000269|PubMed:17143272}.Q9BYG3MK67I5MKI67 FHA domain-interacting nucleolar phosphoproteinvSUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Note=Localizes to mitotic chromosomes in conjunction with MKI67.negative regulation of phosphatase activity [GO:0010923]; protein complex assembly [GO:0006461]; rRNA metabolic process [GO:0016072]; rRNA transcription [GO:0009303]condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q8TDP1RNH2CRibonuclease H2 subunit CDNA replication(38)FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the remo< val of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.Q9NPE3NOP10)H/ACA ribonucleoprotein complex subunit 3SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11074001}. Nucleus, Cajal body {ECO:0000269|PubMed:11074001}. Note=Also localized to Cajal bodies (coiled bodies).Bpseudouridine synthesis [GO:0001522]; rRNA processing [GO:0006364]snoRNA binding [GO:0030515]box H/ACA RNP complex [GO:0072588]; Cajal body [GO:0015030]; nucleolus [GO:0005730]; small nucleolar ribonucleoprotein complex [GO:0005732]jFUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. {ECO:0000269|PubMed:15044956}.Q5T7V8GORABRAB6-interacting golgin p53 negative1SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus.Q6NSI4CX057Uncharacterized protein CXorf57Q96RS6NUDC1 NudC domain-containing protein 1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus."immune system process [GO:0002376]Q9NQT4EXOS5Exosome complex component RRP46SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11812149}. Cytoplasm {ECO:0000305|PubMed:11812149}. Nucleus {ECO:0000305|PubMed:11812149}.defense response to virus [GO:0051607]; DNA deamination [GO:0045006]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA 3'-end processing [GO:0031125]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; U4 snRNA 3'-end processing [GO:0034475]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. {ECO:0000269|PubMed:11782436, ECO:0000269|PubMed:21255825}.Q9H3H3CK068UPF0696 protein C11orf68Q96GS6AB17A2Alpha/beta hydrolase domain-containing protein 17AO76070SYUGGamma-synucleinkSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.adult locomotory behavior [GO:0008344]; protein secretion [GO:0009306]; regulation of dopamine secretion [GO:0014059]; regulation of neurotransmitter secretion [GO:0046928]; synapse organization [GO:0050808]; synaptic transmission [GO:0007268]axon [GO:0030424]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]FUNCTION: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity). {ECO:0000250}.Q9H2P0ADNP2Activity-dependent neuroprotector homeobox proteinactivation of protein kinase activity [GO:0032147]; cellular response to extracellular stimulus [GO:0031668]; estrous cycle [GO:0044849]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein binding [GO:0032091]; negative regulation of synaptic transmission [GO:0050805]; nitric oxide homeostasis [GO:0033484]; positive regulation of axon extension [GO:0045773]; positive regulation of cGMP biosynthetic process [GO:0030828]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of synapse assembly [GO:0051965]; regulation of protein ADP-ribosylation [GO:0010835]; regulation of transcription, DNA-templated [GO:0006355]; response to carbohydrate [GO:0009743]; response to inorganic substance [GO:0010035]; short-term memory [GO:0007614]; transcription, DNA-templated [GO:0006351]wchromatin binding [GO:0003682]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; peptide binding [GO:0042277]axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]FUNCTION: Potential transcription factor. May mediate some of the neuroprotective peptide VIP-associated effects involving normal growth and cancer proliferation.Q15651HMGN3BHigh mobility group nucleosome-binding domain-containing protein 3chromatin modification [GO:0016568]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]gchromatin binding [GO:0003682]; DNA binding [GO:0003677]; thyroid hormone receptor binding [GO:0046966]FUNCTION: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity). {ECO:0000250}.Q6ZT12UBR3 E3 ubiquitin-protein ligase UBR3oembryo development [GO:0009790]; in utero embryonic development [GO:0001701]; olfactory behavior [GO:0042048]; protein ubiquitination [GO:00165< 67]; sensory perception of smell [GO:0007608]; suckling behavior [GO:0001967]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]jcytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; ubiquitin ligase complex [GO:0000151]#FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Does not bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.Q5BKZ1ZN326DBIRD complex subunit ZNF3263SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}.mRNA processing [GO:0006397]; regulation of DNA-templated transcription, elongation [GO:0032784]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core binding [GO:0000993]DBIRD complex [GO:0044609]; intracellular membrane-bounded organelle [GO:0043231]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. {ECO:0000269|PubMed:22446626}.Q13111CAF1A%Chromatin assembly factor 1 subunit A$Chromatin Structure and ModificationWSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10052459}. Note=DNA replication foci.cell cycle [GO:0007049]; chromatin assembly [GO:0031497]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent nucleosome assembly [GO:0006335]; protein complex assembly [GO:0006461]chromatin binding [GO:0003682]; chromo shadow domain binding [GO:0070087]; identical protein binding [GO:0042802]; unfolded protein binding [GO:0051082]nCAF-1 complex [GO:0033186]; nuclear chromatin [GO:0000790]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci (By similarity). {ECO:0000250, ECO:0000269|PubMed:15327775}.P0CB44SKA2L:Putative spindle and kinetochore-associated protein 2-likeQ5T1C6THEM4"Acyl-coenzyme A thioesterase THEM4 inhibitor/AKT?SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11598301}. Cell projection, ruffle membrane {ECO:0000269|PubMed:11598301}. Cytoplasm {ECO:0000269|PubMed:19604401}. Mitochondrion {ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19421406, ECO:0000269|PubMed:19604401}. Mitochondrion inner membrane; Peripheral membrane protein {ECO:0000269|PubMed:19168129}. Mitochondrion intermembrane space {ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19604401}. Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. {ECO:0000269|PubMed:19168129}.-epidermal growth factor receptor signaling pathway [GO:0007173]; fatty acid metabolic process [GO:0006631]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; protein kinase B signaling [GO:0043491]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108]-palmitoyl-CoA hydrolase activity [GO:0016290]cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane. {ECO:0000269|PubMed:11598301, ECO:0000269|PubMed:17615157, ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19421406, ECO:0000269|PubMed:19453107, ECO:0000269|PubMed:22871024}.Q9BZ95NSD3'Histone-lysine N-methyltransferase NSD3chromatin organization [GO:0006325]; histone methylation [GO:0016571]; negative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]histone-lysine N-methyltransferase activity [GO:0018024]; histone methyltransferase activity (H3-K27 specific) [GO:0046976]; histone methyltransferase activity (H3-K4 specific) [GO:0042800]; zinc ion binding [GO:0008270]FUNCTION: Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression. {ECO:0000269|PubMed:16682010}.P51531SMCA2.Probable global transcription activator SNF2L2aortic smooth muscle cell differentiation [GO:0035887]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nervous system development [GO:0007399]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spermatid development [GO:0007286]2ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA-dependent ATPase activity [GO:0008094]; helicase activity [GO:0004386]; RNA polymerase II transcription coactivator activity [GO:0001105]; transcription coactivator activity [GO:0003713]; transcription regulatory region DNA binding [GO:0044212] intermediate filament cytoskeleton [GO:0045111]; intracellular membrane-bounded organelle [GO:0043231]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]vFUNCTION: Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron< -specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.Q96T23RSF1Remodeling and spacing factor 1YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788598, ECO:0000269|PubMed:11944984}.CENP-A containing nucleosome assembly [GO:0034080]; chromatin remodeling [GO:0006338]; DNA-templated transcription, initiation [GO:0006352]; negative regulation of DNA binding [GO:0043392]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleosome assembly [GO:0006334]; nucleosome positioning [GO:0016584]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of viral transcription [GO:0050434]Hnucleoplasm [GO:0005654]; nucleus [GO:0005634]; RSF complex [GO:0031213]FUNCTION: Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex. Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain. {ECO:0000269|PubMed:11788598, ECO:0000269|PubMed:12972596}.Q92562FIG4 Polyphosphoinositide phosphatasetSUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:17556371}. Note=Localization requires VAC14 and PIKFYVE.locomotory behavior [GO:0007626]; myelin assembly [GO:0032288]; negative regulation of myelination [GO:0031642]; neuron development [GO:0048666]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; pigmentation [GO:0043473]; positive regulation of neuron projection development [GO:0010976]; small molecule metabolic process [GO:0044281]; vacuole organization [GO:0007033]phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; phosphatidylinositol-4-phosphate phosphatase activity [GO:0043812]early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; recycling endosome [GO:0055037]FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide substrates in the order PtdIns(4,5)P2 > PtdIns(3,5)P2 > PtdIns(3,4,5)P3. Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. {ECO:0000269|PubMed:17556371}.P00749UROK$Urokinase-type plasminogen activatorJangiogenesis [GO:0001525]; blood coagulation [GO:0007596]; cellular response to fluid shear stress [GO:0071498]; cellular response to glucose stimulus [GO:0071333]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to hypoxia [GO:0071456]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to staurosporine [GO:0072734]; chemotaxis [GO:0006935]; embryo implantation [GO:0007566]; fibrinolysis [GO:0042730]; neuron death [GO:0070997]; plasminogen activation [GO:0031639]; positive regulation of cell proliferation [GO:0008284]; positive regulation of ovulation [GO:0060279]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of smooth muscle cell migration [GO:0014911]; proteolysis [GO:0006508]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of hepatocyte proliferation [GO:2000345]; regulation of receptor activity [GO:0010469]; regulation of smooth muscle cell-matrix adhesion [GO:2000097]; regulation of smooth muscle cell migration [GO:0014910]; regulation of wound healing [GO:0061041]; response to activity [GO:0014823]; response to hyperoxia [GO:0055093]; signal transduction [GO:0007165]; skeletal muscle tissue regeneration [GO:0043403]; smooth muscle cell migration [GO:0014909]; spermatogenesis [GO:0007283]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]YFUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.Q6KF10GDF6Growth/differentiation factor 6BMP/R=SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23307924}.kactivin receptor signaling pathway [GO:0032924]; apoptotic process [GO:0006915]; BMP signaling pathway [GO:0030509]; cell development [GO:0048468]; growth [GO:0040007]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of apoptotic process [GO:0042981]; regulation of MAPK cascade [GO:0043408]; retinal cell apoptotic process [GO:1990009]; SMAD protein signal transduction [GO:0060395] extracellular space [GO:0005615]YFUNCTION: Growth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map. Required for normal formation of bones and joints in the limbs, skull, and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. May signal through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A. {ECO:0000269|PubMed:23307924}.Q4LDE5SVEP1RSushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16206243}. Membrane {ECO:0000269|PubMed:16206243}; Peripheral membrane protein {ECO:0000269|PubMed:16206243}.HFUNCTION: May play a role in the cell attachment process. {ECO:0000250}.P11226MBL2Mannose-binding protein C<SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7982896}.Vacute-phase response [GO:0006953]; complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; complement activation, lectin pathway [GO:0001867]; defense response to bacterium [GO:0042742]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; killing by host of symbiont cells [GO:0051873]; negative regulation of growth of symbiont in host [GO:0044130]; negative regulation of viral process [GO:0048525]; opsonization [GO:0008228]; positive regulation of phagocytosis [GO:0050766]; response to oxidative stress [GO:0006979]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; mannose binding [GO:0005537]; receptor binding [GO:0005102]|cell surface [GO:0009986]; collagen trimer [GO:0005581]; extracellular region [GO:0005576]; extracellular space [GO:0005615]FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. May bind DNA. {ECO:0000269|PubMed:14515269}.P42684ABL2!Abelson tyrosine-protein kinase 2actin filament bundle assembly [GO:0051017]; alpha-beta T cell differentiation [GO:0046632]; axon guidance [GO:0007411]; Bergmann glial cell differentiation [GO:0060020]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular protein localization [GO:0034613]; cellular protein modification process [GO:0006464]; cellular response to retinoic acid [GO:0071300]; c< erebellum morphogenesis [GO:0021587]; dendrite morphogenesis [GO:0048813]; dendritic spine maintenance [GO:0097062]; epidermal growth factor receptor signaling pathway [GO:0007173]; exploration behavior [GO:0035640]; innate immune response [GO:0045087]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of Rho protein signal transduction [GO:0035024]; neuromuscular process controlling balance [GO:0050885]; neuron remodeling [GO:0016322]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; phagocytosis [GO:0006909]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-gamma secretion [GO:1902715]; positive regulation of interleukin-2 secretion [GO:1900042]; positive regulation of neuron projection development [GO:0010976]; positive regulation of oxidoreductase activity [GO:0051353]; positive regulation of phospholipase C activity [GO:0010863]; positive regulation of protein binding [GO:0032092]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of apoptotic process [GO:0042981]; regulation of autophagy [GO:0010506]; regulation of cell adhesion [GO:0030155]; regulation of cell motility [GO:2000145]; regulation of cell proliferation [GO:0042127]; regulation of endocytosis [GO:0030100]; regulation of extracellular matrix organization [GO:1903053]; signal transduction [GO:0007165]; substrate-dependent cell migration, cell extension [GO:0006930]; visual learning [GO:0008542]bactin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; lamellipodium [GO:0030027]; phagocytic cup [GO:0001891]FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. {ECO:0000269|PubMed:15735735, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:18945674}.O43426SYNJ1Synaptojanin-1inositol phosphate dephosphorylation [GO:0046855]; inositol phosphate metabolic process [GO:0043647]; neurotransmitter transport [GO:0006836]; phosphate-containing compound metabolic process [GO:0006796]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid metabolic process [GO:0006644]; positive regulation of synaptic vesicle uncoating [GO:1903390]; regulation of synaptic vesicle membrane organization [GO:1901632]; small molecule metabolic process [GO:0044281]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle priming [GO:0016082]; synaptic vesicle transport [GO:0048489]; synaptic vesicle uncoating [GO:0016191]inositol-polyphosphate 5-phosphatase activity [GO:0004445]; nucleotide binding [GO:0000166]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; phosphatidylinositol phosphate 5-phosphatase activity [GO:0034595]; RNA binding [GO:0003723]0cytosol [GO:0005829]; membrane coat [GO:0030117]SFUNCTION: Inositol 5-phosphatase which has a role in clathrin-mediated endocytosis.Q96EK9KTI12Protein KTI12 homologO43813LANC1LanC-like protein 1SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note=Detected at the surface of Maurer's clefts in malaria-infected erythrocytes at late stages of parasite development.9G-protein coupled receptor signaling pathway [GO:0007186]catalytic activity [GO:0003824]; glutathione binding [GO:0043295]; G-protein coupled receptor activity [GO:0004930]; low-density lipoprotein particle receptor binding [GO:0050750]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]^FUNCTION: May play a role in EPS8 signaling. Binds glutathione. {ECO:0000269|PubMed:19528316}.Q96AM1MRGRF/Mas-related G-protein coupled receptor member FFUNCTION: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity). {ECO:0000250}.Q14192FHL2%Four and a half LIM domains protein 2)zinc finger transcription factor(PC00244)gandrogen receptor signaling pathway [GO:0030521]; atrial cardiac muscle cell development [GO:0055014]; cellular lipid metabolic process [GO:0044255]; heart trabecula formation [GO:0060347]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of transcription, DNA-templated [GO:0045893]; response to hormone [GO:0009725]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; ventricular cardiac muscle cell development [GO:0055015]androgen receptor binding [GO:0050681]; identical protein binding [GO:0042802]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; focal adhesion [GO:0005925]; M band [GO:0031430]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Z disc [GO:0030018]FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation. {ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16652157, ECO:0000269|PubMed:18853468}.Q8IVF2AHNK2Protein AHNAK2costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]; Z disc [GO:0030018]O60507TPST1#Protein-tyrosine sulf< otransferase 1Linflammatory response [GO:0006954]; peptidyl-tyrosine sulfation [GO:0006478]7protein-tyrosine sulfotransferase activity [GO:0008476]^FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.Q14999CUL7Cullin-7SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Golgi apparatus. Note=Colocalizes with FBXW8 at the Golgi apparatus in neurons; localization to Golgi is mediated by OBSL1. During mitosis, localizes to the mitotic apparatus (PubMed:24793695). CCDC8 is required for centrosomal location (PubMed:24793695). {ECO:0000269|PubMed:24793695}.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; epithelial to mesenchymal transition [GO:0001837]; Golgi organization [GO:0007030]; IRE1-mediated unfolded protein response [GO:0036498]; microtubule cytoskeleton organization [GO:0000226]; mitotic cytokinesis [GO:0000281]; placenta development [GO:0001890]; positive regulation of dendrite morphogenesis [GO:0050775]; protein ubiquitination [GO:0016567]; proteolysis [GO:0006508]; regulation of mitotic nuclear division [GO:0007088]; ubiquitin-dependent protein catabolic process [GO:0006511]; vasculogenesis [GO:0001570]; viral process [GO:0016032]43M complex [GO:1990393]; anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; Cul7-RING ubiquitin ligase complex [GO:0031467]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]VFUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695). Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5 (PubMed:24793696). Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1 (PubMed:21572988, PubMed:24362026). Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain (PubMed:21572988). Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) (PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradatation, thereby affecting cell proliferation and differentiation (PubMed:24362026). Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development (PubMed:20139075). Does not promote polyubiquitination and proteasomal degradation of p53/TP53 (PubMed:16547496, PubMed:17332328). While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions. {ECO:0000269|PubMed:16547496, ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745, ECO:0000269|PubMed:20139075, ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.Q03169TNAP2-Tumor necrosis factor alpha-induced protein 2xangiogenesis [GO:0001525]; cell differentiation [GO:0030154]; exocyst localization [GO:0051601]; exocytosis [GO:0006887]6exocyst [GO:0000145]; extracellular space [GO:0005615]IFUNCTION: May play a role as a mediator of inflammation and angiogenesis.Q9UJ41RABX5Rab5 GDP/GTP exchange factorSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12505986}. Early endosome {ECO:0000269|PubMed:12505986}. Recycling endosome {ECO:0000269|PubMed:12505986}.endocytosis [GO:0006897]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 secretion [GO:1900165]; negative regulation of Kit signaling pathway [GO:1900235]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mast cell degranulation [GO:0043305]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of receptor-mediated endocytosis [GO:0048261]; positive regulation of GTPase activity [GO:0043547]; protein targeting to membrane [GO:0006612]; regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060368]DNA binding [GO:0003677]; Rab GTPase binding [GO:0017137]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]Rearly endosome [GO:0005769]; recycling endosome [GO:0055037]; vesicle [GO:0031982]FUNCTION: Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity). {ECO:0000250}.Q9P021CRIPT!Cysteine-rich PDZ-binding proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DLG4 in asymmetric synapses. {ECO:0000250}.cytoplasmic microtubule organization [GO:0031122]; establishment of protein localization [GO:0045184]; protein localization to microtubule [GO:0035372]; regulation of postsynaptic density protein 95 clustering [GO:1902897]microtubule binding [GO:0008017]; PDZ domain binding [GO:0030165]; protein complex binding [GO:0032403]; scaffold protein binding [GO:0097110]cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]pFUNCTION: Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses. {ECO:0000250|UniProtKB:Q792Q4}.Q96L12CALR3Calreticulin-3vSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:21590275}.]cell differentiation [GO:0030154]; protein folding [GO:0006457]; spermatogenesis [GO:0007283]Ccalcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]#FUNCTION: During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium-binding may be absent or much lower than that of CALR. {ECO:0000250, ECO:0000269|PubMed:21590275}.Q9NWQ8PHAG1HPhosphoprotein associated with glycosphingolipid-enriched microdomains 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}; Single-pass type III membrane protein {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}. Note=Present in lipid rafts._epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular signal transduction [GO:0035556]; negative regulation of T cell activation [GO:0050868]; positive regulation of signal transduction [GO:0009967]; regulation of T cell activation [GO:0050863]; signal transduction [GO:0007165]; T cell receptor signaling pathway [GO:0050852]FSH2 domain binding [GO:0042169]; SH3/SH2 adaptor activity [GO:0005070]integral component of membrane [GO:0016021]; intracellular [GO:0005622]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell ad< hesion signaling. {ECO:0000269|PubMed:10790433}.Q9HBG6IF122,Intraflagellar transport protein 122 homologSUBCELLULAR LOCATION: Cytoplasm. Cell projection, cilium {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Localizes to photoreceptor connecting cilia. {ECO:0000250}.camera-type eye morphogenesis [GO:0048593]; ciliary receptor clustering involved in smoothened signaling pathway [GO:0060830]; cilium assembly [GO:0042384]; cilium morphogenesis [GO:0060271]; embryonic body morphogenesis [GO:0010172]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic heart tube development [GO:0035050]; embryonic heart tube left/right pattern formation [GO:0060971]; establishment of protein localization to organelle [GO:0072594]; intraciliary anterograde transport [GO:0035720]; intraciliary retrograde transport [GO:0035721]; intraciliary transport involved in cilium morphogenesis [GO:0035735]; limb development [GO:0060173]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of smoothened signaling pathway involved in ventral spinal cord patterning [GO:0021914]; neural tube closure [GO:0001843]; organelle organization [GO:0006996]; protein localization to cilium [GO:0061512]; signal transduction downstream of smoothened [GO:0007227]; smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:0060831]ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytoplasm [GO:0005737]; intraciliary transport particle A [GO:0030991]; membrane [GO:0016020]; photoreceptor connecting cilium [GO:0032391]; primary cilium [GO:0072372]FUNCTION: Required for cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia (By similarity). {ECO:0000250}.Q9BQC3DPH2"Diphthamide biosynthesis protein 2cellular protein metabolic process [GO:0044267]; peptidyl-diphthamide biosynthetic process from peptidyl-histidine [GO:0017183]; post-translational protein modification [GO:0043687]C2-(3-amino-3-carboxypropyl)histidine synthase activity [GO:0090560]FUNCTION: Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). {ECO:0000250}.P07205PGK2Phosphoglycerate kinase 2activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; sperm motility [GO:0030317]scytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686]Q9Y2X0MED166Mediator of RNA polymerase II transcription subunit 16androgen receptor signaling pathway [GO:0030521]; gene expression [GO:0010467]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; positive regulation of receptor activity [GO:2000273]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]2catalytic activity [GO:0003824]; receptor activity [GO:0004872]; thyroid hormone receptor binding [GO:0046966]; thyroid hormone receptor coactivator activity [GO:0030375]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; vitamin D receptor binding [GO:0042809]DFUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:10198638, ECO:0000269|PubMed:10235266}.O43795MYO1BUnconventional myosin-Ibactin filament-based movement [GO:0030048]; actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; post-Golgi vesicle-mediated transport [GO:0006892]actin-dependent ATPase activity [GO:0030898]; actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]Nactin filament [GO:0005884]; brush border [GO:0005903]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; myosin complex [GO:0016459]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport. {ECO:0000250}.P51157RAB28Ras-related protein Rab-28SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body. Note=Expressed in the basal body and ciliary rootlet of the photoreceptors. {ECO:0000250}.Tsmall GTPase mediated signal transduction [GO:0007264]; toxin transport [GO:1901998]sciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]Q9UMX0UBQL1 Ubiquilin-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:23979357}. Nucleus {ECO:0000269|PubMed:23979357}. Endoplasmic reticulum {ECO:0000269|PubMed:19822669}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:23459205}. Cell membrane {ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:23307288}. Note=Detected in neuronal processes and at synapses (By similarity). Recruited to the ER during ER-associated protein degradation (ERAD) (PubMed:19822669). Isoform 1 and isoform 3 colocalize with PSEN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes (PubMed:21143716). Colocalizes with ORAI1 and TICAM1 in the autophagosome (PubMed:23307288, PubMed:21695056). Colocalizes with EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and with EPS15 also in aggresomes (PubMed:16159959). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288}.aggrephagy [GO:0035973]; cellular response to hypoxia [GO:0071456]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of autophagosome fusion [GO:1902453]; negative regulation of store-operated calcium channel activity [GO:1901340]; negative regulation of toll-like receptor 3 signaling pathway [GO:0034140]; positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; positive regulation of protein ubiquitination [GO:0031398]; regulation of autophagosome assembly [GO:2000785]; regulation of macroautophagy [GO:0016241]; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902175]; regulation of protein ubiquitination [GO:0031396]; response to endoplasmic reticulum stress [GO:0034976]gidentical protein binding [GO:0042802]; kinase binding [GO:0019900]; polyubiquitin binding [GO:0031593]5aggresome [GO:0016235]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]; pro< tein complex [GO:0043234]o FUNCTION: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:15147878). Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:19822669, PubMed:18307982). Isoform 1, isoform 2 and isoform 3 play a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress (PubMed:18953672). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway (PubMed:21695056). Isoform 1 and isoform 3 play a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis (PubMed:21143716). Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:18953672, ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:23459205, ECO:0000303|PubMed:15147878}.P29373RABP2(Cellular retinoic acid-binding protein 2SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus. Note=Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.embryonic forelimb morphogenesis [GO:0035115]; epidermis development [GO:0008544]; positive regulation of collateral sprouting [GO:0048672]; regulation of transcription, DNA-templated [GO:0006355]; retinoic acid metabolic process [GO:0042573]; signal transduction [GO:0007165]retinal binding [GO:0016918]; retinoic acid binding [GO:0001972]; retinoid binding [GO:0005501]; retinol binding [GO:0019841]; transporter activity [GO:0005215]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]FUNCTION: Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.P49458SRP09)Signal recognition particle 9 kDa proteincellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; negative regulation of translational elongation [GO:0045900]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]g7S RNA binding [GO:0008312]; RNA binding [GO:0003723]; signal recognition particle binding [GO:0005047]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]; signal recognition particle receptor complex [GO:0005785];FUNCTION: Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.P46531NOTC1(Neurogenic locus notch homolog protein 1 SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus {ECO:0000250}. Note=Following proteolytical processing NICD is translocated to the nucleus. {ECO:0000250}.aortic valve morphogenesis [GO:0003180]; apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; arterial endothelial cell differentiation [GO:0060842]; astrocyte differentiation [GO:0048708]; atrioventricular node development [GO:0003162]; atrioventricular valve morphogenesis [GO:0003181]; auditory receptor cell fate commitment [GO:0009912]; axonogenesis [GO:0007409]; branching morphogenesis of an epithelial tube [GO:0048754]; cardiac atrium morphogenesis [GO:0003209]; cardiac chamber formation [GO:0003207]; cardiac epithelial to mesenchymal transition [GO:0060317]; cardiac left ventricle morphogenesis [GO:0003214]; cardiac muscle cell proliferation [GO:0060038]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac right atrium morphogenesis [GO:0003213]; cardiac right ventricle formation [GO:0003219]; cardiac septum morphogenesis [GO:0060411]; cardiac vascular smooth muscle cell development [GO:0060948]; cardiac ventricle morphogenesis [GO:0003208]; cell differentiation in spinal cord [GO:0021515]; cell fate specification [GO:0001708]; cell migration involved in endocardial cushion formation [GO:0003273]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; cilium morphogenesis [GO:0060271]; collecting duct development [GO:0072044]; compartment pattern specification [GO:0007386]; coronary artery morphogenesis [GO:0060982]; coronary vein morphogenesis [GO:0003169]; determination of left/right symmetry [GO:0007368]; distal tubule development [GO:0072017]; embryonic hindlimb morphogenesis [GO:0035116]; endocardial cell differentiation [GO:0060956]; endocardial cushion morphogenesis [GO:0003203]; endocardium development [GO:0003157]; endocardium morphogenesis [GO:0003160]; endoderm development [GO:0007492]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; forebrain development [GO:0030900]; foregut morphogenesis [GO:0007440]; gene expression [GO:0010467]; glomerular mesangial cell development [GO:0072144]; growth involved in heart morphogenesis [GO:0003241]; hair follicle morphogenesis [GO:0031069]; heart development [GO:0007507]; heart looping [GO:0001947]; heart trabecula morphogenesis [GO:0061384]; humoral immune response [GO:0006959]; immune response [GO:0006955]; inflammatory response to antigenic stimulus [GO:0002437]; interleukin-4 secretion [GO:0072602]; in utero embryonic development [GO:0001701]; keratinocyte differentiation [GO:0030216]; left/right axis specification [GO:0070986]; liver development [GO:0001889]; lung development [GO:0030324]; mesenchymal cell development [GO:0014031]; mitral valve formation [GO:0003192]; negative regulation of anoikis [GO:2000811]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of catalytic activity [GO:0043086]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of endothelial cell chemotaxis [GO:2001027]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myotube differentiation [GO:0010832]; < negative regulation of neurogenesis [GO:0050768]; negative regulation of oligodendrocyte differentiation [GO:0048715]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of photoreceptor cell differentiation [GO:0046533]; negative regulation of pro-B cell differentiation [GO:2000974]; negative regulation of stem cell differentiation [GO:2000737]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neural tube development [GO:0021915]; neuronal stem cell maintenance [GO:0097150]; Notch receptor processing [GO:0007220]; Notch signaling involved in heart development [GO:0061314]; Notch signaling pathway [GO:0007219]; Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation [GO:0003270]; oligodendrocyte differentiation [GO:0048709]; organ regeneration [GO:0031100]; pericardium morphogenesis [GO:0003344]; positive regulation of apoptotic process [GO:0043065]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of endothelial cell differentiation [GO:0045603]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061419]; positive regulation of transcription of Notch receptor target [GO:0007221]; prostate gland epithelium morphogenesis [GO:0060740]; pulmonary valve morphogenesis [GO:0003184]; regulation of epithelial cell proliferation involved in prostate gland development [GO:0060768]; regulation of extracellular matrix assembly [GO:1901201]; regulation of somitogenesis [GO:0014807]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation [GO:0003256]; response to corticosteroid [GO:0031960]; response to lipopolysaccharide [GO:0032496]; response to muramyl dipeptide [GO:0032495]; secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development [GO:0060528]; skeletal muscle cell differentiation [GO:0035914]; somatic stem cell division [GO:0048103]; spermatogenesis [GO:0007283]; sprouting angiogenesis [GO:0002040]; tissue regeneration [GO:0042246]; transcription initiation from RNA polymerase II promoter [GO:0006367]; tube formation [GO:0035148]; vasculogenesis involved in coronary vascular morphogenesis [GO:0060979]; venous endothelial cell differentiation [GO:0060843]; ventricular septum morphogenesis [GO:0060412]; ventricular trabecula myocardium morphogenesis [GO:0003222]calcium ion binding [GO:0005509]; chromatin DNA binding [GO:0031490]; core promoter binding [GO:0001047]; enzyme binding [GO:0019899]; enzyme inhibitor activity [GO:0004857]; receptor activity [GO:0004872]; RNA polymerase II transcription factor binding transcription activator activity [GO:0001190]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; MAML1-RBP-Jkappa- ICN1 complex [GO:0002193]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000269|PubMed:20616313}.Q9BV40VAMP8%Vesicle-associated membrane protein 8SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:9614193}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:O70404}; Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells. Midbody region during cytokinesis. Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (By similarity). {ECO:0000250|UniProtKB:Q9WUF4}.autophagosome fusion [GO:0000046]; membrane organization [GO:0061024]; mucus secretion [GO:0070254]; negative regulation of secretion by cell [GO:1903531]; positive regulation of histamine secretion by mast cell [GO:1903595]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; regulation of protein localization to plasma membrane [GO:1903076]; vesicle fusion [GO:0006906]; viral entry into host cell [GO:0046718]qchloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]*azurophil granule membrane [GO:0035577]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; mucin granule [GO:0098594]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule membrane [GO:0030667]; SNARE complex [GO:0031201]; vesicle [GO:0031982]FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary< t-SNARE complex (PubMed:23217709, PubMed:25686604). Also required for dense-granule secretion in platelets (PubMed:12130530). Plays also a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:12130530, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604}.Q96J02ITCH)E3 ubiquitin-protein ligase Itchy homologSUBCELLULAR LOCATION: Cell membrane. Cytoplasm {ECO:0000250}. Nucleus. Note=Associates with endocytic vesicles. May be recruited to exosomes by NDFIP1.0apoptotic process [GO:0006915]; defense response to virus [GO:0051607]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of alpha-beta T cell proliferation [GO:0046642]; negative regulation of apoptotic process [GO:0043066]; negative regulation of defense response to virus [GO:0050687]; negative regulation of JNK cascade [GO:0046329]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of type I interferon production [GO:0032480]; Notch signaling pathway [GO:0007219]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of T cell anergy [GO:0002669]; protein K29-linked ubiquitination [GO:0035519]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of cell growth [GO:0001558]; regulation of protein deubiquitination [GO:0090085]; ubiquitin-dependent protein catabolic process [GO:0006511]; viral entry into host cell [GO:0046718]CXCR chemokine receptor binding [GO:0045236]; ligase activity [GO:0016874]; ribonucleoprotein complex binding [GO:0043021]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]. FUNCTION: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). {ECO:0000250|UniProtKB:Q8C863, ECO:0000269|PubMed:14602072, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:17028573, ECO:0000269|PubMed:18628966, ECO:0000269|PubMed:18718448, ECO:0000269|PubMed:18718449, ECO:0000269|PubMed:19131965, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:20392206, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:25631046}.Q9BS26ERP44)Endoplasmic reticulum resident protein 44cell redox homeostasis [GO:0045454]; glycoprotein metabolic process [GO:0009100]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]cell surface [GO:0009986]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]FUNCTION: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum. {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:14517240}.P23634AT2B4-Plasma membrane calcium-transporting ATPase 4{blood coagulation [GO:0007596]; calcium ion export [GO:1901660]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; cellular calcium ion homeostasis [GO:0006874]; cellular response to epinephrine stimulus [GO:0071872]; hippocampus development [GO:0021766]; ion transmembrane transport [GO:0034220]; negative regulation of adrenergic receptor signaling pathway involved in heart process [GO:1901205]; negative regulation of arginine catabolic process [GO:1900082]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of citrulline biosynthetic process [GO:1903249]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of nitric oxide mediated signal transduction [GO:0010751]; negative regulation of nitric-oxide synthase activity [GO:0051001]; negative regulation of peptidyl-cysteine S-nitrosylation [GO:1902083]; negative regulation of the force of heart contraction [GO:0098736]; neural retina development [GO:0003407]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of cell cycle G1/S phase transition [GO:1902806]; regulation of sodium ion transmembrane transport [GO:1902305]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to hydrostatic pressure [GO:0051599]; spermatogenesis [GO:0007283]; transmembrane transport [GO:0055085]CATP binding [GO:0005524]; calcium-transporting ATPase activity [GO:0005388]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase inhibitor activity [GO:0036487]; protein phosphatase 2B binding [GO:0030346]; scaffold protein binding [GO:0097110]5basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; integral component of plasma membrane [GO:0< 005887]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; sperm principal piece [GO:0097228]; T-tubule [GO:0030315]; Z disc [GO:0030018]Q5TC84OGRL1,Opioid growth factor receptor-like protein 1Q8IVL6P3H3Prolyl 3-hydroxylase 3fextracellular matrix organization [GO:0030198]; negative regulation of cell proliferation [GO:0008285]|iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-proline 3-dioxygenase activity [GO:0019797]FUNCTION: Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V. {ECO:0000250}.Q13490BIRC2+Baculoviral IAP repeat-containing protein 26SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells.4 apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; innate immune response [GO:0045087]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; negative regulation of ripoptosome assembly involved in necroptotic process [GO:1902443]; NIK/NF-kappaB signaling [GO:0038061]; placenta development [GO:0001890]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein K48-linked ubiquitination [GO:1902524]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of protein monoubiquitination [GO:1902527]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein heterooligomerization [GO:0051291]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of cell differentiation [GO:0045595]; regulation of cell proliferation [GO:0042127]; regulation of cysteine-type endopeptidase activity [GO:2000116]; regulation of inflammatory response [GO:0050727]; regulation of innate immune response [GO:0045088]; regulation of necroptotic process [GO:0060544]; regulation of necrotic cell death [GO:0010939]; regulation of nucleotide-binding oligomerization domain containing signaling pathway [GO:0070424]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of RIG-I signaling pathway [GO:0039535]; regulation of toll-like receptor signaling pathway [GO:0034121]; regulation of transcription, DNA-templated [GO:0006355]; response to cAMP [GO:0051591]; response to ethanol [GO:0045471]; response to hypoxia [GO:0001666]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; transcription, DNA-templated [GO:0006351]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]%cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; ligase activity [GO:0016874]; protein N-terminus binding [GO:0047485]; transcription coactivator activity [GO:0003713]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleus [GO:0005634]; XY body [GO:0001741]uFUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. {ECO:0000269|PubMed:15665297, ECO:0000269|PubMed:18082613, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:21653699, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969}.P51809VAMP7%Vesicle-associated membrane protein 7#SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type IV membrane protein {ECO:0000269|PubMed:17897319}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney (By similarity). {ECO:0000250}.~calcium ion-dependent exocytosis [GO:0017156]; endosome to lysosome transport [GO:0008333]; eosinophil degranulation [GO:0043308]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi to plasma membrane protein transport [GO:0043001]; membrane organization [GO:0061024]; natural killer cell degranulation [GO:0043320]; neutrophil degranulation [GO:0043312]; phagocytosis, engulfment [GO:0006911]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of histamine secretion by mast cell [GO:1903595]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of protein targeting to vacuolar membrane [GO:1900483]; SNARE complex assembly [GO:0035493]; triglyceride transport [GO:0034197]; vesicle fusion [GO:0006906]; vesicle fusion with Golgi apparatus [GO:0048280]; vesicle-mediated transport [GO:0016192]; vesicle transport along microtubule [GO:0047496]apical part of cell [GO:0045177]; azurophil granule membrane [GO:0035577]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicl< e [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; pseudopodium [GO:0031143]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667]; SNARE complex [GO:0031201]; synapse [GO:0045202]; trans-Golgi network [GO:0005802]; transport vesicle membrane [GO:0030658]FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation. {ECO:0000269|PubMed:10888671, ECO:0000269|PubMed:16677249, ECO:0000269|PubMed:18042464}.O14974MYPT1,Protein phosphatase 1 regulatory subunit 12A PP1R12a/b/cSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:18477460}. Note=Along actomyosin filaments and stress fibers.1centrosome organization [GO:0051297]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of catalytic activity [GO:0043086]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein dephosphorylation [GO:0006470]; regulation of cell adhesion [GO:0030155]; regulation of myosin-light-chain-phosphatase activity [GO:0035507]; regulation of nucleocytoplasmic transport [GO:0046822]; small GTPase mediated signal transduction [GO:0007264]14-3-3 protein binding [GO:0071889]; enzyme inhibitor activity [GO:0004857]; phosphatase regulator activity [GO:0019208]; protein kinase binding [GO:0019901]; signal transducer activity [GO:0004871]actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]; PTW/PP1 phosphatase complex [GO:0072357]:FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:20354225}.Q8IWC1MA7D3 MAP7 domain-containing protein 3SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15561729}. Note=Localizes to the microtubules throughout mitosis. {ECO:0000269|PubMed:22142902}.[microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]imicrotubule binding [GO:0008017]; structural molecule activity [GO:0005198]; tubulin binding [GO:0015631]actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]zFUNCTION: Promotes the assembly and stability of microtubules. {ECO:0000269|PubMed:22142902, ECO:0000269|PubMed:24927501}.Q9BTX7TTPAL&Alpha-tocopherol transfer protein-like1intracellular [GO:0005622]; membrane [GO:0016020]NFUNCTION: May act as a protein that binds a hydrophobic ligand. {ECO:0000305}.Q8NC44F134AProtein FAM134AQ5T1M5FKB15FK506-binding protein 15SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, axon {ECO:0000250}. Early endosome {ECO:0000269|PubMed:19121306}. Note=Present in axons and neuronal growth cones. {ECO:0000250}.pendocytosis [GO:0006897]; negative regulation of phosphatase activity [GO:0010923]; protein folding [GO:0006457]|actin filament [GO:0005884]; axon [GO:0030424]; early endosome [GO:0005769]; growth cone [GO:0030426]; membrane [GO:0016020]6FUNCTION: May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement. {ECO:0000250, ECO:0000269|PubMed:19121306}.Q9UNN5FAF1FAS-associated factor 1Zapoptotic process [GO:0006915]; cell death [GO:0008219]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell death [GO:0010942]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of protein complex assembly [GO:0031334]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell adhesion [GO:0030155]; regulation of protein catabolic process [GO:0042176]; regulation of protein kinase activity [GO:0045859]heat shock protein binding [GO:0031072]; NF-kappaB binding [GO:0051059]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]CD95 death-inducing signaling complex [GO:0031265]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]@FUNCTION: Potentiates but cannot initiate FAS-induced apoptosis.O75717WDHD1+WD repeat and HMG-box DNA-binding protein 1yheterochromatin maintenance [GO:0070829]; regulation of chromosome organization [GO:0033044]; RNA processing [GO:0006396]Rchromatin binding [GO:0003682]; DNA binding [GO:0003677]; RNA binding [GO:0003723]]chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. {ECO:0000269|PubMed:19805216}.Q8WZB0CI1305Putative uncharacterized protein encoded by LINC00476Q6KCM7SCMC25Calcium-binding mitochondrial carrier protein SCaMC-2SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}; Multi-pass membrane protein {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}.aadipose tissue development [GO:0060612]; ATP metabolic process [GO:0046034]; calcium ion transmembrane transport [GO:0070588]; camera-type eye development [GO:0043010]; cellular respiration [GO:0045333]; multicellular organism growth [GO:0035264]; response to activity [GO:0014823]; response to dietary excess [GO:0002021]; response to food [GO:0032094]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria. {ECO:0000269|PubMed:15123600}.Q13509TBB3Tubulin beta-3 chainde novo' posttranslational protein folding [GO:0051084]; axon guidance [GO:0007411]; cellular protein metabolic process [GO:0044267]; microtubule-based process [GO:0007017]; mitotic nuclear division [GO:0007067]; protein folding [GO:0006457]; protein polymerization [GO:0051258]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; peptide binding [GO:0042277]; structural constituent of cytoskeleton [GO:0005200]axon [GO:0030424]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]FUNCTION: Tubulin is the major constituent of microtubules. It binds two< moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and mantainance. {ECO:0000269|PubMed:20074521}.Q9ULL5PRR12Proline-rich protein 12O00220TR10A5Tumor necrosis factor receptor superfamily member 10Ap53 negative feedbackactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097296]; activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; necroptotic process [GO:0070266]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of necrotic cell death [GO:0010939]; signal transduction [GO:0007165]; TRAIL-activated apoptotic signaling pathway [GO:0036462]death receptor activity [GO:0005035]; protease binding [GO:0002020]; receptor activity [GO:0004872]; TRAIL binding [GO:0045569]; transcription factor binding [GO:0008134]FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. {ECO:0000269|PubMed:9430227}.Q68CR1SE1L3Protein sel-1 homolog 3[integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q15029U5S14116 kDa U5 small nuclear ribonucleoprotein componentCajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]qFUNCTION: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP.Q6ZSJ8CA122 Uncharacterized protein C1orf122O00214LEG8 Galectin-8Kplasma cell differentiation [GO:0002317]; T cell costimulation [GO:0031295]wFUNCTION: Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans. {ECO:0000269|PubMed:21288902}.Q9P2W9STX18 Syntaxin-18SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15029241}; Single-pass type IV membrane protein {ECO:0000305|PubMed:15029241}. Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.xendoplasmic reticulum membrane organization [GO:0090158]; intracellular protein transport [GO:0006886]; membrane fusion [GO:0061025]; positive regulation of ER to Golgi vesicle-mediated transport [GO:1902953]; positive regulation of organelle assembly [GO:1902117]; regulation of Golgi organization [GO:1903358]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; SNARE complex [GO:0031201]FUNCTION: Syntaxin that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15029241}.P17612KAPCA5cAMP-dependent protein kinase catalytic subunit alphaRSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium, flagellum. Note=Expressed in the midpiece region of the sperm flagellum. activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; blood coagulation [GO:0007596]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; carbohydrate metabolic process [GO:0005975]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to glucagon stimulus [GO:0071377]; cellular response to glucose stimulus [GO:0071333]; cellular response to parathyroid hormone stimulus [GO:0071374]; cytosolic calcium ion homeostasis [GO:0051480]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G2/M transition of mitotic cell cycle [GO:0000086]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; mesoderm formation [GO:0001707]; mitotic cell cycle [GO:0000278]; negative regulation of meiotic cell cycle [GO:0051447]; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:1901621]; neural tube closure [GO:0001843]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of cell proliferation [GO:0008284]; positive regulation of protein export from nucleus [GO:0046827]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of cardiac muscle contraction [GO:0055117]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cellular respiration [GO:0043457]; regulation of heart rate [GO:0002027]; regulation of insulin secretion [GO:0050796]; regulation of osteoblast differentiation [GO:0045667]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein binding [GO:0043393]; regulation of protein processing [GO:0070613]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; regulation of synaptic transmission, glutamatergic [GO:0051966]; renal water homeostasis [GO:0003091]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sperm capacitation [GO:0048240]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; transmembrane transport [GO:0055085]; triglyceride catabolic process [GO:0019433]; water transport [GO:0006833]ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; ubiquitin protein ligase binding [GO:0031625]2AMP-activated protein kinase complex [GO:0031588]; calcium channel complex [GO:0034704]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sperm midpiece [GO:0097225] FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation< of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. {ECO:0000269|PubMed:15642694, ECO:0000269|PubMed:15905176, ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:17333334, ECO:0000269|PubMed:17565987, ECO:0000269|PubMed:17693412, ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:19949837, ECO:0000269|PubMed:20356841, ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:21514275, ECO:0000269|PubMed:21812984}.B2RUZ4SMIM1!Small integral membrane protein 1@FUNCTION: Regulator of red blood cells formation. {ECO:0000250}.Q92575UBXN4UBX domain-containing protein 4-SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16968747}; Peripheral membrane protein {ECO:0000269|PubMed:16968747}. Nucleus envelope {ECO:0000269|PubMed:16968747}. Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER.sER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; response to unfolded protein [GO:0006986]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]FUNCTION: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD (PubMed:19822669). {ECO:0000269|PubMed:16968747, ECO:0000269|PubMed:19822669}.P42696RBM34RNA-binding protein 34Q92620PRP169Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]JFUNCTION: Probable ATP-binding RNA helicase involved in pre-mRNA splicing.O95639CPSF49Cleavage and polyadenylation specificity factor subunit 4modification by virus of host mRNA processing [GO:0046778]; modulation by virus of host morphology or physiology [GO:0019048]; modulation by virus of host process [GO:0019054]; mRNA processing [GO:0006397]; viral life cycle [GO:0019058]FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U). {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:9224719}.Q7Z6J0SH3R1"E3 ubiquitin-protein ligase SH3RF1SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, lamellipodium. Cytoplasm. Golgi apparatus, trans-Golgi network. Note=Colocalizes, with AKT2, in lamellipodia (By similarity). Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250}.5negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; protein ubiquitination [GO:0016567]; regulation of JNK cascade [GO:0046328]|cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]'FUNCTION: Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. {ECO:0000250}.; FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis.; FUNCTION: Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity.O15243OBRG$Leptin receptor gene-related proteinSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}.negative regulation of growth hormone receptor signaling pathway [GO:0060400]; negative regulation of JAK-STAT cascade [GO:0046426]; negative regulation of protein localization to cell surface [GO:2000009]; positive regulation of protein targeting to mitochondrion [GO:1903955]endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]`FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:18042720, ECO:0000269|PubMed:19907080}.Q9NQ11AT132(Probable cation-transporting ATPase 13A2SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Lysosome {ECO:0000269|PubMed:21542062, ECO:0000269|PubMed:22186024}.Ncation transport [GO:0006812]; cellular response to manganese ion [GO:0071287]integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; vesicle membrane [GO:0012506]FUNCTION: May play a role in intracellular cation homeostasis and the maintenance of neuronal integrity. {ECO:0000269|PubMed:22186024}.Q9UDY8MALT1BMucosa-associated lymphoid tissue lymphoma translocation protein 1TCR/BCRSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16123224}. Nucleus {ECO:0000269|PubMed:16123224}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10.xactivation of NF-kappaB-inducing kinase activity [GO:0007250]; B-1 B cell differentiation [GO:0001923]; defense response [GO:0006952]; Fc-epsilon receptor signaling pathway [GO:00< 38095]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; nuclear export [GO:0051168]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell cytokine production [GO:0002726]; protein oligomerization [GO:0051259]; protein ubiquitination [GO:0016567]; proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]; regulation of T cell receptor signaling pathway [GO:0050856]; response to fungus [GO:0009620]; response to molecule of bacterial origin [GO:0002237]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233]; protein self-association [GO:0043621]; signal transducer activity [GO:0004871]; ubiquitin-protein transferase activity [GO:0004842]CBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity. MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion. {ECO:0000269|PubMed:11262391, ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:18264101}.Q86VV4RNB3LRan-binding protein 3-like$intracellular transport [GO:0046907]Q9UK53ING1Inhibitor of growth protein 1cell cycle [GO:0007049]; chromatin modification [GO:0016568]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; regulation of cell death [GO:0010941]Fmethylated histone binding [GO:0035064]; zinc ion binding [GO:0008270]FUNCTION: Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene. {ECO:0000269|PubMed:9440695}.Q13185CBX3Chromobox protein homolog 3SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Associates with euchromatin and is largely excluded from constitutive heterochromatin. May be associated with microtubules and mitotic poles during mitosis (Potential). {ECO:0000305}.chromatin remodeling [GO:0006338]; negative regulation of transcription, DNA-templated [GO:0045892]; rhythmic process [GO:0048511]; transcription, DNA-templated [GO:0006351]enzyme binding [GO:0019899]; histone methyltransferase binding [GO:1990226]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]chromatin [GO:0000785]; chromocenter [GO:0010369]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; nuclear envelope [GO:0005635]; nuclear euchromatin [GO:0005719]; nuclear heterochromatin [GO:0005720]; nuclear inner membrane [GO:0005637]; nuclear pericentric heterochromatin [GO:0031618]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the mehtyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1.Q9NZL9MAT2B-Methionine adenosyltransferase 2 subunit betamethylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; regulation of catalytic activity [GO:0050790]; S-adenosylmethionine biosynthetic process [GO:0006556]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805][enzyme binding [GO:0019899]; methionine adenosyltransferase regulator activity [GO:0048270]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; methionine adenosyltransferase complex [GO:0048269]; mitochondrion [GO:0005739]; nucleus [GO:0005634]yFUNCTION: Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S-adenosylmethionine inhibition. {ECO:0000269|PubMed:10644686}.O75153CLU&Clustered mitochondria protein homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013}. Cytoplasmic granule {ECO:0000269|PubMed:25349259}. Note=A fraction colocalizes with tyrosinated tubulin and can be detected close to mitochondria. {ECO:0000269|PubMed:25349259}.`intracellular distribution of mitochondria [GO:0048312]; mitochondrion organization [GO:0007005]mRNA binding [GO:0003729]nFUNCTION: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. Specifically binds mRNAs of nuclear-encoded mitochondrial proteins in the cytoplasm and regulates transport or translation of these transcripts close to mitochondria, playing a role in mitochondrial biogenesis. {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:25349259}.Q66PJ3AR6P4<ADP-ribosylation factor-like protein 6-interacting protein 4vSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19582790}. Nucleus speckle {ECO:0000269|PubMed:19582790}.Hnuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. In case of infection by Herpes simplex virus (HSVI), may act as a splicing inhibitor of HSVI pre-mRNA. {ECO:0000269|PubMed:19582790}.O43427FIBP=Acidic fibroblast growth factor intracellular-binding proteinSUBCELLULAR LOCATION: Nucleus. Endomembrane system; Peripheral membrane protein. Note=Also associated with cytoplasmic membranes, particularly of mitochondria.cfibroblast growth factor receptor signaling pathway [GO:0008543]; platelet aggregation [GO:0070527]-fibroblast growth factor binding [GO:0017134]endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]8FUNCTION: May be involved in mitogenic function of FGF1.Q96A00PP14A,Protein phosphatase 1 regulatory subunit 14Abregulation of phosphorylation [GO:0042325]; small GTPase mediated signal transduction [GO:0007264]FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.Q7L3B6CD37LHsp90 co-chaperone Cdc37-like 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11413142}.@protein folding [GO:0006457]; protein stabilization [GO:0050821]nchaperone binding [GO:0051087]; heat shock protein binding [GO:0031072]; unfolded protein binding [GO:0051082]zFUNCTION: Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90. {ECO:0000250}.Q9BSQ5CCM2 Malcaverninblood vessel endothelial cell differentiation [GO:0060837]; cell-cell junction organization [GO:0045216]; endothelial cell development [GO:0001885]; endothelial tube morphogenesis [GO:0061154]; inner < ear development [GO:0048839]; integrin-mediated signaling pathway [GO:0007229]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; pericardium development [GO:0060039]; stress-activated MAPK cascade [GO:0051403]; vasculogenesis [GO:0001570]; venous blood vessel morphogenesis [GO:0048845]4cytoplasm [GO:0005737]; protein complex [GO:0043234]FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity). {ECO:0000250}.Q9NVX2NLE1Notchless protein homolog 1ZSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|Ref.5}.hematopoietic stem cell homeostasis [GO:0061484]; inner cell mass cell differentiation [GO:0001826]; kidney development [GO:0001822]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268]; negative regulation of mitotic cell cycle [GO:0045930]; Notch signaling pathway [GO:0007219]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; ribosomal large subunit biogenesis [GO:0042273]; skeletal system morphogenesis [GO:0048705]; somitogenesis [GO:0001756]FUNCTION: Plays a role in regulating Notch activity. Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival (By similarity). {ECO:0000250}.Q13123RED Protein Red>cell-cell signaling [GO:0007267]; immune response [GO:0006955]Rextracellular space [GO:0005615]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] FUNCTION: May bind to chromatin.Q9NSB8HOME2Homer protein homolog 2?SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Note=Postsynaptic density of neuronal cells. The stabilization and clustering of the metabotropic glutamate receptors appears to be mediated by isoform 1 and isoform 2 at the cell surface.ybehavioral response to cocaine [GO:0048148]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; chemical homeostasis within a tissue [GO:0048875]; G-protein coupled glutamate receptor signaling pathway [GO:0007216]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; regulation of store-operated calcium entry [GO:2001256]9G-protein coupled glutamate receptor binding [GO:0035256]Bapical part of cell [GO:0045177]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; neuronal postsynaptic density [GO:0097481]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.Q96K17BT3L4#Transcription factor BTF3 homolog 4P52569CTR2!Cationic amino acid transporter 2{SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9174363}; Multi-pass membrane protein {ECO:0000269|PubMed:9174363}.amino acid transport [GO:0006865]; cellular amino acid metabolic process [GO:0006520]; ion transport [GO:0006811]; L-arginine import across plasma membrane [GO:0097638]; L-lysine import across plasma membrane [GO:0097639]; L-lysine transmembrane transport [GO:1903401]; L-ornithine import across plasma membrane [GO:0097640]; L-ornithine transmembrane transport [GO:1903352]; macrophage activation [GO:0042116]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide production involved in inflammatory response [GO:0002537]; regulation of inflammatory response [GO:0050727]; regulation of macrophage activation [GO:0043030]; transmembrane transport [GO:0055085]; transport [GO:0006810]5antiporter activity [GO:0015297]; arginine transmembrane transporter activity [GO:0015181]; basic amino acid transmembrane transporter activity [GO:0015174]; high-affinity arginine transmembrane transporter activity [GO:0005289]; high-affinity L-ornithine transmembrane transporter activity [GO:0097627]; high-affinity lysine transmembrane transporter activity [GO:0005292]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]; low-affinity L-arginine transmembrane transporter activity [GO:0097626]FUNCTION: Functions as permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine); the affinity for its substrates differs between isoforms created by alternative splicing. Isoform 1 functions as permease that mediates the transport of the cationic amino acids (arginine, lysine and ornithine), and it has much higher affinity for arginine than isoform 2. Isoform 2 functions as low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) (PubMed:9174363). May play a role in classical or alternative activation of macrophages via its role in arginine transport. {ECO:0000250|UniProtKB:P18581, ECO:0000269|PubMed:9174363}.Q9HAF1EAF6,Chromatin modification-related protein MEAF6GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18794358}.Ochromatin organization [GO:0006325]; histone H2A acetylation [GO:0043968]; histone H3-K14 acetylation [GO:0044154]; histone H4-K12 acetylation [GO:0043983]; histone H4-K5 acetylation [GO:0043981]; histone H4-K8 acetylation [GO:0043982]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]centrosome [GO:0005813]; cytoplasm [GO:0005737]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.Q9GZN8CT027UPF0687 protein C20orf27P17050NAGABAlpha-N-acetylgalactosaminidasecarbohydrate catabolic process [GO:0016052]; glycolipid catabolic process [GO:0019377]; glycoside catabolic process [GO:0016139]; glycosylceramide catabolic process [GO:0046477]; oligosaccharide metabolic process [GO:0009311]alpha-galactosidase activity [GO:0004557]; alpha-N-acetylgalactosaminidase activity [GO:0008456]; protein homodimerization activity [GO:0042803]FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids. {ECO:0000269|PubMed:9741689}.Q9NVC3S38A78Putative sodium-coupled neutral amino acid transporter 7SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=In neurons, located in soma and axons. {ECO:0000250}.eamino acid transmembrane transport [GO:0003333]; asparagine transport [GO:0006867]; aspartate transport [GO:0015810]< ; glutamine transport [GO:0006868]; histidine transport [GO:0015817]; L-alanine transport [GO:0015808]; L-glutamate transport [GO:0015813]; L-serine transport [GO:0015825]; methionine transport [GO:0015821]; sodium ion transport [GO:0006814]\L-alanine transmembrane transporter activity [GO:0015180]; L-amino acid transmembrane transporter activity [GO:0015179]; L-asparagine transmembrane transporter activity [GO:0015182]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]; L-glutamine transmembrane transporter activity [GO:0015186]; L-histidine transmembrane transporter activity [GO:0005290]; L-leucine transmembrane transporter activity [GO:0015190]; L-methionine transmembrane transporter activity [GO:0015191]; L-serine transmembrane transporter activity [GO:0015194]_axon [GO:0030424]; integral component of membrane [GO:0016021]; neuronal cell body [GO:0043025]hFUNCTION: Mediates sodium-dependent transport of amino acids, preferentially L-glutamine. {ECO:0000250}.O14494LPP1"Lipid phosphate phosphohydrolase 1candrogen receptor signaling pathway [GO:0030521]; germ cell migration [GO:0008354]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lipid metabolic process [GO:0006629]; negative regulation of cell proliferation [GO:0008285]; phospholipid dephosphorylation [GO:0046839]; protein dephosphorylation [GO:0006470]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]; regulation of lipid metabolic process [GO:0019216]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]/phosphatidate phosphatase activity [GO:0008195]FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma. {ECO:0000269|PubMed:12909631}.Q8IVL5P3H2Prolyl 3-hydroxylase 2SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:15063763}. Golgi apparatus {ECO:0000269|PubMed:15063763}.collagen metabolic process [GO:0032963]; extracellular matrix organization [GO:0030198]; negative regulation of cell proliferation [GO:0008285]; peptidyl-proline hydroxylation [GO:0019511]basement membrane [GO:0005604]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; Golgi apparatus [GO:0005794]FUNCTION: Shows prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types II, IV and V. {ECO:0000250}.Q9H579MROH8 Protein MROH8Q9Y3P4RHBD3$Rhomboid domain-containing protein 3Pliver development [GO:0001889]; MAPK cascade [GO:0000165]; negative regulation of natural killer cell activation [GO:0032815]; positive regulation of protein catabolic process [GO:0045732]; regulation of acute inflammatory response [GO:0002673]; regulation of protein secretion [GO:0050708]; response to xenobiotic stimulus [GO:0009410]Gintegral component of membrane [GO:0016021]; intracellular [GO:0005622]Q969T9WBP2WW domain-binding protein 2;cellular response to estrogen stimulus [GO:0071391]; establishment of protein localization [GO:0045184]; positive regulation of gene expression, epigenetic [GO:0045815]; positive regulation of histone H3-K14 acetylation [GO:0071442]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]chromatin DNA binding [GO:0031490]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II transcription coactivator activity [GO:0001105]Q9NV56MRGBPMRG/MORF4L-binding proteinchromatin modification [GO:0016568]; chromatin organization [GO:0006325]; regulation of growth [GO:0040008]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]eH4/H2A histone acetyltransferase complex [GO:0043189]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage.Q70CQ3UBP30(Ubiquitin carboxyl-terminal hydrolase 30nSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18287522, ECO:0000269|PubMed:24896179}.emitochondrial fusion [GO:0008053]; mitochondrion degradation [GO:0000422]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K11-linked deubiquitination [GO:0035871]; protein K6-linked deubiquitination [GO:0044313]; regulation of proteasomal protein catabolic process [GO:0061136]vFUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PARK2): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:18287522, PubMed:24896179, PubMed:25527291, PubMed:25621951). Preferentially cleaves 'Lys-6'- and 'Lys-11'-linked polyubiquitin chains, 2 types of linkage that participate to mitophagic signaling (PubMed:25621951). Does not cleave efficiently polyubiquitin phosphorylated at 'Ser-65' (PubMed:25527291). Acts as negative regulator of mitochondrial fusion by mediating deubiquitination of MFN1 and MFN2 (By similarity). {ECO:0000250|UniProtKB:Q3UN04, ECO:0000269|PubMed:18287522, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951}.Q9H4L5OSBL3+Oxysterol-binding protein-related protein 3cytosol [GO:0005829]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]O75420PERQ19PERQ amino acid-rich with GYF domain-containing protein 1Binsulin-like growth factor receptor signaling pathway [GO:0048009]FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling. May increase IGF1 receptor phosphorylation under IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By similarity). {ECO:0000250}.O00746NDKM,Nucleoside diphosphate kinase, mitochondrialuSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:18635542}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086). {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086}.DCTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; lipid transport [GO:0006869]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleoside metabolic process [GO:0009116]; nucleoside triphosphate biosynthetic process [GO:0009142]; purine nucleotide metabolic p< rocess [GO:0006163]; pyrimidine nucleotide metabolic process [GO:0006220]; regulation of apoptotic process [GO:0042981]; small molecule metabolic process [GO:0044281]; UTP biosynthetic process [GO:0006228]ATP binding [GO:0005524]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]cytosol [GO:0005829]; intracellular [GO:0005622]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis (PubMed:10799505). Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity (PubMed:18635542, PubMed:23150663). Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration (PubMed:18635542). Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria (PubMed:24970086). In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (PubMed:18635542, PubMed:17028143, PubMed:23150663). {ECO:0000269|PubMed:10799505, ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663, ECO:0000305, ECO:0000305|PubMed:24970086}.Q8TDY2RBCC1#RB1-inducible coiled-coil protein 1RSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Preautophagosomal structure membrane; Peripheral membrane protein. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000250}.autophagosome assembly [GO:0000045]; cell cycle [GO:0007049]; heart development [GO:0007507]; JNK cascade [GO:0007254]; liver development [GO:0001889]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; positive regulation of cell size [GO:0045793]; positive regulation of protein phosphorylation [GO:0001934]; regulation of autophagy [GO:0010506]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]ATG1/UKL1 kinase complex [GO:1990316]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; pre-autophagosomal structure membrane [GO:0034045]FUNCTION: Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111. Involved in autophagy. Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1. Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) duting S.typhimurium infection and subsequent xenophagy. Autophagy positively regulates repair of DNA damage induced by ionizing radiation and negatively regulates apoptosis. Plays an indispensible role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity). Implicated in the regulation of RB1 expression. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway and a mediator that plays a crucial role in muscular differentiation. Expression is, thus, a prerequisite for myogenic differentiation. Inhibits PTK2/FAK1 and PTK2B/PYK2 activity and activation of downstream signaling pathways. {ECO:0000250, ECO:0000269|PubMed:10769033, ECO:0000269|PubMed:12095676, ECO:0000269|PubMed:12163359, ECO:0000269|PubMed:12221124, ECO:0000269|PubMed:14533007, ECO:0000269|PubMed:21775823, ECO:0000269|PubMed:23262492}.Q96G01BICD1Protein bicaudal D homolog 1anatomical structure morphogenesis [GO:0009653]; intracellular mRNA localization [GO:0008298]; microtubule anchoring at microtubule organizing center [GO:0072393]; minus-end-directed organelle transport along microtubule [GO:0072385]; negative regulation of phospholipase C-activating G-protein coupled receptor signaling pathway [GO:1900737]; negative regulation of phospholipase C activity [GO:1900275]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein localization to organelle [GO:0033365]; regulation of proteinase activated receptor activity [GO:1900276]; RNA processing [GO:0006396]; stress granule assembly [GO:0034063]; viral process [GO:0016032]cytoskeletal adaptor activity [GO:0008093]; dynactin binding [GO:0034452]; dynein binding [GO:0045502]; proteinase activated receptor binding [GO:0031871]; Rab GTPase binding [GO:0017137]; structural constituent of cytoskeleton [GO:0005200] cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; host cell viral assembly compartment [GO:0072517]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; trans-Golgi network [GO:0005802]FUNCTION: Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.P35520CBSCystathionine beta-synthaseeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17087506}. Nucleus {ECO:0000269|PubMed:17087506}.cellular nitrogen compound metabolic process [GO:0034641]; cysteine biosynthetic process [GO:0019344]; cysteine biosynthetic process from serine [GO:0006535]; cysteine biosynthetic process via cystathionine [GO:0019343]; DNA protection [GO:0042262]; homocysteine catabolic process [GO:0043418]; homocysteine metabolic process [GO:0050667]; hydrogen sulfide biosynthetic process [GO:0070814]; L-cysteine catabolic process [GO:0019448]; L-serine catabolic process [GO:0006565]; L-serine metabolic process [GO:0006563]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]; transsulfuration [GO:0019346].carbon monoxide binding [GO:0070025]; cystathionine beta-synthase activity [GO:0004122]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; modified amino acid binding [GO:0072341]; nitric oxide binding [GO:0070026]; nitrite reductase (NO-forming) activity [GO:0050421]; oxygen binding [GO:0019825]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; S-adenosyl-L-methionine binding [GO:1904047]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity). {ECO:0000250}.P60484PTENdPhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body. Note=Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies. XIAP/BIRC4 promotes its nuclear localization.; SUBCELLULAR LOCATION: Isoform alpha: Secreted {ECO:0000269|PubMed:23744781, < ECO:0000269|PubMed:24768297}. Note=May be secreted via a classical signal peptide and reenter into cells with the help of a poly-Arg motif.]activation of APC-Cdc20 complex activity [GO:0007092]; adult behavior [GO:0030534]; aging [GO:0007568]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; brain morphogenesis [GO:0048854]; canonical Wnt signaling pathway [GO:0060070]; cardiac muscle tissue development [GO:0048738]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cellular response to hypoxia [GO:0071456]; central nervous system development [GO:0007417]; central nervous system myelin maintenance [GO:0032286]; central nervous system neuron axonogenesis [GO:0021955]; dendritic spine morphogenesis [GO:0060997]; dentate gyrus development [GO:0021542]; endothelial cell migration [GO:0043542]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; forebrain morphogenesis [GO:0048853]; gene expression [GO:0010467]; heart development [GO:0007507]; innate immune response [GO:0045087]; inositol phosphate dephosphorylation [GO:0046855]; inositol phosphate metabolic process [GO:0043647]; learning or memory [GO:0007611]; locomotor rhythm [GO:0045475]; locomotory behavior [GO:0007626]; long term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; male mating behavior [GO:0060179]; maternal behavior [GO:0042711]; memory [GO:0007613]; multicellular organismal response to stress [GO:0033555]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell aging [GO:0090344]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cell size [GO:0045792]; negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031658]; negative regulation of dendritic spine morphogenesis [GO:0061002]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of excitatory postsynaptic membrane potential [GO:0090394]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of myelination [GO:0031642]; negative regulation of organ growth [GO:0046621]; negative regulation of phagocytosis [GO:0050765]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of ribosome biogenesis [GO:0090071]; negative regulation of synaptic vesicle clustering [GO:2000808]; neuron-neuron synaptic transmission [GO:0007270]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-tyrosine dephosphorylation [GO:0035335]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipid metabolic process [GO:0006644]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of excitatory postsynaptic membrane potential [GO:2000463]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; postsynaptic density assembly [GO:0097107]; prepulse inhibition [GO:0060134]; presynaptic membrane assembly [GO:0097105]; prostate gland growth [GO:0060736]; protein dephosphorylation [GO:0006470]; protein kinase B signaling [GO:0043491]; protein stabilization [GO:0050821]; regulation of axon regeneration [GO:0048679]; regulation of B cell apoptotic process [GO:0002902]; regulation of cellular component size [GO:0032535]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of myeloid cell apoptotic process [GO:0033032]; regulation of neuron projection development [GO:0010975]; regulation of protein stability [GO:0031647]; regulation of synaptic transmission, GABAergic [GO:0032228]; response to arsenic-containing substance [GO:0046685]; response to ATP [GO:0033198]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to nutrient [GO:0007584]; response to zinc ion [GO:0010043]; rhythmic synaptic transmission [GO:0060024]; small molecule metabolic process [GO:0044281]; social behavior [GO:0035176]; synapse assembly [GO:0007416]; synapse maturation [GO:0060074]; T cell receptor signaling pathway [GO:0050852]; transcription initiation from RNA polymerase II promoter [GO:0006367]anaphase-promoting complex binding [GO:0010997]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [GO:0051717]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; PDZ domain binding [GO:0030165]; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [GO:0016314]; phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity [GO:0051800]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]apical plasma membrane [GO:0016324]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; myelin sheath adaxonal region [GO:0035749]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic membrane [GO:0045211]; Schmidt-Lanterman incisure [GO:0043220]RFUNCTION: Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.; FUNCTION: Isoform alpha: Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1.< O15381NVL'Nuclear valosin-containing protein-likecSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:9286697}.:ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q96PU5NED4L&E3 ubiquitin-protein ligase NEDD4-likeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:18819914}. Note=May be recruited to exosomes by NDFIP1. cellular sodium ion homeostasis [GO:0006883]; excretion [GO:0007588]; gene expression [GO:0010467]; ion transmembrane transport [GO:0034220]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of sodium ion transmembrane transport [GO:1902306]; negative regulation of sodium ion transmembrane transporter activity [GO:2000650]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of cation channel activity [GO:2001259]; positive regulation of caveolin-mediated endocytosis [GO:2001288]; positive regulation of dendrite extension [GO:1903861]; positive regulation of endocytosis [GO:0045807]; positive regulation of sodium ion transport [GO:0010765]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of ion transmembrane transport [GO:0034765]; regulation of membrane depolarization [GO:0003254]; regulation of membrane potential [GO:0042391]; regulation of membrane repolarization [GO:0060306]; regulation of potassium ion transmembrane transporter activity [GO:1901016]; regulation of protein catabolic process [GO:0042176]; response to metal ion [GO:0010038]; response to salt stress [GO:0009651]; sodium ion transport [GO:0006814]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; transmembrane transport [GO:0055085]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; ventricular cardiac muscle cell action potential [GO:0086005]; viral life cycle [GO:0019058]; viral process [GO:0016032]; water homeostasis [GO:0030104]iion channel binding [GO:0044325]; ligase activity [GO:0016874]; potassium channel inhibitor activity [GO:0019870]; potassium channel regulator activity [GO:0015459]; sodium channel inhibitor activity [GO:0019871]; sodium channel regulator activity [GO:0017080]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]WFUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). {ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15217910, ECO:0000269|PubMed:15489223, ECO:0000269|PubMed:15496141, ECO:0000269|PubMed:15576372, ECO:0000269|PubMed:19144635, ECO:0000269|PubMed:25631046}.Q8WUH1CHURProtein Churchillmulticellular organismal development [GO:0007275]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]FUNCTION: Transcriptional activator that mediates FGF signaling during neural development. Plays a role in the regulation of cell movement (By similarity). Does not bind DNA by itself. {ECO:0000250}.P27482CALL3Calmodulin-like protein 3[FUNCTION: May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates. {ECO:0000269|PubMed:11278607, ECO:0000269|PubMed:18295593}.Q9C0B0UNK#RING finger protein unkempt homolog;negative regulation of cytoplasmic translation [GO:2000766]^mRNA CDS binding [GO:1990715]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]Q9UPP5K1107 Uncharacterized protein KIAA1107O60784TOM1Target of Myb protein 1qSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.endocytosis [GO:0006897]; endosomal transport [GO:0016197]; intracellular protein transport [GO:0006886]; protein transport [GO:0015031]clathrin binding [GO:0030276]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; membrane [GO:0016020]\FUNCTION: May be involved in intracellular trafficking. Probable association with membranes.Q6GQQ9OTU7B OTU domain-containing protein 7BuSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner.mucosal immune response [GO:0002385]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; protein deubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0071947]; protein K11-linked deubiquitination [GO:0035871]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; regulation of inflammatory response [GO:0050727]; regulation of innate immune response [GO:0045088]cysteine-type peptidase activity [GO:0008234]; DNA binding [GO:0003677]; K63-linked polyubiquitin binding [GO:0070530]; Lys48-specific deubiquitinase activity [GO:1990380]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Mediates deubiquitination of EGFR. Has deubiquitinating activity toward 'Lys-11', 'Lys-48' or 'Lys-63'-linked polyubiquitin chains. In vitro, has preference for 'Lys-11'-linked polyubiquitin chains; however such data are unsure in vivo. Hydrolyzes both linear and branched forms of polyubiquitin. {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:18178551, ECO:0000269|PubMed:20622874, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681}.O00635TRI38&Tripartite motif-containing protein 38cytokine-mediated signaling pathway [GO:0019221]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of defense response to virus [GO:0050687]; positive regulation of I-kappaB kinase/NF-kappaB signa< ling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of viral entry into host cell [GO:0046598]; positive regulation of viral genome replication [GO:0045070]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; regulation of interferon-beta production [GO:0032648]dligase activity [GO:0016874]; signal transducer activity [GO:0004871]; zinc ion binding [GO:0008270]FUNCTION: E3 ubiquitin-protein ligase. Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling. {ECO:0000269|PubMed:23056470}.Q8IWS0PHF6PHD finger protein 6SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}. Note=Nuclear, it particularly localizes to the nucleolus.XDNA binding [GO:0003677]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; phosphoprotein binding [GO:0051219]; poly(A) RNA binding [GO:0044822]; ribonucleoprotein complex binding [GO:0043021]; scaffold protein binding [GO:0097110]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270]ucondensed chromosome kinetochore [GO:0000777]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269|PubMed:23229552}.P26599PTBP1&Polypyrimidine tract-binding protein 1 alternative mRNA splicing, via spliceosome [GO:0000380]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of RNA splicing [GO:0033119]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; poly-pyrimidine tract binding [GO:0008187]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723]kextracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:16179478, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:21518792}.Q9Y343SNX24Sorting nexin-24phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314])cytoplasmic vesicle membrane [GO:0030659]P17405ASMSphingomyelin phosphodiesteraseSphingomyelinaseceramide biosynthetic process [GO:0046513]; glycosphingolipid metabolic process [GO:0006687]; negative regulation of MAP kinase activity [GO:0043407]; nervous system development [GO:0007399]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein dephosphorylation [GO:0035307]; response to cocaine [GO:0042220]; response to drug [GO:0042493]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684]; termination of signal transduction [GO:0023021]endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lamellar body [GO:0042599]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; plasma membrane [GO:0005886]FUNCTION: Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Isoform 2 and isoform 3 have lost catalytic activity.Q86WN1FCSD1$FCH and double SH3 domains protein 1O75151PHF2 Lysine-specific demethylase PHF2SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20129925}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.chromatin organization [GO:0006325]; liver development [GO:0001889]; negative regulation of chromatin silencing at rDNA [GO:0061188]; protein demethylation [GO:0006482]; transcription, DNA-templated [GO:0006351]dioxygenase activity [GO:0051213]; histone demethylase activity (H3-K9 specific) [GO:0032454]; iron ion binding [GO:0005506]; methylated histone binding [GO:0035064]; zinc ion binding [GO:0008270]condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA. {ECO:0000269|PubMed:20129925, ECO:0000269|PubMed:21167174, ECO:0000269|PubMed:21532585}.Q9NZZ3CHMP5%Charged multivesicular body protein 5SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.Zcell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; endosome to lysosome transport [GO:0008333]; lysosome organization [GO:0007040]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; multivesicular body sorting pathway [GO:0071985]; nucleus organization [GO:0006997]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; regulation of receptor recycling [GO:0001919]; viral budding [GO:0046755]; viral life cycle [GO:0019058]; viral process [GO:0016032]ncytosol [GO:0005829]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunc< tion with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14519844}.O43715TRIA1'TP53-regulated inhibitor of apoptosis 1fSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Mitochondrion. Mitochondrion intermembrane space.2cellular response to UV [GO:0034644]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; phospholipid transport [GO:0015914]; positive regulation of phospholipid transport [GO:2001140]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of membrane lipid distribution [GO:0097035]p53 binding [GO:0002039]mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]-FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis. {ECO:0000269|PubMed:15735003, ECO:0000269|PubMed:23931759}.Q16181Septin-7ySUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18460473}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18460473}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18460473}. Cleavage furrow {ECO:0000269|PubMed:18460473}. Midbody {ECO:0000269|PubMed:18460473}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Note=Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase. Associated with actin stress fibers (By similarity). {ECO:0000250}.cilium morphogenesis [GO:0060271]; cytokinesis [GO:0000910]; mitotic nuclear division [GO:0007067]; protein heterooligomerization [GO:0051291]; regulation of embryonic cell shape [GO:0016476]kGTP binding [GO:0005525]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]actin cytoskeleton [GO:0015629]; axoneme [GO:0005930]; axon terminus [GO:0043679]; cleavage furrow [GO:0032154]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; septin complex [GO:0031105]; spindle [GO:0005819]; stress fiber [GO:0001725]; synapse [GO:0045202]iFUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. {ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18460473}.P60059SC61G-Protein transport protein Sec61 subunit gammamantigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; gene expression [GO:0010467]; IRE1-mediated unfolded protein response [GO:0036498]; protein targeting to ER [GO:0045047]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]}P-P-bond-hydrolysis-driven protein transmembrane transporter activity [GO:0015450]; protein transporter activity [GO:0008565]cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]ZFUNCTION: Necessary for protein translocation in the endoplasmic reticulum. {ECO:0000250}.Q96MK2FA65CProtein FAM65CO75530EEDPolycomb protein EEDlSUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Transiently colocalizes with XIST at inactive X chromosomes."chromatin organization [GO:0006325]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of histone H3-K27 methylation [GO:0061087]; regulation of gene expression, epigenetic [GO:0040029]; regulation of gene expression by genetic imprinting [GO:0006349]; spinal cord development [GO:0021510]; transcription, DNA-templated [GO:0006351]wchromatin binding [GO:0003682]; histone methyltransferase activity [GO:0042054]; identical protein binding [GO:0042802]cytoplasm [GO:0005737]; ESC/E(Z) complex [GO:0035098]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pronucleus [GO:0045120]; sex chromatin [GO:0001739]FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:9584199}.Q5TA45INT11Integrator complex subunit 11eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15684398}. Cytoplasm {ECO:0000269|PubMed:15684398}.Yblood microparticle [GO:0072562]; cytoplasm [GO:0005737]; integrator complex [GO:0032039]FUNCTION: Catalytic component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Mediates the snRNAs 3' cleavage. {ECO:0000269|PubMed:16239144}.P62070RRAS2Ras-related protein R-Ras2osteoblast differentiation [GO:0001649]; positive regulation of cell migration [GO:0030335]; Ras protein signal transduction [GO:0007265]; regulation of neuron death [GO:1901214]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion.O14508SOCS2"Suppressor of cytokine signaling 2CytokineR/Jak/SOCS5aging [GO:0007568]; cellular response to hormone stimulus [GO:0032870]; cytokine-mediated signaling pathway [GO:0019221]; growth hormone receptor signaling pathway [GO:0060396]; JAK-STAT cascade < [GO:0007259]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of JAK-STAT cascade [GO:0046426]; negative regulation of protein kinase activity [GO:0006469]; positive regulation of signal transduction [GO:0009967]; protein ubiquitination [GO:0016567]; regulation of cell growth [GO:0001558]; regulation of signal transduction [GO:0009966]; response to estradiol [GO:0032355]growth hormone receptor binding [GO:0005131]; insulin-like growth factor receptor binding [GO:0005159]; JAK pathway signal transduction adaptor activity [GO:0008269]; protein kinase inhibitor activity [GO:0004860]; SH3/SH2 adaptor activity [GO:0005070]FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.Q9NRP2COXM2,COX assembly mitochondrial protein 2 homologBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20220131}.LFUNCTION: May be involved in cytochrome c oxidase biogenesis. {ECO:0000250}.Q9NZU5LMCD1'LIM and cysteine-rich domains protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May shuttle between the cytoplasm and the nucleus. {ECO:0000250}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of defense response to virus by host [GO:0002230]; regulation of cardiac muscle hypertrophy [GO:0010611]; transcription, DNA-templated [GO:0006351]Ncytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]FUNCTION: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6-mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. {ECO:0000250, ECO:0000269|PubMed:20026769}.P28300LYOXProtein-lysine 6-oxidase]blood vessel development [GO:0001568]; cellular protein modification process [GO:0006464]; collagen fibril organization [GO:0030199]; elastic fiber assembly [GO:0048251]; extracellular matrix organization [GO:0030198]; lung development [GO:0030324]; response to drug [GO:0042493]; response to steroid hormone [GO:0048545]; wound healing [GO:0042060]Ocopper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720]collagen trimer [GO:0005581]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression.Q6P2C8MED276Mediator of RNA polymerase II transcription subunit 27XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:9989412}.gene expression [GO:0010467]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; stem cell maintenance [GO:0019827]; transcription initiation from RNA polymerase II promoter [GO:0006367]cytoplasm [GO:0005737]; mediator complex [GO:0016592]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]; ubiquitin ligase complex [GO:0000151]CFUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:9989412}.Q8NEY1NAV1Neuron navigator 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associates with a subset of microtubule plus ends. Enriched in neuronal growth cones (By similarity). {ECO:0000250}.Hmicrotubule bundle formation [GO:0001578]; neuron migration [GO:0001764]?FUNCTION: May be involved in neuronal migration. {ECO:0000250}.Q8NI22MCFD20Multiple coagulation factor deficiency protein 2SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:12717434}. Endoplasmic reticulum {ECO:0000269|PubMed:12717434}. Golgi apparatus {ECO:0000269|PubMed:12717434}.cellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors. {ECO:0000269|PubMed:12717434}.Q8NG11TSN14Tetraspanin-14cell surface [GO:0009986]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197]O75391SPAG7Sperm-associated antigen 7P08172ACM2$Muscarinic acetylcholine receptor M2 Receptor/GPCRSUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250}."adenylate cyclase-inhibiting G-protein coupled acetylcholine receptor signaling pathway [GO:0007197]; adenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; G-protein coupled receptor signaling pathway [GO:0007186]; G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; nervous system development [GO:0007399]; phospholipase C-activating G-protein coupled acetylcholine receptor signaling pathway [GO:0007207]; regulation of heart contraction [GO:0008016]; regulation of smooth muscle contraction [GO:0006940]; response to virus [GO:0009615]; sensory perception of chemical stimulus [GO:0007606]; synaptic transmission, cholinergic [GO:0007271]Ydrug binding [GO:0008144]; G-protein coupled acetylcholine receptor activity [GO:0016907];asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; cell junction [GO:0030054]; dendrite [GO:0030425]; integral component of plasma membrane [GO:0005887]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; symmetric synapse [GO:0032280]; synapse [GO:0045202]FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to < the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol. {ECO:0000269|PubMed:24256733, ECO:0000269|PubMed:3443095}.Q14596NBR1Next to BRCA1 gene 1 protein SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, autophagosome. Lysosome. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}. Note=In cardiac muscles localizes to the sarcomeric M line (By similarity). Is targeted to lysosomes for degradation. {ECO:0000250}.macroautophagy [GO:0016236]; negative regulation of osteoblast differentiation [GO:0045668]; protein oligomerization [GO:0051259]; regulation of bone mineralization [GO:0030500]; regulation of stress-activated MAPK cascade [GO:0032872]tmitogen-activated protein kinase binding [GO:0051019]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270]autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; late endosome [GO:0005770]; lysosome [GO:0005764]; M band [GO:0031430]; membrane [GO:0016020]; pre-autophagosomal structure [GO:0000407]FUNCTION: Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets. {ECO:0000269|PubMed:19250911}.Q8NCA5FA98AProtein FAM98AQ3YEC7RABL6Rab-like protein 6SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Predominantly cytoplasmic.; SUBCELLULAR LOCATION: Isoform 3: Nucleus. Note=Predominantly nuclear.]centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]}FUNCTION: May enhance cellular proliferation. May reduce growth inhibitory activity of CDKN2A. {ECO:0000269|PubMed:16582619}.Q9Y547IFT25+Intraflagellar transport protein 25 homologheart development [GO:0007507]; left/right axis specification [GO:0070986]; lung development [GO:0030324]; organelle organization [GO:0006996]; protein transport [GO:0015031]; skeletal system development [GO:0001501]; smoothened signaling pathway [GO:0007224]centrosome [GO:0005813]; ciliary tip [GO:0097542]; extracellular exosome [GO:0070062]; intraciliary transport particle B [GO:0030992]; primary cilium [GO:0072372]FUNCTION: Component of the IFT complex B required for sonic hedgehog/SHH signaling. May mediate transport of SHH components: required for the export of SMO and PTCH1 receptors out of the cilium and the accumulation of GLI2 at the ciliary tip in response to activation of the SHH pathway, suggesting it is involved in the dynamic transport of SHH signaling molecules within the cilium. Not required for ciliary assembly (By similarity). {ECO:0000250}.O60343TBCD4TBC1 domain family member 4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18771725}. Note=Isoform 2 shows a cytoplasmic perinuclear localization in a myoblastic cell line in resting and insulin-stimulated cells.cellular response to insulin stimulus [GO:0032869]; membrane organization [GO:0061024]; negative regulation of vesicle fusion [GO:0031339]; vesicle-mediated transport [GO:0016192]ecytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]6FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A, RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose transporter SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing glucose uptake. {ECO:0000269|PubMed:15971998, ECO:0000269|PubMed:18771725, ECO:0000269|PubMed:22908308}.Q9UJ83HACL12-hydroxyacyl-CoA lyase 1cellular lipid metabolic process [GO:0044255]; fatty acid alpha-oxidation [GO:0001561]; protein oligomerization [GO:0051259]; small molecule metabolic process [GO:0044281]carbon-carbon lyase activity [GO:0016830]; cofactor binding [GO:0048037]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; receptor binding [GO:0005102]; thiamine pyrophosphate binding [GO:0030976]FUNCTION: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.P31949S10ABProtein S100-A11eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618420}. Nucleus {ECO:0000269|PubMed:18618420}.negative regulation of cell proliferation [GO:0008285]; negative regulation of DNA replication [GO:0008156]; signal transduction [GO:0007165]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; protein homodimerization activity [GO:0042803]; S100 protein binding [GO:0044548]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ruffle [GO:0001726]pFUNCTION: Facilitates the differentiation and the cornification of keratinocytes. {ECO:0000269|PubMed:18618420}.Q13315ATMSerine-protein kinase ATMSUBCELLULAR LOCATION: Nucleus. Cytoplasmic vesicle. Note=Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin.brain development [GO:0007420]; cell cycle arrest [GO:0007050]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to gamma radiation [GO:0071480]; cellular response to heat [GO:0034605]; determination of adult lifespan [GO:0008340]; DNA damage induced protein phosphorylation [GO:0006975]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; heart development [GO:0007507]; histone mRNA catabolic process [GO:0071044]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lipoprotein catabolic process [GO:0042159]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of B cell proliferation [GO:0030889]; neuron apoptotic process [GO:0051402]; oocyte development [GO:0048599]; peptidyl-serine phosphorylation [GO:0018105]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; positive regulation of neuron apoptotic process [GO:0043525]; pre-B cell allelic exclusion [GO:0002331]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; reciprocal meiotic recombination [GO:0007131]; regulation of cellular response to heat [GO:1900034]; replicative senescence [GO:0090399]; response to hypoxia [GO:0001666]; response to ionizing radiation [GO:0010212]; signal transduction [GO:0007165]; signal transduction involved in mitotic G2 DNA damage checkpoint [GO:0072434]; somitogenesis [GO:0001756]; telomere maintenance [GO:0000723]; V(D)J recombination [GO:0033151]|1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-dependent protein kinase activity [GO:0004677]; histone serine kinase activity [GO:0035174]; protein complex binding [GO:0032403]; protein dimerization activity [GO:0046983]; protein N-terminus binding [GO:0047485]; protein serine/threonine kinase activity [GO:0004674]acytoplasmic membrane-bounded vesicle [GO:0016023]; nucleoplasm [GO:0005654]; spindle [GO:0005819]4FUNCTION: Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in< signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. {ECO:0000269|PubMed:10973490, ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:19965871}.P11021GRP78 78 kDa glucose-regulated proteinSUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. Cytoplasm {ECO:0000250}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.activation of signaling protein activity involved in unfolded protein response [GO:0006987]; ATF6-mediated unfolded protein response [GO:0036500]; blood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; cellular response to antibiotic [GO:0071236]; cellular response to glucose starvation [GO:0042149]; cellular response to interleukin-4 [GO:0071353]; cerebellar Purkinje cell layer development [GO:0021680]; cerebellum structural organization [GO:0021589]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; ER overload response [GO:0006983]; IRE1-mediated unfolded protein response [GO:0036498]; maintenance of protein localization in endoplasmic reticulum [GO:0035437]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein homodimerization activity [GO:0090074]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; PERK-mediated unfolded protein response [GO:0036499]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of cell migration [GO:0030335]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress [GO:1990440]; protein folding in endoplasmic reticulum [GO:0034975]; regulation of ATF6-mediated unfolded protein response [GO:1903891]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; regulation of PERK-mediated unfolded protein response [GO:1903897]; regulation of protein folding in endoplasmic reticulum [GO:0060904]; substantia nigra development [GO:0021762]; toxin transport [GO:1901998]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; chaperone binding [GO:0051087]; enzyme binding [GO:0019899]; glycoprotein binding [GO:0001948]; misfolded protein binding [GO:0051787]; protein domain specific binding [GO:0019904]; ribosome binding [GO:0043022]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]ncell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of endoplasmic reticulum membrane [GO:0030176]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate. {ECO:0000269|PubMed:2294010, ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:23990668}.Q12788TBL3Transducin beta-like protein 3G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger [GO:0007199]; intracellular signal transduction [GO:0035556]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]opoly(A) RNA binding [GO:0044822]; receptor signaling protein activity [GO:0005057]; snoRNA binding [GO:0030515]nucleolus [GO:0005730]; nucleus [GO:0005634]; Pwp2p-containing subcomplex of 90S preribosome [GO:0034388]; small-subunit processome [GO:0032040]Q9BXB4OSB11,Oxysterol-binding protein-related protein 11fat cell differentiation [GO:0045444]; lipid transport [GO:0006869]; positive regulation of sequestering of triglyceride [GO:0010890]AGolgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]$FUNCTION: Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:23028956}.Q15417CNN3 Calponin-3actomyosin structure organization [GO:0031032]; epithelial cell differentiation [GO:0030855]; negative regulation of ATPase activity [GO:0032780]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; focal adhesion [GO:0005925]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]Q6PJF5RHDF2Inactive rhomboid protein 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22265016}.negative regulation of protein secretion [GO:0050709]; protein transport [GO:0015031]; proteolysis [GO:0006508]; regulation of epidermal growth factor receptor signaling pathway [GO:0042058]; regulation of protein secretion [GO:0050708]vendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]VFUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration (By similarity). {ECO:0000250}.Q9Y6D9MD1L10Mitotic spindle assembly checkpoint protein MAD1SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Colocalizes with NEK2 at the kinetochore.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of T cell proliferation [GO:0042130]; regulation of metaphase plate congression [GO:0090235]; small GTPase mediated signal transduction [GO:0007264]; thymus development [GO:0048538]actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle pole [GO:0000922]FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, p< ossibly by interfering with MYC binding. {ECO:0000269|PubMed:10049595, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:20133940}.Q9Y314NOSIP)Nitric oxide synthase-interacting proteinxSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates from nucleus to cytoplasm in the G2 phase of the cell cycle.negative regulation of catalytic activity [GO:0043086]; negative regulation of nitric-oxide synthase activity [GO:0051001]; nitric oxide metabolic process [GO:0046209]; regulation of nitric-oxide synthase activity [GO:0050999]; small molecule metabolic process [GO:0044281]ycytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity. {ECO:0000269|PubMed:11149895, ECO:0000269|PubMed:15548660, ECO:0000269|PubMed:16135813}.Q96KM6Z512BZinc finger protein 512BQ96RL1UIMC1BRCA1-A complex subunit RAP80SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610, ECO:0000269|PubMed:17643121}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).Ndouble-strand break repair [GO:0006302]; G2 DNA damage checkpoint [GO:0031572]; histone H2A K63-linked deubiquitination [GO:0070537]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of DNA repair [GO:0045739]; response to ionizing radiation [GO:0010212]; transcription, DNA-templated [GO:0006351]Khistone binding [GO:0042393]; K63-linked polyubiquitin binding [GO:0070530]2BRCA1-A complex [GO:0070531]; nucleus [GO:0005634]UFUNCTION: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1. {ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19261748}.Q00577PURA+Transcriptional activator protein Pur-alphacell differentiation [GO:0030154]; DNA replication initiation [GO:0006270]; DNA unwinding involved in DNA replication [GO:0006268]; negative regulation of transcription, DNA-templated [GO:0045892]; nervous system development [GO:0007399]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]double-stranded telomeric DNA binding [GO:0003691]; poly(A) RNA binding [GO:0044822]; purine-rich negative regulatory element binding [GO:0032422]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; single-stranded DNA binding [GO:0003697]; transcription factor binding [GO:0008134]; translation repressor activity, nucleic acid binding [GO:0000900]cytoplasm [GO:0005737]; dendrite [GO:0030425]; DNA replication factor A complex [GO:0005662]; neuronal cell body [GO:0043025]; nuclear chromosome, telomeric region [GO:0000784]; nucleus [GO:0005634]FUNCTION: This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the MYC gene. May play a role in the initiation of DNA replication and in recombination.Q14331FRG1 Protein FRG1SUBCELLULAR LOCATION: Nucleus, Cajal body. Nucleus, nucleolus. Cytoplasm. Cytoplasm, myofibril, sarcomere, Z line. Note=Localization changes during myogenesis from mainly cytoplasmic in undifferentiated myoblasts, to strongly nucleolar in early myotubes and back to cytoplasmic 5 days post-differentiation. Localized at the Z-line in the sarcomere of matured myotubes 8 days post-differentiation.pmRNA splicing, via spliceosome [GO:0000398]; muscle organ development [GO:0007517]; rRNA processing [GO:0006364]oCajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; nucleolus [GO:0005730]; Z disc [GO:0030018]FUNCTION: Binds to mRNA in a sequence-independent manner. May play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. May be involved in mRNA transport. May be involved in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase SUV420H1. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15060122, ECO:0000269|PubMed:20970242, ECO:0000269|PubMed:21699900, ECO:0000269|PubMed:23720823}.O60291MGRN1!E3 ubiquitin-protein ligase MGRN1SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19737927}. Note=The endosomal localization is dependent on the interaction with TSG101.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytosol. Nucleus. Note=Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Excluded from nucleoli.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol. Cell membrane.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm, cytosol. Cell membrane.endosome to lysosome transport [GO:0008333]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of G-protein coupled receptor protein signaling pathway [GO:0045744]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. {ECO:0000269|PubMed:17229889, ECO:0000269|PubMed:19703557, ECO:0000269|PubMed:19737927}.P20742PZPPregnancy zone proteinYfemale pregnancy [GO:0007565]; negative regulation of endopeptidase activity [GO:0010951]sFUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.Q8NBA8DTWD2DTW domain-containing protein 2P32780TF2H1*General transcription factor IIH subunit 1q7-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-e< xcision repair, DNA damage removal [GO:0000718]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]Zcore TFIIH complex [GO:0000439]; holo TFIIH complex [GO:0005675]; nucleoplasm [GO:0005654]FUNCTION: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.P52655TF2AA-Transcription initiation factor IIA subunit 1DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; TBP-class protein binding [GO:0017025]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]acytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; transcription factor TFIIA complex [GO:0005672]FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity. {ECO:0000269|PubMed:11030333, ECO:0000269|PubMed:16537915}.Q8WUH6TM263Transmembrane protein 263P17900SAP3Ganglioside GM2 activator)other lysosomal enzymes and activators(5)ganglioside catabolic process [GO:0006689]; glycosphingolipid metabolic process [GO:0006687]; learning or memory [GO:0007611]; lipid storage [GO:0019915]; neuromuscular process controlling balance [GO:0050885]; oligosaccharide catabolic process [GO:0009313]; positive regulation of hydrolase activity [GO:0051345]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]beta-N-acetylgalactosaminidase activity [GO:0032428]; lipid transporter activity [GO:0005319]; phospholipase activator activity [GO:0016004]apical cortex [GO:0045179]; cytoplasmic side of plasma membrane [GO:0009898]; extracellular exosome [GO:0070062]; hydrogen:potassium-exchanging ATPase complex [GO:0005889]; lysosomal lumen [GO:0043202]; mitochondrion [GO:0005739]FUNCTION: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. {ECO:0000250}.P55854SUMO3"Small ubiquitin-related modifier 3JSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}.+cellular protein metabolic process [GO:0044267]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; post-translational protein modification [GO:0043687]; protein localization to nucleus [GO:0034504]; protein sumoylation [GO:0016925]&SUMO transferase activity [GO:0019789]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; kinetochore [GO:0000776]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605].FUNCTION: Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678}.Q2TAY7SMU1#WD40 repeat-containing protein SMU1P61916NPC2Epididymal secretory protein E1SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19723497}. Endoplasmic reticulum {ECO:0000269|PubMed:19723497}. Lysosome {ECO:0000269|PubMed:19723497}.cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; glycolipid transport [GO:0046836]; intracellular cholesterol transport [GO:0032367]; intracellular sterol transport [GO:0032366]; phospholipid transport [GO:0015914]; regulation of isoprenoid metabolic process [GO:0019747]; response to virus [GO:0009615]=cholesterol binding [GO:0015485]; enzyme binding [GO:0019899]FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport. {ECO:0000269|PubMed:17018531, ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:18823126}.Q86X55CARM1(Histone-arginine methyltransferase CARM1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane.(aging [GO:0007568]; cellular lipid metabolic process [GO:0044255]; chromatin organization [GO:0006325]; endochondral bone morphogenesis [GO:0060350]; histone H3-R17 methylation [GO:0034971]; histone H3-R2 methylation [GO:0034970]; histone methylation [GO:0016571]; intracellular estrogen receptor signaling pathway [GO:0030520]; negative regulation of dendrite development [GO:2000171]; negative regulation of protein binding [GO:0032091]; pathogenesis [GO:0009405]; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [GO:0019919]; positive regulation of cell proliferation [GO:0008284]; positive regulation of fat cell differentiation [GO:0045600]; regulation of growth plate cartilage chondrocyte proliferation [GO:0003420]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of mRNA binding [GO:1902415]; regulation of transcription, DNA-templated [GO:0006355]; response to cAMP [GO:0051591]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]ybeta-catenin binding [GO:0008013]; histone-arginine N-methyltransferase activity [GO:0008469]; histone methyltransferase activity [GO:0042054]; histone methyltransferase activity (H3-R17 specific) [GO:0035642]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; lysine-acetylated histone binding [GO:0070577]; protein-arginine N-methyltransferase activity [GO:0016274]; < protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein methyltransferase activity [GO:0008276]; transcription coactivator activity [GO:0003713]; transcription regulatory region DNA binding [GO:0044212]FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs. {ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:19405910}.Q969F9HPS3#Hermansky-Pudlak syndrome 3 protein>organelle organization [GO:0006996]; pigmentation [GO:0043473]ZFUNCTION: Involved in early stages of melanosome biogenesis and maturation. {ECO:0000250}.Q8IWA5CTL2"Choline transporter-like protein 2ycholine transport [GO:0015871]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid metabolic process [GO:0006644]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]`choline transmembrane transporter activity [GO:0015220]; signal transducer activity [GO:0004871]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]FUNCTION: Isoform 1, but not isoform 3, exhibits some choline transporter activity. {ECO:0000269|PubMed:10677542, ECO:0000269|PubMed:20665236}.O60930RNH1Ribonuclease H1DNA replication, removal of RNA primer [GO:0043137]; RNA catabolic process [GO:0006401]; RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]magnesium ion binding [GO:0000287]; nucleic acid binding [GO:0003676]; ribonuclease activity [GO:0004540]; RNA binding [GO:0003723]; RNA-DNA hybrid ribonuclease activity [GO:0004523]FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224). {ECO:0000269|PubMed:10497183, ECO:0000269|PubMed:21700224}.O75410TACC14Transforming acidic coiled-coil-containing protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis.0cell cycle [GO:0007049]; cell division [GO:0051301]; cell proliferation [GO:0008283]; cerebral cortex development [GO:0021987]; interkinetic nuclear migration [GO:0022027]; microtubule cytoskeleton organization [GO:0000226]; neurogenesis [GO:0022008]; regulation of microtubule-based process [GO:0032886]cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]wFUNCTION: Likely involved in the processes that promote cell division prior to the formation of differentiated tissues.Q9BRJ6CG050Uncharacterized protein C7orf50O75143ATG13Autophagy-related protein 13HSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. {ECO:0000250}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; autophagosome assembly [GO:0000045]; positive regulation of protein targeting to mitochondrion [GO:1903955]ATG1/UKL1 kinase complex [GO:1990316]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; pre-autophagosomal structure [GO:0000407]=FUNCTION: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:21855797}.P17252KPCAProtein kinase C alpha typeSUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Mitochondrion membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Nucleus. activation of adenylate cyclase activity [GO:0007190]; activation of phospholipase C activity [GO:0007202]; angiogenesis [GO:0001525]; apoptotic signaling pathway [GO:0097190]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cellular calcium ion homeostasis [GO:0006874]; cellular response to carbohydrate stimulus [GO:0071322]; chondrocyte differentiation [GO:0002062]; desmosome assembly [GO:0002159]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix organization [GO:0030198]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; histone H3-T6 phosphorylation [GO:0035408]; inactivation of MAPK activity [GO:0000188]; induction of positive chemotaxis [GO:0050930]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; negative regulation of adenylate cyclase activity [GO:0007194]; negative regulation of cell proliferation [GO:0008285]; negative regulation of glial cell apoptotic process [GO:0034351]; negative regulation of glucose import [GO:0046325]; negative regulation of insulin receptor signaling pathway [GO:0046627]; neurotrophin TRK receptor signaling pathway [GO:0048011]; neutrophil chemotaxis [GO:0030593]; peptidyl-serine autophosphorylation [GO:0036289]; phototransduction, visible light [GO:0007603]; platelet activation [GO:0030168]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of dense core granule biogenesis [GO:2000707]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation< of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of inflammatory response [GO:0050729]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of mitotic cell cycle [GO:0045931]; protein phosphorylation [GO:0006468]; regulation of insulin secretion [GO:0050796]; regulation of muscle contraction [GO:0006937]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of platelet aggregation [GO:0090330]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; regulation of the force of heart contraction [GO:0002026]; response to interleukin-1 [GO:0070555]; rhodopsin mediated signaling pathway [GO:0016056]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]JATP binding [GO:0005524]; calcium-dependent protein kinase C activity [GO:0004698]; enzyme binding [GO:0019899]; histone kinase activity (H3-T6 specific) [GO:0035403]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]; zinc ion binding [GO:0008270]apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. {ECO:0000269|PubMed:10848585, ECO:0000269|PubMed:11909826, ECO:0000269|PubMed:12724315, ECO:0000269|PubMed:12832403, ECO:0000269|PubMed:15016832, ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:18056764, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:21576361, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:9738012, ECO:0000269|PubMed:9830023, ECO:0000269|PubMed:9873035, ECO:0000269|PubMed:9927633}.Q7Z7K6CENPVCentromere protein V]SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Enriched at the nuclear periphery and around the nucleolus. In mitotic cells, localizes to kinetochores from prometaphase to metaphase. At anaphase onset, transfers to the spindle midzone and then to the mid-body in telophase and cytokinesis./ameboidal-type cell migration [GO:0001667]; cell division [GO:0051301]; centromere complex assembly [GO:0034508]; mitotic nuclear division [GO:0007067]; pericentric heterochromatin assembly [GO:0031508]; positive regulation of cytokinesis [GO:0032467]; regulation of chromosome organization [GO:0033044])carbon-sulfur lyase activity [GO:0016846]condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle midzone [GO:0051233]FUNCTION: Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis. {ECO:0000269|PubMed:18772885}.Q68D91MBLC22Metallo-beta-lactamase domain-containing protein 2Q969K3RNF34!E3 ubiquitin-protein ligase RNF34eSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15069192}; Peripheral membrane protein {ECO:0000305}. Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus {ECO:0000269|PubMed:22064484}. Nucleus speckle {ECO:0000269|PubMed:12118383}. Cytoplasm, cytosol {ECO:0000269|PubMed:15069192}.cellular response to cold [GO:0070417]; negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:2001271]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of signal transduction by p53 class mediator [GO:1901797]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:004316< 1]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of oxygen metabolic process [GO:2000374]ligase activity [GO:0016874]; p53 binding [GO:0002039]; phosphatidylinositol phosphate binding [GO:1901981]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]>FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219). {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:15897238, ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219, ECO:0000269|Ref.13, ECO:0000303|PubMed:18382127}.O95716RAB3DRas-related protein Rab-3DFintracellular protein transport [GO:0006886]; peptidyl-cysteine methylation [GO:0018125]; positive regulation of regulated secretory pathway [GO:1903307]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking involved in exocytosis [GO:0006904]UGTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin V binding [GO:0031489]endosome [GO:0005768]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]; synaptic vesicle [GO:0008021]; transport vesicle [GO:0030133]; zymogen granule [GO:0042588]fFUNCTION: Protein transport. Probably involved in regulated exocytosis (By similarity). {ECO:0000250}.Q9Y5B0CTDP19RNA polymerase II subunit A C-terminal domain phosphataseSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22692537}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22692537}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22692537}. Midbody {ECO:0000269|PubMed:22692537}. Note=Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively.Xcell division [GO:0051301]; exit from mitosis [GO:0010458]; gene expression [GO:0010467]; positive regulation of viral transcription [GO:0050434]; protein dephosphorylation [GO:0006470]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]XCTD phosphatase activity [GO:0008420]; DNA-directed RNA polymerase activity [GO:0003899]actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; spindle [GO:0005819]; spindle midzone [GO:0051233]; spindle pole [GO:0000922]FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. {ECO:0000269|PubMed:22692537}.Q8NBP0TTC13#Tetratricopeptide repeat protein 13Q9NYF8BCLF1'Bcl-2-associated transcription factor 1apoptotic process [GO:0006915]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription, initiation [GO:2000144]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of response to DNA damage stimulus [GO:2001022]; regulation of DNA-templated transcription in response to stress [GO:0043620]; transcription, DNA-templated [GO:0006351]FUNCTION: Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:18794151}.P27797CALR CalreticulinESUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasm, cytosol. Secreted, extracellular space, extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen {ECO:0000250}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes. antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; ATF6-mediated unfolded protein response [GO:0036500]; cardiac muscle cell differentiation [GO:0055007]; cell cycle arrest [GO:0007050]; cellular calcium ion homeostasis [GO:0006874]; cellular protein metabolic process [GO:0044267]; cellular response to lithium ion [GO:0071285]; cellular senescence [GO:0090398]; chaperone-mediated protein folding [GO:0061077]; cortical actin cytoskeleton organization [GO:0030866]; endoplasmic reticulum unfolded protein response [GO:0030968]; glucocorticoid receptor signaling pathway [GO:0042921]; negative regulation of intracellular steroid hormone receptor signaling pathway [GO:0033144]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of translation [GO:0017148]; peptide antigen assembly with MHC class I protein complex [GO:0002502]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell proliferation [GO:0008284]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of DNA replication [GO:0045740]; positive regulation of gene expression [GO:0010628]; positive regulation of phagocytosis [GO:0050766]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; post-translational protein modification [GO:0043687]; protein export from nucleus [GO:0006611]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; protein localization to nucleus [GO:0034504]; protein maturation by protein folding [GO:0022417]; protein N-linked glycosylation via asparagine [GO:0018279]; protein stabilization [GO:0050821]; receptor-mediated endocytosis [GO:0006898]; regulation of apoptotic process [GO:0042981]; regulation of meiotic nuclear division [GO:0040020]; regulation of transcription, DNA-templated [GO:0006355]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to testosterone [GO:0033574]; sequestering of calcium ion [GO:0051208]; spermatogenesis [GO:0007283]]androgen receptor binding [GO:0050681]; calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; chaperone binding [GO:0051087]; complement componen< t C1q binding [GO:0001849]; DNA binding [GO:0003677]; glycoprotein binding [GO:0001948]; hormone binding [GO:0042562]; integrin binding [GO:0005178]; iron ion binding [GO:0005506]; mRNA binding [GO:0003729]; peptide binding [GO:0042277]; poly(A) RNA binding [GO:0044822]; protein binding involved in protein folding [GO:0044183]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]; zinc ion binding [GO:0008270]Hacrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; intracellular [GO:0005622]; membrane [GO:0016020]; MHC class I peptide loading complex [GO:0042824]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]; proteinaceous extracellular matrix [GO:0005578]; sarcoplasmic reticulum lumen [GO:0033018]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). {ECO:0000250}.P46013KI67 Antigen KI-67PoncoSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Chromosome {ECO:0000269|PubMed:22002106}. Note=Predominantly localized in the G1 phase in the perinucleolar region, in the later phases it is also detected throughout the nuclear interior, being predominantly localized in the nuclear matrix. In mitosis, it is present on all chromosomes.cell proliferation [GO:0008283]; cellular response to heat [GO:0034605]; DNA metabolic process [GO:0006259]; hyaluronan metabolic process [GO:0030212]; meiotic nuclear division [GO:0007126]; organ regeneration [GO:0031100]; response to organic cyclic compound [GO:0014070]cATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; protein C-terminus binding [GO:0008022]chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]DFUNCTION: Thought to be required for maintaining cell proliferation.Q9NWU1OXSM83-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15668256}.acyl-CoA metabolic process [GO:0006637]; medium-chain fatty acid biosynthetic process [GO:0051792]; short-chain fatty acid biosynthetic process [GO:0051790]?3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]FUNCTION: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function. {ECO:0000269|PubMed:15668256}.Q9NXE4NSMA3!Sphingomyelin phosphodiesterase 4SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16517606}; Single-pass membrane protein {ECO:0000269|PubMed:16517606}. Golgi apparatus membrane {ECO:0000269|PubMed:16517606}; Single-pass membrane protein {ECO:0000269|PubMed:16517606}.Scellular response to tumor necrosis factor [GO:0071356]; ceramide biosynthetic process [GO:0046513]; glycerophospholipid catabolic process [GO:0046475]; glycosphingolipid metabolic process [GO:0006687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]; sphingomyelin catabolic process [GO:0006685]metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767]; sphingomyelin phosphodiesterase D activity [GO:0050290]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; trans-Golgi network [GO:0005802]FUNCTION: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. {ECO:0000269|PubMed:16517606}.Q6RW13ATRAP1Type-1 angiotensin II receptor-associated proteinSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12960423}; Multi-pass membrane protein {ECO:0000269|PubMed:12960423}. Golgi apparatus membrane {ECO:0000269|PubMed:12960423}; Multi-pass membrane protein {ECO:0000269|PubMed:12960423}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12960423}; Multi-pass membrane protein {ECO:0000269|PubMed:12960423}. Note=Present in perinuclear vesicular membranes, Endoplasmic reticulum, Golgi and endocytic vesicles.Kregulation of blood pressure [GO:0008217]; response to hypoxia [GO:0001666]2angiotensin type II receptor activity [GO:0004945]Acell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]WFUNCTION: Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity. {ECO:0000269|PubMed:12960423}.O60678ANM3&Protein arginine N-methyltransferase 3histone arginine methylation [GO:0034969]; negative regulation of protein ubiquitination [GO:0031397]; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [GO:0019919]; regulation of transcription, DNA-templated [GO:0006355] histone-arginine N-methyltransferase activity [GO:0008469]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]Ccytoplasm [GO:0005737]; cytosol [GO:0005829]; ribosome [GO:0005840]vFUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.O95208EPN2Epsin-2'SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10567358}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10567358}. Note=In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex.embryonic organ development [GO:0048568]; endocytosis [GO:0006897]; in utero embryonic development [GO:0001701]; Notch signaling pathway [GO:0007219]; regulation of endocytosis [GO:0030100]clathrin coat of endocytic vesicle [GO:0030128]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]xFUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.Q9NRZ5PLCD41-acyl-sn-glycerol-3-phosphate acyltransferase deltaFUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000250}.Q9P2D0IBTK#Inhibitor of Bruton tyrosine kinaseSUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Translocates to the plasma membrane upon IgM stimulation.; SUBCELLULAR LOCATION: Isoform 2: Nucleus.negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein tyrosine kinase activity [GO:0061099]; release of sequestered calcium ion into cytosol [GO:0051209]\protein kinase binding [GO:0019901]; protein tyrosine kinase i< nhibitor activity [GO:0030292]FUNCTION: Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription. {ECO:0000269|PubMed:11577348}.Q01581HMCS1/Hydroxymethylglutaryl-CoA synthase, cytoplasmicbrain development [GO:0007420]; cellular lipid metabolic process [GO:0044255]; cellular response to cholesterol [GO:0071397]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cholesterol biosynthetic process [GO:0006695]; isoprenoid biosynthetic process [GO:0008299]; lipid metabolic process [GO:0006629]; liver development [GO:0001889]; male gonad development [GO:0008584]; response to drug [GO:0042493]; response to lipoprotein particle [GO:0055094]; response to low light intensity stimulus [GO:0009645]; response to purine-containing compound [GO:0014074]; response to tellurium ion [GO:0046690]; response to vitamin E [GO:0033197]; small molecule metabolic process [GO:0044281]drug binding [GO:0008144]; hydroxymethylglutaryl-CoA synthase activity [GO:0004421]; isomerase activity [GO:0016853]; organic acid binding [GO:0043177]zcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]~FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.Q02447SP3Transcription factor Sp3SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies.6B cell differentiation [GO:0030183]; definitive hemopoiesis [GO:0060216]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; embryonic skeletal system development [GO:0048706]; enucleate erythrocyte differentiation [GO:0043353]; granulocyte differentiation [GO:0030851]; liver development [GO:0001889]; lung development [GO:0030324]; megakaryocyte differentiation [GO:0030219]; monocyte differentiation [GO:0030224]; natural killer cell differentiation [GO:0001779]; negative regulation of transcription, DNA-templated [GO:0045892]; ossification [GO:0001503]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; T cell differentiation [GO:0030217]; transcription, DNA-templated [GO:0006351]; trophectodermal cell differentiation [GO:0001829]Uchromatin binding [GO:0003682]; core promoter proximal region sequence-specific DNA binding [GO:0000987]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; transcriptional repressor complex [GO:0017053]FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping. {ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11812829, ECO:0000269|PubMed:12419227, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:15247228, ECO:0000269|PubMed:15494207, ECO:0000269|PubMed:15554904, ECO:0000269|PubMed:16781829, ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:18187045, ECO:0000269|PubMed:18617891, ECO:0000269|PubMed:9278495}.P07203GPX1Glutathione peroxidase 1 aging [GO:0007568]; angiogenesis involved in wound healing [GO:0060055]; arachidonic acid metabolic process [GO:0019369]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; endothelial cell development [GO:0001885]; fat cell differentiation [GO:0045444]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide catabolic process [GO:0042744]; interaction with symbiont [GO:0051702]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; lipoxygenase pathway [GO:0019372]; myoblast proliferation [GO:0051450]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of fibril organization [GO:1902905]; positive regulation of protein kinase B signaling [GO:0051897]; protein oxidation [GO:0018158]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide catabolic process [GO:0006195]; regulation of gene expression, epigenetic [GO:0040029]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of neuron apoptotic process [GO:0043523]; regulation of proteasomal protein catabolic process [GO:0061136]; response to estradiol [GO:0032355]; response to folic acid [GO:0051593]; response to gamma radiation [GO:0010332]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to lipid hydroperoxide [GO:0006982]; response to nicotine [GO:0035094]; response to reactive oxygen species [GO:0000302]; response to selenium ion [GO:0010269]; response to symbiotic bacterium [GO:0009609]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; skeletal muscle fiber development [GO:0048741]; skeletal muscle tissue regeneration [GO:0043403]; small molecule metabolic process [GO:0044281]; temperature homeostasis [GO:0001659]; triglyceride metabolic process [GO:0006641]; UV protection [GO:0009650]; vasodilation [GO:0042311]glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; selenium binding [GO:0008430]; SH3 domain binding [GO:0017124]KFUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown.Q86WC4OSTM10Osteopetrosis-associated transmembrane protein 1SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21527911}; Single-pass type I membrane protein {ECO:0000269|PubMed:21527911}. Note=Requires CLCN7 to travel to lysosomes.wion transmembrane transport [GO:0034220]; osteoclast differentiation [GO:0030316]; transmembrane transport [GO:0055085]cytoplasm [GO:0005737]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; nucleus [GO:0005634]XFUNCTION: Required for osteoclast and melanocyte maturation and function. {ECO:0000250}.P54819KAD2!Adenylate kinase 2, mitochondrialMADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide phosphorylation [GO:0046939]; small molecule< metabolic process [GO:0044281]@adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; sperm mitochondrial sheath [GO:0097226]FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:19043416}.O60292SI1L38Signal-induced proliferation-associated 1-like protein 3hematopoietic progenitor cell differentiation [GO:0002244]; regulation of small GTPase mediated signal transduction [GO:0051056]Q8IUH5ZDH17Palmitoyltransferase ZDHHC17xSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15603740, ECO:0000269|PubMed:18794299}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18794299}; Multi-pass membrane protein {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi membrane vesicles. {ECO:0000269|PubMed:18794299}.lipoprotein transport [GO:0042953]; magnesium ion transport [GO:0015693]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein palmitoylation [GO:0018345]; signal transduction [GO:0007165]identical protein binding [GO:0042802]; magnesium ion transmembrane transporter activity [GO:0015095]; palmitoyltransferase activity [GO:0016409]; protein-cysteine S-palmitoyltransferase activity [GO:0019706]; signal transducer activity [GO:0004871]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle membrane [GO:0030660]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]hFUNCTION: Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD (PubMed:15603740, PubMed:15489887, PubMed:19139280). Palmitoylates MPP1 in erythrocytes (PubMed:22496366). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (PubMed:12393793). May play a role in Mg(2+) transport (PubMed:18794299). {ECO:0000269|PubMed:12393793, ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603740, ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19139280, ECO:0000269|PubMed:22496366}.Q9NRS6SNX15Sorting nexin-15xSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11085978}. Membrane {ECO:0000269|PubMed:11085978}; Peripheral membrane protein {ECO:0000269|PubMed:11085978}; Cytoplasmic side {ECO:0000269|PubMed:11085978}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11085978}; Peripheral membrane protein {ECO:0000269|PubMed:11085978}; Cytoplasmic side {ECO:0000269|PubMed:11085978}.cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]FUNCTION: May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN. {ECO:0000269|PubMed:11085978}.Q15154PCM1!Pericentriolar material 1 proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic granule. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cytoplasm, cytoskeleton, cilium basal body. Note=Recruitement to the centrosome requires microtubules and dynein. The majority of the protein dissociates from the centrosome during metaphase and subsequently localizes to the cleavage site in telophase. Displaced from centriolar satellites and centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAP kinase signaling.centrosome organization [GO:0051297]; cilium assembly [GO:0042384]; cytoplasmic microtubule organization [GO:0031122]; G2/M transition of mitotic cell cycle [GO:0000086]; interkinetic nuclear migration [GO:0022027]; intraciliary transport involved in cilium morphogenesis [GO:0035735]; microtubule anchoring [GO:0034453]; microtubule anchoring at centrosome [GO:0034454]; mitotic cell cycle [GO:0000278]; negative regulation of neurogenesis [GO:0050768]; neuronal stem cell maintenance [GO:0097150]; nonmotile primary cilium assembly [GO:0035058]; organelle organization [GO:0006996]; positive regulation of intracellular protein transport [GO:0090316]; protein localization to centrosome [GO:0071539]centriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; pericentriolar material [GO:0000242]; protein complex [GO:0043234]FUNCTION: Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia. {ECO:0000269|PubMed:12403812, ECO:0000269|PubMed:15659651, ECO:0000269|PubMed:16943179, ECO:0000269|PubMed:20551181, ECO:0000269|PubMed:24121310}.O95870ABHGA)Abhydrolase domain-containing protein 16AP16298PP2BBFSerine/threonine-protein phosphatase 2B catalytic subunit beta isoform"axon extension [GO:0048675]; calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion-dependent exocytosis [GO:0017156]; cellular response to drug [GO:0035690]; dephosphorylation [GO:0016311]; Fc-epsilon receptor signaling pathway [GO:0038095]; heart development [GO:0007507]; innate immune response [GO:0045087]; learning [GO:0007612]; locomotion involved in locomotory behavior [GO:0031987]; lymphangiogenesis [GO:0001946]; memory [GO:0007613]; negative regulation of T cell mediated cytotoxicity [GO:0001915]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of NFAT protein import into nucleus [GO:0051533]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein dephosphorylation [GO:0006470]; protein phosphorylation [GO:0006468]; regulation of insulin secretion [GO:0050796]; regulation of synaptic plasticity [GO:0048167]; response to cytokine [GO:0034097]; signal transduction [GO:0007165]; social behavior [GO:0035176]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell activation [GO:0042110]; T cell differentiation [GO:0030217]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]Ncalcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; drug binding [GO:0008144]; enzyme binding [GO:0019899]; protein dimerization activity [GO:0046983]; protein phosphatase 2B binding [GO:0030346]; protein serine/threonine phosphatase activity [GO:0004722]calcineurin complex [GO:0005955]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]; Z disc [GO:0030018]FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.Q8WVM0TFB1M.Dimethyladenosine transferase 1, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11809803}.mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]{DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179]Fmitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO< :0042645]FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. {ECO:0000269|PubMed:11809803, ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151}.P62140PP1B?Serine/threonine-protein phosphatase PP1-beta catalytic subunitwSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654}. Nucleus {ECO:0000269|PubMed:11739654}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11739654}. Nucleus, nucleolus {ECO:0000269|PubMed:11739654}. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.7cell division [GO:0051301]; circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; G2/M transition of mitotic cell cycle [GO:0000086]; glycogen metabolic process [GO:0005977]; mitotic cell cycle [GO:0000278]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; protein dephosphorylation [GO:0006470]; regulation of cell adhesion [GO:0030155]; regulation of circadian rhythm [GO:0042752]; regulation of glycogen biosynthetic process [GO:0005979]; regulation of glycogen catabolic process [GO:0005981]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transforming growth factor beta receptor signaling pathway [GO:0007179]; triglyceride catabolic process [GO:0019433]metal ion binding [GO:0046872]; myosin-light-chain-phosphatase activity [GO:0050115]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein kinase binding [GO:0019901]4cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; glycogen granule [GO:0042587]; MLL5-L complex [GO:0070688]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein phosphatase type 1 complex [GO:0000164]; PTW/PP1 phosphatase complex [GO:0072357]DFUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.P14625ENPL EndoplasminSUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.Dactin rod assembly [GO:0031247]; ATF6-mediated unfolded protein response [GO:0036500]; cellular protein metabolic process [GO:0044267]; cellular response to ATP [GO:0071318]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; protein folding in endoplasmic reticulum [GO:0034975]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; regulation of phosphoprotein phosphatase activity [GO:0043666]; response to endoplasmic reticulum stress [GO:0034976]; response to hypoxia [GO:0001666]; retrograde protein transport, ER to cytosol [GO:0030970]; sequestering of calcium ion [GO:0051208]; toll-like receptor signaling pathway [GO:0002224]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; low-density lipoprotein particle receptor binding [GO:0050750]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]; virion binding [GO:0046790]cytosol [GO:0005829]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]EFUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. {ECO:0000250, ECO:0000269|PubMed:18264092}.Q5JU67CI117 Uncharacterized protein C9orf117Q8TBC4UBA3,NEDD8-activating enzyme E1 catalytic subunitdcellular protein modification process [GO:0006464]; endomitotic cell cycle [GO:0007113]; innate immune response [GO:0045087]; negative regulation of transcription, DNA-templated [GO:0045892]; protein neddylation [GO:0045116]; proteolysis [GO:0006508]; regulation of cell cycle [GO:0051726]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]acid-amino acid ligase activity [GO:0016881]; ATP binding [GO:0005524]; NEDD8 activating enzyme activity [GO:0019781]; protein heterodimerization activity [GO:0046982]FUNCTION: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. {ECO:0000269|PubMed:10207026, ECO:0000269|PubMed:12740388, ECO:0000269|PubMed:9694792}.Q8TEW0PARD3 Partitioning defective 3 homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endomembrane system {ECO:0000269|PubMed:20332120}. Cell junction {ECO:0000269|PubMed:20332120}. Cell junction, tight junction {ECO:0000269|PubMed:20332120}. Cell membrane {ECO:0000269|PubMed:20332120}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20332120}. Note=Localized along the cell-cell contact region. Colocalizes with PARD6A and PRKCI at epithelial tight junctions. Colocalizes with the cortical actin that overlays the meiotic spindle during metaphase I and metaphase II. Colocalized with SIRT2 in internode region of myelin sheat (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. {ECO:0000250}. apical constriction [GO:0003383]; asymmetric cell division [GO:0008356]; axonogenesis [GO:0007409]; bicellular tight junction assembly [GO:0070830]; cell-cell junction organization [GO:0045216]; cell cycle [GO:0007049]; cell junction assembly [GO:0034329]; centrosome localization [GO:0051642]; establishment of epithelial cell polarity [GO:0090162]; establishment or maintenance of cell polarity [GO:0007163]; microtubule cytoskeleton organization [GO:0000226]; myelination in peripheral nervous system [GO:0022011]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of myelination [GO:0031643]; protein complex assembly [GO:0006461]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]; protein targeting to membrane [GO:0006612]; regulation of actin filament-bas< ed process [GO:0032970]; regulation of cellular localization [GO:0060341]; transforming growth factor beta receptor signaling pathway [GO:0007179]; wound healing, spreading of cells [GO:0044319]phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]apical part of cell [GO:0045177]; axonal growth cone [GO:0044295]; bicellular tight junction [GO:0005923]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; internode region of axon [GO:0033269]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; spindle [GO:0005819]FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Targets the phosphatase PTEN to cell junctions. Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:19812038}.P11940PABP1Polyadenylate-binding protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus.kcellular protein metabolic process [GO:0044267]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; mRNA stabilization [GO:0048255]; negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; positive regulation of translation [GO:0045727]; translation [GO:0006412]; translational initiation [GO:0006413]nucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; poly(U) RNA binding [GO:0008266]; protein C-terminus binding [GO:0008022]; translation activator activity [GO:0008494]Jcatalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299). {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:25480299}.Q13439GOGA4Golgin subfamily A member 4hSUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus.Golgi to plasma membrane protein transport [GO:0043001]; positive regulation of axon extension [GO:0045773]; protein targeting to Golgi [GO:0000042]; vesicle-mediated transport [GO:0016192]GTPase binding [GO:0051020]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; trans-Golgi network [GO:0005802]FUNCTION: May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1. {ECO:0000269|PubMed:15265687}.Q9BXP2S12A9!Solute carrier family 12 member 9}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10871601}; Multi-pass membrane protein {ECO:0000269|PubMed:10871601}.cell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; potassium ion homeostasis [GO:0055075]; potassium ion import [GO:0010107]cation:chloride symporter activity [GO:0015377]; potassium:chloride symporter activity [GO:0015379]; potassium ion symporter activity [GO:0022820]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]FUNCTION: May be an inhibitor of SLC12A1. Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function. {ECO:0000269|PubMed:10871601}.Q8TBF4ZCRB1@Zinc finger CCHC-type and RNA-binding motif-containing protein 1fSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16959469}.Q15629TRAM11Translocating chain-associated membrane protein 1 cellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; gene expression [GO:0010467]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]; viral process [GO:0016032]eFUNCTION: Stimulatory or required for the translocation of secretory proteins across the ER membrane.O95059RPP14"Ribonuclease P protein subunit p14>ribonuclease P activity [GO:0004526]; RNA binding [GO:0003723]sFUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.Q9NZV1CRIM1$Cysteine-rich motor neuron 1 proteinSUBCELLULAR LOCATION: Processed cysteine-rich motor neuron 1 protein: Secreted.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12805376}; Single-pass type I membrane protein {ECO:0000269|PubMed:12805376}.insulin-like growth factor receptor signaling pathway [GO:0048009]; nervous system development [GO:0007399]; regulation of cell growth [GO:0001558]insulin-like growth factor-activated receptor activity [GO:0005010]; PDZ domain binding [GO:0030165]; serine-type endopeptidase inhibitor activity [GO:0004867]eFUNCTION: May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface. {ECO:0000269|PubMed:12464430, ECO:0000269|PubMed:12805376}.Q9Y646CBPQCarboxypeptidase Q+SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:10206990}. Golgi apparatus {ECO:0000269|PubMed:10206990}. Lysosome {ECO:0000250}. Secreted {ECO:0000269|PubMed:10206990}. Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. {ECO:0000250}.peptide catabolic process [GO:0043171]; proteolysis< [GO:0006508]; thyroid hormone generation [GO:0006590]; tissue regeneration [GO:0042246]carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallodipeptidase activity [GO:0070573]; protein homodimerization activity [GO:0042803]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]FUNCTION: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor.Q9BTU6P4K2A*Phosphatidylinositol 4-kinase type 2-alpha}SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:22535966}; Lipid-anchor {ECO:0000269|PubMed:22535966}. Membrane raft {ECO:0000269|PubMed:11279162}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q2TBE6}. Cell junction, synapse, presynaptic cell membrane {ECO:0000250|UniProtKB:Q2TBE6}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q2TBE6}. Mitochondrion {ECO:0000250|UniProtKB:Q2TBE6}. Endosome {ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:23146885}. Cytoplasmic vesicle {ECO:0000269|PubMed:16443754}. Membrane {ECO:0000269|PubMed:24675427}; Lipid-anchor {ECO:0000269|PubMed:24675427}. Cell membrane {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754}. Note=Localized in neuronal cell body. Transported from neuronal cell body to neuron projections in a BLOC-1- and AP-3-complexes-dependent manner. Enriched in neurite tips and neuron projections in a BLOC-1- and AP-3-complexes-dependent manner (By similarity). Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. {ECO:0000250|UniProtKB:Q2TBE6, ECO:0000250|UniProtKB:Q99M64}.<activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; basophil degranulation [GO:0002561]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]1-phosphatidylinositol 4-kinase activity [GO:0004430]; AP-3 adaptor complex binding [GO:0035651]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]cell junction [GO:0030054]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; exocytic vesicle [GO:0070382]; Golgi apparatus [GO:0005794]; growing cell tip [GO:0035838]; host cell presynaptic membrane [GO:0044231]; integral component of plasma membrane [GO:0005887]; intrinsic component of membrane [GO:0031224]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; presynaptic membrane [GO:0042734]; protein complex [GO:0043234]; synaptic vesicle membrane [GO:0030672]FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). {ECO:0000269|PubMed:11279162, ECO:0000269|PubMed:16443754, ECO:0000269|PubMed:20388919, ECO:0000269|PubMed:23146885, ECO:0000269|PubMed:24675427, ECO:0000269|PubMed:25168678, ECO:0000305}.P29597TYK2)Non-receptor tyrosine-protein kinase TYK2 JAK kniasescell differentiation [GO:0030154]; cell migration [GO:0016477]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; peptidyl-tyrosine autophosphorylation [GO:0038083]; protein phosphorylation [GO:0006468]; regulation of cell proliferation [GO:0042127]; regulation of type I interferon-mediated signaling pathway [GO:0060338]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; type I interferon signaling pathway [GO:0060337]ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]FUNCTION: Probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. {ECO:0000269|PubMed:7526154}.Q8WWM9CYGB Cytoglobinfatty acid oxidation [GO:0019395]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of hepatic stellate cell activation [GO:2000490]; nitric oxide metabolic process [GO:0046209]; oxygen transport [GO:0015671]; regulation of nitric-oxide synthase activity [GO:0050999]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]catalase activity [GO:0004096]; fatty acid peroxidase activity [GO:0047888]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; nitric oxide dioxygenase activity [GO:0008941]; oxygen binding [GO:0019825]; oxygen transporter activity [GO:0005344]; peroxidase activity [GO:0004601]Ucytosol [GO:0005829]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]FUNCTION: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.Q9BSH4TACO11Translational activator of cytochrome c oxidase 1BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19503089}.}FUNCTION: Acts as a translational activator of mitochondrially-encoded cytochrome c oxidase 1. {ECO:0000269|PubMed:19503089}.P36941TNR33Tumor necrosis factor receptor superfamily member 3apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; myeloid dendritic cell differentiation [GO:0043011]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of JNK cascade [GO:0046330]; signal transduction [GO:0007165]; viral process [GO:0016032]Uidentical protein binding [GO:0042802]; ubiquitin protein ligase binding [GO:0031625]FUNCTION: Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs. {ECO:0000269|PubMed:10799510, ECO:0000269|PubMed:8171323}.Q9UPS8ANR26+Ankyrin repeat domain-containing protein 26glucose homeostasis [GO:0042593]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of organ growth [GO:0046621]; regulation of fatty acid metabolic process [GO:0019217]; regulation of feeding behavior [GO:0060259]4actin filament [GO:0005884]; centrosome [GO:0005813]Q8IXB1DJC10"DnaJ homolog subfamily C member 10SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:23769672}.cell redox homeostasis [GO:0045454]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum st< ress [GO:0070059]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of ATPase activity [GO:0032781]; protein folding in endoplasmic reticulum [GO:0034975]; response to endoplasmic reticulum stress [GO:0034976]xATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; chaperone binding [GO:0051087]; disulfide oxidoreductase activity [GO:0015036]; Hsp70 protein binding [GO:0030544]; misfolded protein binding [GO:0051787]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; protein disulfide oxidoreductase activity [GO:0015035];FUNCTION: Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress. {ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:18400946, ECO:0000269|PubMed:19122239, ECO:0000269|PubMed:23769672}.Q86VZ4LRP113Low-density lipoprotein receptor-related protein 11#phosphoprotein binding [GO:0051219]Q8NBL1PGLT1Protein O-glucosyltransferase 1mSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16524674, ECO:0000269|PubMed:24387993}.cardiovascular system development [GO:0072358]; glycolipid metabolic process [GO:0006664]; Notch signaling pathway [GO:0007219]; positive regulation of Notch signaling pathway [GO:0045747]; protein O-linked glycosylation [GO:0006493]glucosyltransferase activity [GO:0046527]; protein xylosyltransferase activity [GO:0030158]; UDP-glucosyltransferase activity [GO:0035251]; UDP-xylosyltransferase activity [GO:0035252]FUNCTION: Dual specificity glycosyltransferase. Catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats, such as those found in F7, F9 and NOTCH2, on the consensus sequence C-X-S-X-P-C. Positively regulates Notch signaling without affecting Notch ligand binding. {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:21949356}.P27694RFA10Replication protein A 70 kDa DNA-binding subunitSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17959650}. Nucleus, PML body {ECO:0000269|PubMed:17959650}. Note=Enriched in PML bodies in cells displaying alternative lengthening of their telomeres. {ECO:0000269|PubMed:17959650}.base-excision repair [GO:0006284]; cellular protein metabolic process [GO:0044267]; cellular response to heat [GO:0034605]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA recombinase assembly [GO:0000730]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; G1/S transition of mitotic cell cycle [GO:0000082]; hemopoiesis [GO:0030097]; homeostasis of number of cells within a tissue [GO:0048873]; in utero embryonic development [GO:0001701]; meiotic nuclear division [GO:0007126]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA gap filling [GO:0006297]; positive regulation of cell proliferation [GO:0008284]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of cellular response to heat [GO:1900034]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]DNA replication factor A complex [GO:0005662]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance (PubMed:17959650). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). {ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.Q9H305CDIP1(Cell death-inducing p53-target protein 1apoptotic process [GO:0006915]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; tumor necrosis factor-mediated signaling pathway [GO:0033209]FUNCTION: Acts as an important p53/TP53-apoptotic effector. Regulates TNF-alpha-mediated apoptosis in a p53/TP53-dependent manner. {ECO:0000269|PubMed:17599062}.Q9NWB7IFT57+Intraflagellar transport protein 57 homologSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Concentrates within the inner segment of cilia. {ECO:0000250}.Nactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; cilium assembly [GO:0042384]; heart looping [GO:0001947]; intraciliary transport [GO:0042073]; left/right pattern formation [GO:0060972]; negative regulation of epithelial cell proliferation [GO:0050680]; neural tube closure [GO:0001843]; organelle organization [GO:0006996]; regulation of apoptotic process [GO:0042981]; regulation of transcription, DNA-templated [GO:0006355]; smoothened signaling pathway [GO:0007224]; transcription, DNA-templated [GO:0006351]6axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:003606< 4]; ciliary tip [GO:0097542]; cilium [GO:0005929]; dendrite terminus [GO:0044292]; Golgi apparatus [GO:0005794]; intraciliary transport particle B [GO:0030992]; photoreceptor connecting cilium [GO:0032391]; primary cilium [GO:0072372]FUNCTION: Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway (By similarity). Has pro-apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear. {ECO:0000250, ECO:0000269|PubMed:11788820, ECO:0000269|PubMed:17107665, ECO:0000269|PubMed:17623017}.Q8IY47KBTB20Kelch repeat and BTB domain-containing protein 2Q9Y3I0RTCB!tRNA-splicing ligase RtcB homolog#SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24608264}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03144, ECO:0000269|PubMed:24608264}. Note=Enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low. {ECO:0000269|PubMed:24608264}.in utero embryonic development [GO:0001701]; placenta development [GO:0001890]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; RNA ligase (ATP) activity [GO:0003972]; vinculin binding [GO:0017166]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; tRNA-splicing ligase complex [GO:0072669]FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. {ECO:0000269|PubMed:21311021, ECO:0000269|PubMed:24870230}.Q96D31CRCM13Calcium release-activated calcium channel protein 1JSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:24351972}; Multi-pass membrane protein {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:22641696, ECO:0000269|PubMed:24351972}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23307288}. Note=Isoform beta is more mobile in the plasma membrane. Colocalizes with UBQLN1 in the autophagosome. {ECO:0000269|PubMed:23307288}.blood coagulation [GO:0007596]; immune system process [GO:0002376]; positive regulation of calcium ion transport [GO:0051928]; regulation of calcium ion transport [GO:0051924]; store-operated calcium entry [GO:0002115]\identical protein binding [GO:0042802]; store-operated calcium channel activity [GO:0015279]autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; protein complex [GO:0043234]eFUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT. {ECO:0000269|PubMed:16582901, ECO:0000269|PubMed:16645049, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628}.Q8IY95TM192Transmembrane protein 192TSUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. Late endosome.extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]Q6P6B7ANR16+Ankyrin repeat domain-containing protein 16Q68CQ4DIEXF(Digestive organ expansion factor homologmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; multicellular organismal development [GO:0007275][poly(A) RNA binding [GO:0044822]; rRNA binding [GO:0019843]; U3 snoRNA binding [GO:0034511]=nucleolus [GO:0005730]; small-subunit processome [GO:0032040]gFUNCTION: Regulates the p53 pathway to control the expansion growth of digestive organs. {ECO:0000250}.Q5SXM8DNLZDNL-type zinc finger proteinBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23462535}.wprotein folding [GO:0006457]; protein import into mitochondrial matrix [GO:0030150]; protein stabilization [GO:0050821]=chaperone binding [GO:0051087]; zinc ion binding [GO:0008270]FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation. {ECO:0000269|PubMed:23462535}.O95159ZFPL1Zinc finger protein-like 1SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:18323775}; Single-pass membrane protein {ECO:0000269|PubMed:18323775}.`regulation of transcription, DNA-templated [GO:0006355]; vesicle-mediated transport [GO:0016192]_Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]FUNCTION: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130. {ECO:0000269|PubMed:18323775}.Q96SK2TM209Transmembrane protein 209Q15464SHB'SH2 domain-containing adapter protein BSUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Associates with membrane lipid rafts upon TCR stimulation.angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; positive regulation of signal transduction [GO:0009967]; signal transduction [GO:0007165]; vascular endothelial growth factor receptor signaling pathway [GO:0048010] FUNCTION: Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells. {ECO:0000269|PubMed:10828022, ECO:0000269|PubMed:10837138, ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12464388, ECO:0000269|PubMed:12520086, ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15919073, ECO:0000269|PubMed:8806685, ECO:0000269|PubMed:9484780, ECO:0000269|PubMed:9751119}.Q9H8W4PKHF27Pleckstrin homology domain-containing family F member 2-SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein. Endoplasmic reticulum. Note=Colocalizes with EEA1 and RAB5 at endosomal membrane fusion hot spots. May translocate to the endoplasmic reticulum in the early phase of apoptosis (PubMed:18288467). {ECO:0000269|PubMed:18288467}.hearly endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; transport vesicle [GO:0030133](FUNCTION: May play a role in early endosome fusion upstream of RAB5, hence regulating receptor trafficking and fluid-phase transport. Enhances cellular sensitivity to TNF-induced apoptosis (PubMed:18288467). {ECO:0000269|PubMed:18288467, ECO:0000269|PubMed:19995552, ECO:0000269|PubMed:22816767}.Q02952AKA12A-kinase anchor protein 12SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=May be part of the cortical cytoskeleton.G-protein coupled recepto< r signaling pathway [GO:0007186]; positive regulation of cAMP biosynthetic process [GO:0030819]; positive regulation of protein kinase A signaling [GO:0010739]; protein targeting [GO:0006605]; regulation of protein kinase C signaling [GO:0090036]Madenylate cyclase binding [GO:0008179]; protein kinase A binding [GO:0051018]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]FUNCTION: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).Q9Y2D4EXC6BExocyst complex component 6Bexocyst [GO:0000145]P30260CDC27&Cell division cycle protein 27 homologanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; cell proliferation [GO:0008283]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K11-linked ubiquitination [GO:0070979]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]Q86YZ3HORNHornerinSUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:21282207}. Note=Found in keratohyalin granules in the granular cells of the epidermis.cell envelope organization [GO:0043163]; establishment of skin barrier [GO:0061436]; hematopoietic progenitor cell differentiation [GO:0002244]; keratinization [GO:0031424]cell envelope [GO:0030313]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; keratohyalin granule [GO:0036457]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]]FUNCTION: Component of the epidermal cornified cell envelopes. {ECO:0000269|PubMed:21282207}.O95816BAG2*BAG family molecular chaperone regulator 2cellular response to heat [GO:0034605]; protein folding [GO:0006457]; protein metabolic process [GO:0019538]; regulation of cellular response to heat [GO:1900034]XFUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.O95865DDAH23N(G),N(G)-dimethylarginine dimethylaminohydrolase 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21898353}. Mitochondrion {ECO:0000269|PubMed:21898353}. Note=Translocates from cytosol to mitochondrion upon IL-1beta stimulation in chondrocytes.8arginine catabolic process [GO:0006527]; citrulline metabolic process [GO:0000052]; negative regulation of apoptotic process [GO:0043066]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated signal transduction [GO:0007263]; positive regulation of nitric oxide biosynthetic process [GO:0045429]jamino acid binding [GO:0016597]; catalytic activity [GO:0003824]; dimethylargininase activity [GO:0016403]FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. {ECO:0000269|PubMed:10493931}.P20962PTMS Parathymosin@DNA replication [GO:0006260]; immune system process [GO:0002376]FUNCTION: Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections.P36021MOT8Monocarboxylate transporter 8ion transmembrane transport [GO:0034220]; monocarboxylic acid transport [GO:0015718]; thyroid hormone transport [GO:0070327]; transport [GO:0006810]monocarboxylic acid transmembrane transporter activity [GO:0008028]; symporter activity [GO:0015293]; thyroid hormone transmembrane transporter activity [GO:0015349]; transporter activity [GO:0005215]FUNCTION: Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr (By similarity). {ECO:0000250}.P02766TTHY Transthyretin*SUBCELLULAR LOCATION: Secreted. Cytoplasm.extracellular matrix organization [GO:0030198]; phototransduction, visible light [GO:0007603]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; thyroid hormone transport [GO:0070327]; transport [GO:0006810]Lidentical protein binding [GO:0042802]; thyroid hormone binding [GO:0070324]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein complex [GO:0043234]FUNCTION: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. {ECO:0000269|PubMed:3714052}.P28827PTPRM-Receptor-type tyrosine-protein phosphatase muRhomophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; neuron projection development [GO:0031175]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of vasodilation [GO:0045909]; protein dephosphorylation [GO:0006470]; response to drug [GO:0042493]; retina layer formation [GO:0010842]; retinal ganglion cell axon guidance [GO:0031290]; signal transduction [GO:0007165]cadherin binding [GO:0045296]; identical protein binding [GO:0042802]; protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. {ECO:0000269|PubMed:16456543}.O15067PUR4*Phosphoribosylformylglycinamidine synthasede novo' IMP biosynthetic process [GO:0006189]; glutamine metabolic process [GO:0006541]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; ribonucleoside monophosphate biosynthetic process [GO:0009156]; small molecule metabolic process [GO:0044281]zATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylformylglycinamidine synthase activity [GO:0004642]#FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity). {ECO:0000250}.Q14696MESDLDLR chaperone MESDgSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:15014448, ECO:0000269|PubMed:17488095}.mesoderm development [GO:0007498]; protein folding [GO:0006457]; protein localization to cell surface [GO:0034394]; Wnt signaling pathway [GO:0016055]@endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]FUNCTION: Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. {ECO:0000269|PubMed:15014448, ECO:0000269|PubMed:17488095}.P05413FABPH!Fatty acid-binding protein, heartcholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; long-chain fatt< y acid import [GO:0044539]; negative regulation of cell proliferation [GO:0008285]; phospholipid homeostasis [GO:0055091]; positive regulation of phospholipid biosynthetic process [GO:0071073]; regulation of fatty acid oxidation [GO:0046320]; response to drug [GO:0042493]; response to fatty acid [GO:0070542]; response to insulin [GO:0032868]; small molecule metabolic process [GO:0044281]; triglyceride catabolic process [GO:0019433]cytoskeletal protein binding [GO:0008092]; icosatetraenoic acid binding [GO:0050543]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]scytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; sarcoplasm [GO:0016528]}FUNCTION: FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.Q6UX15LAYNLayilinSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the membrane ruffles. {ECO:0000250}.Gcarbohydrate binding [GO:0030246]; hyaluronic acid binding [GO:0005540]xcell surface [GO:0009986]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; ruffle [GO:0001726]BFUNCTION: Receptor for hyaluronate. {ECO:0000269|PubMed:11294894}.Q96RQ1ERGI2>Endoplasmic reticulum-Golgi intermediate compartment protein 2SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasm. Nucleus. Note=Cycles between the endoplasmic reticulum and the Golgi. According to a report, localizes to the nucleus (PubMed:11445006). Another report shows a partial localization in the nucleus (PubMed:17980171). {ECO:0000269|PubMed:11445006, ECO:0000269|PubMed:17980171}.Vcytoplasm [GO:0005737]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]O15397IPO8 Importin-8lgene expression [GO:0010467]; intracellular protein transport [GO:0006886]; signal transduction [GO:0007165]Ran GTPase binding [GO:0008536]FUNCTION: Seems to function in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro mediates the nuclear import of SRP19. {ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9214382}.P04424ARLYArgininosuccinate lyasearginine biosynthetic process via ornithine [GO:0042450]; arginine catabolic process [GO:0006527]; cellular nitrogen compound metabolic process [GO:0034641]; internal protein amino acid acetylation [GO:0006475]; small molecule metabolic process [GO:0044281]; urea cycle [GO:0000050]-argininosuccinate lyase activity [GO:0004056]Q6AI12ANR40+Ankyrin repeat domain-containing protein 40Q9P258RCC2 Protein RCC2kSUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Note=Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during anaphase. Here, the protein covers the entire equatorial diameter from cortex to cortex.activation of GTPase activity [GO:0090630]; cell division [GO:0051301]; chromosome passenger complex localization to kinetochore [GO:0072356]; endosome organization [GO:0007032]; establishment of protein localization [GO:0045184]; focal adhesion assembly [GO:0048041]; integrin-mediated signaling pathway [GO:0007229]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of GTPase activity [GO:0034260]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; positive regulation of attachment of spindle microtubules to kinetochore [GO:0051987]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; regulation of cell migration [GO:0030334]; regulation of fibroblast migration [GO:0010762]; regulation of ruffle assembly [GO:1900027]; small GTPase mediated signal transduction [GO:0007264]microtubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; Rac GTPase binding [GO:0048365]; small GTPase binding [GO:0031267]chromosome, centromeric core domain [GO:0034506]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]FUNCTION: Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1. {ECO:0000269|PubMed:12919680}.Q7Z3B1NEGR1Neuronal growth regulator 1feeding behavior [GO:0007631]; locomotory behavior [GO:0007626]; positive regulation of neuron projection development [GO:0010976]; regulation of neurogenesis [GO:0050767]; single organismal cell-cell adhesion [GO:0016337]anchored component of membrane [GO:0031225]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]FUNCTION: May be involved in cell-adhesion. May function as a trans-neural growth-promoting factor in regenerative axon sprouting in the mammalian brain (By similarity). {ECO:0000250}.O60884DNJA2!DnaJ homolog subfamily A member 2carbon tetrachloride metabolic process [GO:0018885]; positive regulation of cell proliferation [GO:0008284]; protein refolding [GO:0042026]; response to heat [GO:0009408]ATP binding [GO:0005524]; chaperone binding [GO:0051087]; metal ion binding [GO:0046872]; unfolded protein binding [GO:0051082] FUNCTION: Co-chaperone of Hsc70.O75794CD123'Cell division cycle protein 123 homologcell cycle arrest [GO:0007050]; cell division [GO:0051301]; positive regulation of cell proliferation [GO:0008284]; regulation of mitotic cell cycle [GO:0007346]FFUNCTION: Required for S phase entry of the cell cycle. {ECO:0000250}.Q9NRF8PYRG2CTP synthase 2Ede novo' CTP biosynthetic process [GO:0044210]; glutamine metabolic process [GO:0006541]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleotide metabolic process [GO:0006220]; small molecule metabolic process [GO:0044281]FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides. {ECO:0000269|PubMed:10899599, ECO:0000269|PubMed:16179339}.O95628CNOT4(CCR4-NOT transcription complex subunit 4gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; protein autoubiquitination [GO:0051865]ligase activity [GO:0016874]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; < ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: Has E3 ubiquitin ligase activity. Involved in activation of the JAK/STAT pathway. {ECO:0000269|PubMed:11823428, ECO:0000269|PubMed:22159038}.Q8NEU8DP13BDCC-interacting protein 13-betaESUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:15016378}; Peripheral membrane protein {ECO:0000269|PubMed:15016378}. Nucleus {ECO:0000269|PubMed:15016378}. Note=Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF.Zcell cycle [GO:0007049]; cell proliferation [GO:0008283]; signal transduction [GO:0007165]cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals mediated by an early endosomal compartment. Links Rab5 to nuclear signal transduction. {ECO:0000269|PubMed:15016378}.Q9UDT6CLIP2*CAP-Gly domain-containing linker protein 2tcytoplasmic microtubule [GO:0005881]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]-FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations (By similarity). {ECO:0000250}.Q9H7C9AAMDC Mth938 domain-containing proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Diffuse distribution with some highly concentrated spots around the nucleus. {ECO:0000250}.negative regulation of apoptotic process [GO:0043066]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]ZFUNCTION: May play a role in preadipocyte differentiation and adipogenesis. {ECO:0000250}.Q9Y6F6MRVI1 Protein MRVI1SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Sarcoplasmic reticulum {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.wblood coagulation [GO:0007596]; cGMP-mediated signaling [GO:0019934]; relaxation of vascular smooth muscle [GO:0060087]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; platelet dense tubular network membrane [GO:0031095]; sarcoplasmic reticulum [GO:0016529]8FUNCTION: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation. {ECO:0000269|PubMed:14729908}.P43490NAMPT&Nicotinamide phosphoribosyltransferaseSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24130902}. Cytoplasm {ECO:0000250|UniProtKB:Q99KQ4}. Secreted {ECO:0000269|PubMed:21741723}. Note=Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher concentrations compared to maternal serum. {ECO:0000269|PubMed:21741723, ECO:0000269|PubMed:24130902}.cell-cell signaling [GO:0007267]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; female pregnancy [GO:0007565]; NAD biosynthetic process [GO:0009435]; NAD metabolic process [GO:0019674]; nicotinamide metabolic process [GO:0006769]; positive regulation of cell proliferation [GO:0008284]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; response to organic cyclic compound [GO:0014070]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]cytokine activity [GO:0005125]; drug binding [GO:0008144]; nicotinamide phosphoribosyltransferase activity [GO:0047280]; nicotinate-nucleotide diphosphorylase (carboxylating) activity [GO:0004514]\FUNCTION: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity). {ECO:0000250|UniProtKB:Q99KQ4, ECO:0000269|PubMed:24130902}.Q92636FAN Protein FANceramide metabolic process [GO:0006672]; endosomal transport [GO:0016197]; intracellular signal transduction [GO:0035556]; signal transduction [GO:0007165]Sphospholipid binding [GO:0005543]; receptor signaling protein activity [GO:0005057]fcytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extrinsic component of membrane [GO:0019898]FUNCTION: Couples the p55 TNF-receptor (TNF-R55 / TNFR1) to neutral sphingomyelinase (N-SMASE). Specifically binds to the N-smase activation domain of TNF-R55. May regulate ceramide production by N-SMASE.O15040TCPR23Tectonin beta-propeller repeat-containing protein 2bFUNCTION: Probably plays a role as positive regulator of autophagy. {ECO:0000269|PubMed:23176824}.Q9BUK0CHCH7?Coiled-coil-helix-coiled-coil-helix domain-containing protein 7FSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000305}..mitochondrial intermembrane space [GO:0005758]Q6UWS5PT117%Protein PET117 homolog, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22356826}.P68400CSK21Casein kinase II subunit alpha<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24962073}.axon guidance [GO:0007411]; chaperone-mediated protein folding [GO:0061077]; mitotic cell cycle [GO:0000278]; mitotic spindle checkpoint [GO:0071174]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of cell growth [GO:0030307]; positive regulation of cell proliferation [GO:0008284]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of Wnt signaling pathway [GO:0030177]; protein phosphorylation [GO:0006468]; regulation of transcription, DNA-templated [GO:0006355]; rhythmic process [GO:0048511]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]ATP binding [GO:0005524]; Hsp90 protein binding [GO:0051879]; protein N-terminus binding [GO:0047485]; protein serine/threonine kinase activity [GO:0004674]~cytosol [GO:0005829]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; plasma membrane [GO:0005886]; Sin3 complex [GO:0016580] FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellul< ar response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073). {ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064, ECO:0000269|PubMed:19188443, ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:24962073}.P02765FETUAAlpha-2-HS-glycoproteinacute-phase response [GO:0006953]; negative regulation of bone mineralization [GO:0030502]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of phosphorylation [GO:0042326]; ossification [GO:0001503]; pinocytosis [GO:0006907]; positive regulation of phagocytosis [GO:0050766]; regulation of bone mineralization [GO:0030500]; regulation of inflammatory response [GO:0050727]; skeletal system development [GO:0001501]ccysteine-type endopeptidase inhibitor activity [GO:0004869]; kinase inhibitor activity [GO:0019210]FUNCTION: Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions.Q9UBX3DIC#Mitochondrial dicarboxylate carrier'Proximal tubule bicarbonate reclamationcarbohydrate metabolic process [GO:0005975]; cellular nitrogen compound metabolic process [GO:0034641]; dicarboxylic acid transport [GO:0006835]; gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]; ion transport [GO:0006811]; mitochondrial transport [GO:0006839]; small molecule metabolic process [GO:0044281]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]; sulfur amino acid catabolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]; transmembrane transport [GO:0055085]Adicarboxylic acid transmembrane transporter activity [GO:0005310]lintegral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; nucleus [GO:0005634]FUNCTION: Involved in translocation of malonate, malate and succinate in exchange for phosphate, sulfate, sulfite or thiosulfate across mitochondrial inner membrane.Q9BZI7REN3B$Regulator of nonsense transcripts 3B_SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttling between the nucleus and the cytoplasm.gene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of translation [GO:0045727]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]mRNA binding [GO:0003729]; nucleocytoplasmic transporter activity [GO:0005487]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]LFUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core. {ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:12718880, ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16601204, ECO:0000269|PubMed:18066079}.P63218GBG5AGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; G-protein coupled receptor signaling pathway [GO:0007186]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]fGTPase activity [GO:0003924]; PDZ domain binding [GO:0030165]; signal transducer activity [GO:0004871]extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q04726TLE3"Transducin-like enhancer protein 3Notch signaling pathway [GO:0007219]; organ morphogenesis [GO:0009887]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]CFUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits the transcriptional activation mediated by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES (By similarity). {ECO:0000250}.Q9HCE1MOV10Putative helicase MOV-10FSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16289642}.epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; mRNA cleavage involved in gene silencing by miRNA [GO:0035279]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; phosphatidylinositol-mediated signaling [GO:0048015]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]ecytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular space [GO:0005615]]FUNCTION: Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC. Also required for RNA-directed transcription and replication of the human hepatitis delta virus (HDV). Interacts with small capped HDV RNAs derived from genomic hairpin structures that mark the initiation sites of RNA-dependent HDV RNA transcription. {ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:18552826, ECO:0000269|PubMed:22791714}.Q8IUR7ARMC8%Armadillo repeat-containing protein 8Q9NSY0NRBP2"Nuclear receptor-binding protein 2negative regulation of macroautophagy [GO:0016242]; negative regulation of neuron apoptotic process [GO:0043524]; neuron differentiation [GO:0030182]hFUNCTION: May regulate apoptosis of neural progenitor cells during < their differentiation. {ECO:0000250}.Q9H4X1RGCCRegulator of cell cycle RGCCSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase.activation of protein kinase activity [GO:0032147]; cellular response to hypoxia [GO:0071456]; complement activation [GO:0006956]; fibroblast activation [GO:0072537]; mitotic cell cycle arrest [GO:0071850]; negative regulation of angiogenesis [GO:0016525]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cytokine secretion [GO:0050710]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of exit from mitosis [GO:0001100]; negative regulation of fibroblast growth factor production [GO:0090272]; negative regulation of mitotic cell cycle phase transition [GO:1901991]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of extracellular matrix constituent secretion [GO:0003331]; positive regulation of gene expression [GO:0010628]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]pprotein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; R-SMAD binding [GO:0070412]Ecentrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]FUNCTION: Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation. {ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:17146433, ECO:0000269|PubMed:19158077, ECO:0000269|PubMed:22163048}.O94901SUN1SUN domain-containing protein 1wSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}; Single-pass type II membrane protein {ECO:0000269|PubMed:12958361, ECO:0000269|PubMed:16445915, ECO:0000269|PubMed:17132086, ECO:0000269|PubMed:18845190, ECO:0000269|PubMed:19933576}.cytoskeletal anchoring at nuclear membrane [GO:0090286]; nuclear envelope organization [GO:0006998]; nuclear matrix anchoring at nuclear membrane [GO:0090292]; synapsis [GO:0007129]protein anchor [GO:0043495]acrosomal membrane [GO:0002080]; integral component of nuclear inner membrane [GO:0005639]; intracellular membrane-bounded organelle [GO:0043231]; LINC complex [GO:0034993]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]KFUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). {ECO:0000250}.Q96BR5COA7&Cytochrome c oxidase assembly factor 7VSUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:24333015}.{FUNCTION: Required for assembly of mitochondrial respiratory chain complex I and complex IV. {ECO:0000269|PubMed:24333015}.P08651NFICNuclear factor 1 C-type5DNA replication [GO:0006260]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription from RNA polymerase II promoter [GO:0006366]ydouble-stranded DNA binding [GO:0003690]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.Q9BUI4RPC3,DNA-directed RNA polymerase III subunit RPC35defense response to virus [GO:0051607]; gene expression [GO:0010467]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of type I interferon production [GO:0032481]; regulation of transcription from RNA polymerase III promoter [GO:0006359]; termination of RNA polymerase III transcription [GO:0006386]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription from RNA polymerase III promoter [GO:0006383]zcytosol [GO:0005829]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.Q9BPX5ARP5L8Actin-related protein 2/3 complex subunit 5-like proteinArp2/3 complex(7)5Arp2/3 complex-mediated actin nucleation [GO:0034314]|Arp2/3 protein complex [GO:0005885]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]FUNCTION: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.Q5SVZ6ZMYM1Zinc finger MYM-type protein 1O95478NSA2(Ribosome biogenesis protein NSA2 homol< ogTnucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). {ECO:0000250}.Q16878CDO1Cysteine dioxygenase type 1 Organosulfur biosynthesiscellular nitrogen compound metabolic process [GO:0034641]; cysteine metabolic process [GO:0006534]; inflammatory response [GO:0006954]; lactation [GO:0007595]; L-cysteine catabolic process [GO:0019448]; oxidation-reduction process [GO:0055114]; response to amino acid [GO:0043200]; response to cAMP [GO:0051591]; response to ethanol [GO:0045471]; response to glucagon [GO:0033762]; response to glucocorticoid [GO:0051384]; small molecule metabolic process [GO:0044281]; sulfur amino acid biosynthetic process [GO:0000097]; sulfur amino acid catabolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]; taurine biosynthetic process [GO:0042412]Mcysteine dioxygenase activity [GO:0017172]; ferrous iron binding [GO:0008198]KFUNCTION: Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.Q08426ECHPPeroxisomal bifunctional enzyme\fatty acid beta-oxidation [GO:0006635]; internal protein amino acid acetylation [GO:0006475]3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; dodecenoyl-CoA delta-isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; enzyme binding [GO:0019899]; receptor binding [GO:0005102]Icytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]Q96BP3PPWD1BPeptidylprolyl isomerase domain and WD repeat-containing protein 1iSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18397323}. Note=Associated with spliceosomal complexes.Ycatalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Putative peptidylprolyl isomerase (PPIase). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.Q969X6CIR1ACirhindSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16225863}.maturation of SSU-rRNA [GO:0030490]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]FUNCTION: May be a transcriptional regulator. Acts as a positive regulator of HIVEP1 which specifically binds to the DNA sequence 5'-GGGACTTTCC-3' found in enhancer elements of numerous viral promoters such as those of HIV-1, SV40, or CMV. Ribosome biogenesis factor involved in small subunit (SSU) pre-rRNA processing at sites A', A0, 1 and 2b. {ECO:0000269|PubMed:19732766, ECO:0000269|PubMed:22916032}.P52657T2AG-Transcription initiation factor IIA subunit 2gene expression [GO:0010467]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; RNA polymerase II transcriptional preinitiation complex assembly [GO:0051123]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; TBP-class protein binding [GO:0017025]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]ecell junction [GO:0030054]; nucleoplasm [GO:0005654]; transcription factor TFIIA complex [GO:0005672]FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity. {ECO:0000269|PubMed:11030333}.Q99747SNAG$Gamma-soluble NSF attachment proteinintracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane fusion [GO:0061025]; protein complex assembly [GO:0006461]; protein stabilization [GO:0050821]Ssoluble NSF attachment protein activity [GO:0005483]; syntaxin binding [GO:0019905]extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; SNARE complex [GO:0031201]eFUNCTION: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.O95563MPC2 Mitochondrial pyruvate carrier 2SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:22628558}; Multi-pass membrane protein {ECO:0000269|PubMed:22628558}.cellular metabolic process [GO:0044237]; mitochondrial pyruvate transport [GO:0006850]; pyruvate metabolic process [GO:0006090]; small molecule metabolic process [GO:0044281]8pyruvate transmembrane transporter activity [GO:0050833][FUNCTION: Mediates the uptake of pyruvate into mitochondria. {ECO:0000269|PubMed:22628558}.O75688PPM1BProtein phosphatase 1BSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750}. Membrane {ECO:0000250}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250}.cytokine-mediated signaling pathway [GO:0019221]; negative regulation of defense response to virus [GO:0050687]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of NF-kappaB import into nucleus [GO:0042347]; N-terminal protein myristoylation [GO:0006499]; peptidyl-threonine dephosphorylation [GO:0035970]; protein dephosphorylation [GO:0006470]magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein serine/threonine phosphatase activity [GO:0004722]FUNCTION: Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:18930133, ECO:0000269|PubMed:22750291}.Q6PIJ6FBX38F-box only protein 38FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. May coactivate KLF7, but does not seem to promote KLF7 ubiquitination (By similarity). {ECO:0000250}.Q13889TF2H3*General transcription factor IIH subunit 37-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; phosphorylation of RNA polymerase II C-terminal domain [GO:0070816]; positive regulation of viral transcription [GO:0050434]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; translation [GO:0006412]; viral process [GO:0016032]damaged DNA binding [GO:0003684]; metal ion binding [GO:0046872]; protein N-terminus binding [GO:0047485]; sequence-specific DNA binding transcription factor activity [GO:0003700]; translation factor activity, RNA binding [GO:0008135]FUNCTION: Component of the core-TFIIH basal transcription factor< involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Anchors XPB.Q9UJY4GGA2,ADP-ribosylation factor-binding protein GGA2 SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15039775}; Peripheral membrane protein {ECO:0000269|PubMed:15039775}. Endosome membrane {ECO:0000269|PubMed:15039775}; Peripheral membrane protein {ECO:0000269|PubMed:15039775}.,ADP-ribosylation factor binding [GO:0030306]clathrin adaptor complex [GO:0030131]; clathrin-coated vesicle [GO:0030136]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; trans-Golgi network [GO:0005802]#FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.Q9Y2J4AMOL2Angiomotin-like protein 27SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}.@hippo signaling [GO:0035329]; Wnt signaling pathway [GO:0016055]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; recycling endosome [GO:0055037]?FUNCTION: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC. {ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:21937427, ECO:0000269|PubMed:22362771}.O95999BCL10B-cell lymphoma/leukemia 106SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Appears to have a perinuclear, compact and filamentous pattern of expression. Also found in the nucleus of several types of tumor cells. Colocalized with DPP4 in membrane rafts.adaptive immune response [GO:0002250]; B cell apoptotic process [GO:0001783]; cell death [GO:0008219]; cellular defense response [GO:0006968]; cellular response to mechanical stimulus [GO:0071260]; Fc-epsilon receptor signaling pathway [GO:0038095]; immunoglobulin mediated immune response [GO:0016064]; innate immune response [GO:0045087]; interleukin-6 biosynthetic process [GO:0042226]; lymphotoxin A biosynthetic process [GO:0042109]; negative regulation of mature B cell apoptotic process [GO:0002906]; neural tube closure [GO:0001843]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-8 biosynthetic process [GO:0045416]; positive regulation of mast cell cytokine production [GO:0032765]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of T cell activation [GO:0050870]; positive regulation of transcription, DNA-templated [GO:0045893]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein oligomerization [GO:0051259]; regulation of T cell receptor signaling pathway [GO:0050856]; response to food [GO:0032094]; response to fungus [GO:0009620]; response to molecule of bacterial origin [GO:0002237]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell apoptotic process [GO:0070231]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor signaling pathway [GO:0002224]enzyme binding [GO:0019899]; kinase binding [GO:0019900]; NF-kappaB binding [GO:0051059]; protease binding [GO:0002020]; protein C-terminus binding [GO:0008022]; protein kinase B binding [GO:0043422]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]CCBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]pFUNCTION: Involved in adaptive immune response (PubMed:25365219). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK. May be an adapter protein between upstream TNFR1-TRADD-RIP complex and the downstream NIK-IKK-IKAP complex. Is a substrate for MALT1 (PubMed:18264101). {ECO:0000269|PubMed:18264101, ECO:0000269|PubMed:25365219}.Q92889XPFDNA repair endonuclease XPFcellular response to UV [GO:0034644]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; negative regulation of telomere maintenance [GO:0032205]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA incision [GO:0033683]; nucleotide-excision repair, DNA incision, 3'-to lesion [GO:0006295]; nucleotide-excision repair, DNA incision, 5'-to lesion [GO:0006296]; nucleotide-excision repair involved in interstrand cross-link repair [GO:1901255]; resolution of meiotic recombination intermediates [GO:0000712]; response to UV [GO:0009411]; telomere maintenance [GO:0000723]; transcription-coupled nucleotide-excision repair [GO:0006283]; UV protection [GO:0009650] damaged DNA binding [GO:0003684]; endodeoxyribonuclease activity [GO:0004520]; protein C-terminus binding [GO:0008022]; protein N-terminus binding [GO:0047485]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]Jchromosome, telomeric region [GO:0000781]; ERCC4-ERCC1 complex [GO:0070522]; nuclear chromosome, telomeric region [GO:0000784]; nucleoplasm [GO:0005654]; nucleotide-excision repair complex [GO:0000109]; nucleotide-excision repair factor 1 complex [GO:0000110]; nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669]FUNCTION: Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link. {ECO:0000269|PubMed:19596235}.Q04756HGFA"Hepatocyte growth factor activatorSUBCELLULAR LOCATION: Secreted. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.\serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]pFUNCTION: Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form.P35222CTNB1Catenin beta-1fSUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:24342833}. Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell junction. Cell membrane {ECO:0000269|PubMed:24342833}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (By similarity). Cytoplasmic when it is unstabilized (high level of phosphorylation) or bound to CDH1. Translocates to the nucleus when it is stabilized (low level of phosphorylation). Interaction with GLIS2 and MUC1 promotes nuclear translocation. Interaction with EMD inhibits nuclear localization. The majority of beta-catenin is localized to the cell membrane. In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250. In mitosis, when NEK2 activity increases, it localizes to centrosome< s at spindle poles independent of CROCC. Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells. {ECO:0000250}.padherens junction assembly [GO:0034333]; androgen receptor signaling pathway [GO:0030521]; anterior/posterior axis specification [GO:0009948]; apoptotic process [GO:0006915]; bone resorption [GO:0045453]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in negative regulation of apoptotic process [GO:0044336]; canonical Wnt signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation [GO:0061324]; canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition [GO:0044334]; cell adhesion [GO:0007155]; cell fate specification [GO:0001708]; cell-matrix adhesion [GO:0007160]; cell maturation [GO:0048469]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular response to growth factor stimulus [GO:0071363]; cellular response to indole-3-methanol [GO:0071681]; central nervous system vasculogenesis [GO:0022009]; chromatin-mediated maintenance of transcription [GO:0048096]; dorsal/ventral axis specification [GO:0009950]; ectoderm development [GO:0007398]; embryonic axis specification [GO:0000578]; embryonic digit morphogenesis [GO:0042733]; embryonic foregut morphogenesis [GO:0048617]; embryonic forelimb morphogenesis [GO:0035115]; embryonic heart tube development [GO:0035050]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal limb joint morphogenesis [GO:0036023]; endodermal cell fate commitment [GO:0001711]; endothelial tube morphogenesis [GO:0061154]; epithelial cell differentiation involved in prostate gland development [GO:0060742]; epithelial to mesenchymal transition [GO:0001837]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; fungiform papilla formation [GO:0061198]; gastrulation with mouth forming second [GO:0001702]; genitalia morphogenesis [GO:0035112]; glial cell fate determination [GO:0007403]; hair cell differentiation [GO:0035315]; hair follicle morphogenesis [GO:0031069]; hair follicle placode formation [GO:0060789]; innate immune response [GO:0045087]; in utero embryonic development [GO:0001701]; layer formation in cerebral cortex [GO:0021819]; lens morphogenesis in camera-type eye [GO:0002089]; lung-associated mesenchyme development [GO:0060484]; lung cell differentiation [GO:0060479]; lung induction [GO:0060492]; male genitalia development [GO:0030539]; mesenchymal cell proliferation involved in lung development [GO:0060916]; mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003337]; muscle cell differentiation [GO:0042692]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of cell proliferation [GO:0008285]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of mitotic cell cycle, embryonic [GO:0045976]; negative regulation of neuron death [GO:1901215]; negative regulation of oligodendrocyte differentiation [GO:0048715]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nephron tubule formation [GO:0072079]; neural plate development [GO:0001840]; neuron migration [GO:0001764]; odontogenesis of dentin-containing tooth [GO:0042475]; oocyte development [GO:0048599]; osteoclast differentiation [GO:0030316]; oviduct development [GO:0060066]; pancreas development [GO:0031016]; patterning of blood vessels [GO:0001569]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of determination of dorsal identity [GO:2000017]; positive regulation of DNA-templated transcription, initiation [GO:2000144]; positive regulation of endothelial cell differentiation [GO:0045603]; positive regulation of epithelial cell proliferation involved in prostate gland development [GO:0060769]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of heparan sulfate proteoglycan biosynthetic process [GO:0010909]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere maintenance via telomerase [GO:0032212]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; programmed cell death [GO:0012501]; protein localization to cell surface [GO:0034394]; proximal/distal pattern formation [GO:0009954]; regulation of angiogenesis [GO:0045765]; regulation of calcium ion import [GO:0090279]; regulation of cell fate specification [GO:0042659]; regulation of centriole-centriole cohesion [GO:0030997]; regulation of centromeric sister chromatid cohesion [GO:0070602]; regulation of fibroblast proliferation [GO:0048145]; regulation of myelination [GO:0031641]; regulation of nephron tubule epithelial cell differentiation [GO:0072182]; regulation of protein localization to cell surface [GO:2000008]; regulation of secondary heart field cardioblast proliferation [GO:0003266]; regulation of smooth muscle cell proliferation [GO:0048660]; regulation of T cell proliferation [GO:0042129]; renal inner medulla development [GO:0072053]; renal outer medulla development [GO:0072054]; renal vesicle formation [GO:0072033]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; single organismal cell-cell adhesion [GO:0016337]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle cell differentiation [GO:0051145]; stem cell maintenance [GO:0019827]; sympathetic ganglion development [GO:0061549]; synapse organization [GO:0050808]; synaptic transmission [GO:0007268]; synaptic vesicle transport [GO:0048489]; T cell differentiation in thymus [GO:0033077]; thymus development [GO:0048538]; trachea formation [GO:0060440]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]aalpha-catenin binding [GO:0045294]; androgen receptor binding [GO:0050681]; cadherin binding [GO:0045296]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; estrogen receptor binding [GO:0030331]; euchromatin binding [GO:1990188]; ion channel binding [GO:0044325]; I-SMAD binding [GO:0070411]; kinase binding [GO:0019900]; nuclear hormone receptor binding [GO:0035257]; protein C-terminus binding [GO:0008022]; protein phosphatase binding [GO:0019903]; RNA polymerase II activating transcription factor binding [GO:0001102]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]; SMAD binding [GO:0046332]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]badherens junction [GO:0005912]; apical part of cell [GO:0045177]; basolateral plasma membrane [GO:0016323]; beta-catenin destruction complex [GO:0030877]; beta-catenin-TCF7L2 complex [GO:0070369]; bicellular tight junction [GO:0005923]; catenin complex [GO:0016342]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cell cortex [GO:0005938]; cell junction [GO:0030054]; ce< ll periphery [GO:0071944]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microvillus membrane [GO:0031528]; nuclear euchromatin [GO:0005719]; nuclear transcription factor complex [GO:0044798]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; protein-DNA complex [GO:0032993]; Scrib-APC-beta-catenin complex [GO:0034750]; spindle pole [GO:0000922]; transcription factor complex [GO:0005667]; Z disc [GO:0030018]FUNCTION: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22647378, PubMed:22699938, PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18957423, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22699938}.Q9NRY6PLS3Phospholipid scramblase 3SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:17226776}; Single-pass type II membrane protein {ECO:0000269|PubMed:17226776}.apoptotic process [GO:0006915]; cellular response to lipopolysaccharide [GO:0071222]; cholesterol homeostasis [GO:0042632]; glucose homeostasis [GO:0042593]; phospholipid scrambling [GO:0017121]calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; phospholipid scramblase activity [GO:0017128]nintegral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]qFUNCTION: May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. Seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages. {ECO:0000269|PubMed:17226776}.P02788TRFLLactotransferrinSUBCELLULAR LOCATION: Isoform 1: Secreted. Cytoplasmic granule. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils.; SUBCELLULAR LOCATION: Isoform DeltaLf: Cytoplasm. Nucleus. Note=Mainly localized in the cytoplasm.antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; bone morphogenesis [GO:0060349]; humoral immune response [GO:0006959]; innate immune response in mucosa [GO:0002227]; interaction with host [GO:0051701]; ion transport [GO:0006811]; iron assimilation by chelation and transport [GO:0033214]; negative regulation by host of viral process [GO:0044793]; negative regulation of apoptotic process [GO:0043066]; negative regulation of ATPase activity [GO:0032780]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of osteoclast development [GO:2001205]; negative regulation of single-species biofilm formation in or on host organism [GO:1900229]; negative regulation of tumor necrosis factor (ligand) superfamily member 11 production [GO:2000308]; negative regulation of viral genome replication [GO:0045071]; negative regulation of viral process [GO:0048525]; ossification [GO:0001503]; phagosome maturation [GO:0090382]; positive regulation of bone mineralization involved in bone maturation [GO:1900159]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of toll-like receptor 4 signaling pathway [GO:0034145]; regulation of cytokine production [GO:0001817]; regulation of tumor necrosis factor production [GO:0032680]; response to host immune response [GO:0052572]; retina homeostasis [GO:0001895]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; heparin binding [GO:0008201]; iron ion binding [GO:0005506]; protein serine/threonine kinase activator activity [GO:0043539]; serine-type endopeptidase activity [GO:0004252]4cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; phagocytic vesicle lumen [GO:0097013]; protein complex [GO:0043234]; secretory granule [GO:0030141]; specific granule [GO:0042581] FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.; FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.; FUNCTION: Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal memb< ranes.; FUNCTION: Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.; FUNCTION: Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.Q96S97MYADM)Myeloid-associated differentiation markerKestablishment of endothelial barrier [GO:0061028]; membrane raft organization [GO:0031579]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of gene expression [GO:0010629]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of protein kinase C signaling [GO:0090038]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of cell migration [GO:0030335]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein targeting to plasma membrane [GO:0072661]cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; ruffle [GO:0001726]O75319DUS11)RNA/RNP complex-1-interacting phosphataseiSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9685386}. Nucleus speckle {ECO:0000269|PubMed:9685386}.peptidyl-tyrosine dephosphorylation [GO:0035335]; polynucleotide 5' dephosphorylation [GO:0098507]; RNA metabolic process [GO:0016070]; RNA processing [GO:0006396]Unucleotide phosphatase activity, acting on free nucleotides [GO:0098519]; phosphatase activity [GO:0016791]; poly(A) RNA binding [GO:0044822]; polynucleotide 5'-phosphatase activity [GO:0004651]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]vFUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism. {ECO:0000269|PubMed:10347225, ECO:0000269|PubMed:24447265, ECO:0000269|PubMed:9685386}.Q9BRQ8AIFM2Apoptosis-inducing factor 2>SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane.capoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]DNA binding [GO:0003677]; electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]FUNCTION: Oxidoreductase, which may play a role in mediating a p53/TP53-dependent apoptosis response. Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death. Binds to DNA in a sequence-independent manner. May contribute to genotoxin-induced growth arrest. {ECO:0000269|PubMed:11980907, ECO:0000269|PubMed:12135761, ECO:0000269|PubMed:15958387}.A6NKF1SAC31 SAC3 domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes on centrosomes in interphase cells and at spindles in mitosis. {ECO:0000250}.Xcytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; spindle [GO:0005819]TFUNCTION: Involved in centrosome duplication and mitotic progression. {ECO:0000250}.Q96BI3APH1AGamma-secretase subunit APH-1ASUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Note=Predominantly located in the endoplasmic reticulum and in the cis-Golgi.bamyloid precursor protein catabolic process [GO:0042987]; apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; membrane protein ectodomain proteolysis [GO:0006509]; membrane protein intracellular domain proteolysis [GO:0031293]; metanephros development [GO:0001656]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. {ECO:0000269|PubMed:12297508, ECO:0000269|PubMed:12522139, ECO:0000269|PubMed:12763021}.A1L390PKHG37Pleckstrin homology domain-containing family G member 3:regulation of Rho protein signal transduction [GO:0035023]Q8N612F16A2 FTS and Hook-interacting proteinearly endosome to late endosome transport [GO:0045022]; endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; lysosome organization [GO:0007040]; protein transport [GO:0015031]FHF complex [GO:0070695]FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). {ECO:0000269|PubMed:18799622}.P13861KAP2>cAMP-dependent protein kinase type II-alpha regulatory subunitSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane.4activation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; blood coagulation [GO:0007596]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of insulin secretion [GO:0050796]; renal water homeostasis [GO:0003091]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; water transport [GO:0006833]`AMP-activated protein kinase complex [GO:0031588]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.O14772FPGT&Fucose-1-phosphate guanylyltransferase%fucose metabolic process [GO:0006004]wcatalytic activity [GO:0003824]; fucose-1-phosphate guanylyltransferase activity [GO:0047341]; GTP bin< ding [GO:0005525]FUNCTION: Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids.Q15528MED226Mediator of RNA polymerase II transcription subunit 225cytoplasm [GO:0005737]; mediator complex [GO:0016592]Q9Y3A3PHOCNMOB-like protein phoceinSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234}; Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a perinuclear punctate pattern. Associated with membranes and the Golgi stacks.cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]mFUNCTION: May play a role in membrane trafficking, specifically in membrane budding reactions. {ECO:0000250}.Q9NZ01TECR#Very-long-chain enoyl-CoA reductase+cellular lipid metabolic process [GO:0044255]; fatty acid elongation [GO:0030497]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]; very long-chain fatty acid biosynthetic process [GO:0042761]Ioxidoreductase activity, acting on the CH-CH group of donors [GO:0016627]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; nucleus [GO:0005634]oFUNCTION: Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:12482854}.O95070YIF1A Protein YIF1ASUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Cycles between the endoplasmic reticulum and the endoplasmic reticulum-Golgi intermediate compartment.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]9endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; microtubule organizing center [GO:0005815]lFUNCTION: Possible role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:15990086}.Q3L8U1CHD9+Chromodomain-helicase-DNA-binding protein 9eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16095617}. Nucleus {ECO:0000269|PubMed:16095617}.cellular lipid metabolic process [GO:0044255]; chromatin modification [GO:0016568]; regulation of transcription, DNA-templated [GO:0006355]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]FUNCTION: Acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. Proposed to be a ATP-dependent chromatin remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-rich DNA. Associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis (By similarity). {ECO:0000250}.Q02809PLOD11Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1ccellular protein modification process [GO:0006464]; cellular response to hormone stimulus [GO:0032870]; epidermis development [GO:0008544]; extracellular matrix organization [GO:0030198]; hydroxylysine biosynthetic process [GO:0046947]; oxidation-reduction process [GO:0055114]; peptidyl-lysine hydroxylation [GO:0017185]; response to hypoxia [GO:0001666]ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; peptide binding [GO:0042277]; procollagen-lysine 5-dioxygenase activity [GO:0008475]; protein homodimerization activity [GO:0042803]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; rough endoplasmic reticulum membrane [GO:0030867]Q5JSL3DOC11#Dedicator of cytokinesis protein 11Vblood coagulation [GO:0007596]; small GTPase mediated signal transduction [GO:0007264]|FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. {ECO:0000250}.Q9H6Y2WDR55WD repeat-containing protein 55PSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}.qribosomal large subunit biogenesis [GO:0042273]; RNA metabolic process [GO:0016070]; rRNA processing [GO:0006364]FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity). {ECO:0000250}.O14618CCS)Copper chaperone for superoxide dismutase=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9726962}.'copper ion transmembrane transport [GO:0035434]; intracellular copper ion transport [GO:0015680]; positive regulation of oxidoreductase activity [GO:0051353]; removal of superoxide radicals [GO:0019430]; response to reactive oxygen species [GO:0000302]; superoxide metabolic process [GO:0006801]copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; protein disulfide oxidoreductase activity [GO:0015035]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270]EFUNCTION: Delivers copper to copper zinc superoxide dismutase (SOD1).Q6PD62CTR9.RNA polymerase-associated protein CTR9 homolog[SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Note=Found in speckles. {ECO:0000250}.blastocyst growth [GO:0001832]; cellular response to lipopolysaccharide [GO:0071222]; endodermal cell fate commitment [GO:0001711]; histone H2B ubiquitination [GO:0033523]; histone H3-K4 trimethylation [GO:0080182]; histone monoubiquitination [GO:0010390]; inner cell mass cell differentiation [GO:0001826]; interleukin-6-mediated signaling pathway [GO:0070102]; JAK-STAT cascade [GO:0007259]; negative regulation of mRNA polyadenylation [GO:1900364]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of histone H2B ubiquitination [GO:2001168]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of histone H3-K79 methylation [GO:2001162]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of genetic imprinting [GO:2000653]; stem cell maintenance [GO:0019827]; transcription, DNA-templated [GO:0006351]; trophectodermal cell differentiation [GO:0001829]; Wnt signaling pathway [GO:0016055]lCdc73/Paf1 complex [GO:0016593]; nuclear speck [GO:0016607]; transcriptionally active chromatin [GO:0035327]FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. < PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity). {ECO:0000250}.P33240CSTF2%Cleavage stimulation factor subunit 2iSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11598190}. Note=Localized with DDX1 in cleavage bodies.cleavage body [GO:0071920]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}.Q8N3Z3GTPB8GTP-binding protein 8$barrier septum assembly [GO:0000917]Q9UBS9SUCO)SUN domain-containing ossification factor|SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.multicellular organismal development [GO:0007275]; ossification [GO:0001503]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of bone remodeling [GO:0046850]integral component of membrane [GO:0016021]; membrane [GO:0016020]; rough endoplasmic reticulum [GO:0005791]; rough endoplasmic reticulum membrane [GO:0030867]FUNCTION: Required for bone modeling during late embryogenesis. Regulates type I collagen synthesis in osteoblasts during their postnatal maturation (By similarity). {ECO:0000250}.Q9UBI6GBG12BGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12icellular response to glucagon stimulus [GO:0071377]; cerebral cortex development [GO:0021987]; energy reserve metabolic process [GO:0006112]; G-protein coupled receptor signaling pathway [GO:0007186]; response to lipopolysaccharide [GO:0032496]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]lPDZ domain binding [GO:0030165]; phosphate ion binding [GO:0042301]; signal transducer activity [GO:0004871]actin filament [GO:0005884]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886]Q96LR5UB2E2"Ubiquitin-conjugating enzyme E2 E28cellular response to DNA damage stimulus [GO:0006974]; ISG15-protein conjugation [GO:0032020]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; protein K11-linked ubiquitination [GO:0070979]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]VFUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein. {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20133869, ECO:0000269|PubMed:9371400}.Q9NVA4T184CTransmembrane protein 184ChFUNCTION: Possible tumor suppressor which may play a role in cell growth. {ECO:0000269|PubMed:17072649}.Q9P2P5HECW2!E3 ubiquitin-protein ligase HECW2]protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of TP73. Acts to stabilize TP73 and enhance activation of transcription by TP73. {ECO:0000269|PubMed:12890487}.Q14644RASA3Ras GTPase-activating protein 3$SUBCELLULAR LOCATION: Cell membrane.calcium ion transmembrane transport [GO:0070588]; intracellular signal transduction [GO:0035556]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]ucalcium-release channel activity [GO:0015278]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.Q8NHV4NEDD1 Protein NEDD1wSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19029337}.cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; organelle organization [GO:0006996]apical part of cell [GO:0045177]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; pericentriolar material [GO:0000242]; plasma membrane [GO:0005886]; spindle pole [GO:0000922]FUNCTION: Required for mitosis progression. Promotes the nucleation of microtubules from the spindle. {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19509060}.Q5JTV8TOIP1Torsin-1A-interacting protein 1SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647}; Single-pass membrane protein {ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647}.nuclear membrane organization [GO:0071763]; positive regulation of ATPase activity [GO:0032781]; protein localization to nucleus [GO:0034504]nATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; cytoskeletal protein binding [GO:0008092]fintegral component of membrane [GO:0016021]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634]FUNCTION: Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina. {ECO:0000269|PubMed:23569223}.P14868SYDC#Aspartate--tRNA ligase, cytoplasmicaspartyl-tRNA aminoacylation [GO:0006422]; gene expression [GO:0010467]; protein complex assembly [GO:0006461]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418]aminoacylase activity [GO:0004046]; aspartate-tRNA ligase activity [GO:0004815]; ATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.Q9NSC5HOME3Homer protein homolog 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}.G-protein coupled glutamate receptor signaling pathway [GO:0007216]; protein targeting [GO:0006605]; regulation of store-operated calcium entry [GO:2001256]basal part of cell [GO:0045178]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal postsyn< aptic density [GO:0097481]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.Q13363CTBP1C-terminal-binding protein 1eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12679040}. Nucleus {ECO:0000269|PubMed:12679040}.negative regulation of cell proliferation [GO:0008285]; negative regulation of histone acetylation [GO:0035067]; negative regulation of histone H4 acetylation [GO:0090241]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transcription from RNA polymerase II promoter by histone modification [GO:1903758]; positive regulation of histone deacetylation [GO:0031065]; protein phosphorylation [GO:0006468]; regulation of cell cycle [GO:0051726]; transcription, DNA-templated [GO:0006351]; viral genome replication [GO:0019079]; white fat cell differentiation [GO:0050872]NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; protein C-terminus binding [GO:0008022]; protein domain specific binding [GO:0019904]; repressing transcription factor binding [GO:0070491]; RNA polymerase II transcription corepressor activity [GO:0001106]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]; transcription factor complex [GO:0005667]FUNCTION: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. {ECO:0000269|PubMed:12419229, ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:9858600}.Q9NRR5UBQL4 Ubiquilin-4SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11001934, ECO:0000269|PubMed:15280365}. Cytoplasm {ECO:0000269|PubMed:15280365}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99NB8}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:23459205}. Note=Colocalizes with the proteasome, both in nucleus and cytoplasm. {ECO:0000269|PubMed:15280365}.autophagy [GO:0006914]; negative regulation of autophagosome fusion [GO:1902453]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]Jidentical protein binding [GO:0042802]; polyubiquitin binding [GO:0031593]autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]VFUNCTION: Plays a role in the regulation of protein degradation via the ubiquitin-proteasome system (UPS). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (Ref. 6). Plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity). Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery. Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C) and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:23459205). {ECO:0000250|UniProtKB:Q99NB8, ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:23459205}.Q96IG2FXL20F-box/LRR-repeat protein 20behavioral fear response [GO:0001662]; protein ubiquitination [GO:0016567]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]Acytoplasm [GO:0005737]; SCF ubiquitin ligase complex [GO:0019005]FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Role in neural transmission (By similarity). {ECO:0000250}.P16219ACADS:Short-chain specific acyl-CoA dehydrogenase, mitochondrialbutyrate catabolic process [GO:0046359]; cellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]; protein homotetramerization [GO:0051289]; response to glucocorticoid [GO:0051384]; response to starvation [GO:0042594]; small molecule metabolic process [GO:0044281]acyl-CoA dehydrogenase activity [GO:0003995]; butyryl-CoA dehydrogenase activity [GO:0004085]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]Q9UBC1IKBL1#NF-kappa-B inhibitor-like protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829348}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with CACTIN in the nucleus.cellular response to lipopolysaccharide [GO:0071222]; cytoplasmic sequestering of transcription factor [GO:0042994]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; negative regulation of tumor necrosis factor production [GO:0032720]ucytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]]FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli. {ECO:0000269|PubMed:20829348}.Q9BRT6LLPHProtein LLP homologQ9Y5A9YTHD2&YTH domain-containing family protein 2FSUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:24284625}.Ohumoral immune response [GO:0006959]; regulation of mRNA stability [GO:0043488]FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (PubMed:24284625, PubMed:26046440). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:22575960, PubMed:24284625, PubMed:25412658, PubMed:25412661). Acts as a regulator of mRNA stability: binding to m6A-containing mRNAs results in the localization to mRNA decay sites, such as processing bodies (P-bodies), leading to mRNA degradation (PubMed:24284625, PubMed:26046440). {ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25412658, ECO:0000269|PubMed:25412661, ECO:0000269|PubMed:26046440}.O43491E41L2Band 4.1-like protein 2iSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22361696}.5cortical actin cytoskeleton organization [GO:0030866]cell junction [GO:0030054]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spectrin [GO:0008091]Q01780EXOSXExosome component 10SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus. Note=Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence of a nucleolar RNA exosome complex form.< ECUT catabolic process [GO:0071034]; dosage compensation by inactivation of X chromosome [GO:0009048]; histone mRNA catabolic process [GO:0071044]; maturation of 5.8S rRNA [GO:0000460]; nuclear mRNA surveillance [GO:0071028]; nuclear polyadenylation-dependent rRNA catabolic process [GO:0071035]; nuclear retention of unspliced pre-mRNA at the site of transcription [GO:0071048]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]3'-5' exonuclease activity [GO:0008408]; exoribonuclease activity [GO:0004532]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; exosome (RNase complex) [GO:0000178]; membrane [GO:0016020]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327];FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 has 3'-5' exonuclease activity (By similarity). EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of SKIV2L2, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA. {ECO:0000250, ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273}.P05783K1C18Keratin, type I cytoskeletal 18HSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus, nucleolus.anatomical structure morphogenesis [GO:0009653]; cell cycle [GO:0007049]; extrinsic apoptotic signaling pathway [GO:0097191]; Golgi to plasma membrane CFTR protein transport [GO:0043000]; hepatocyte apoptotic process [GO:0097284]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of apoptotic process [GO:0043066]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; viral process [GO:0016032]rpoly(A) RNA binding [GO:0044822]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]/cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0000250, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.P00491PNPHPurine nucleoside phosphorylaseeSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22509282}.immune response [GO:0006955]; inosine catabolic process [GO:0006148]; interleukin-2 secretion [GO:0070970]; NAD biosynthesis via nicotinamide riboside salvage pathway [GO:0034356]; nicotinamide riboside catabolic process [GO:0006738]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of T cell proliferation [GO:0042102]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide catabolic process [GO:0006195]; response to drug [GO:0042493]; small molecule metabolic process [GO:0044281]; urate biosynthetic process [GO:0034418]drug binding [GO:0008144]; nucleoside binding [GO:0001882]; phosphate ion binding [GO:0042301]; purine nucleobase binding [GO:0002060]; purine-nucleoside phosphorylase activity [GO:0004731]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; nucleus [GO:0005634] FUNCTION: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. {ECO:0000269|PubMed:2104852}.Q8WVR3CG043Uncharacterized protein C7orf43P26006ITA3Integrin alpha-3oSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15611341}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15611341}; Lipid-anchor {ECO:0000269|PubMed:15611341}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. {ECO:0000269|PubMed:10455171}.)blood coagulation [GO:0007596]; cell-matrix adhesion [GO:0007160]; dendritic spine maintenance [GO:0097062]; exploration behavior [GO:0035640]; extracellular matrix organization [GO:0030198]; heart development [GO:0007507]; integrin-mediated signaling pathway [GO:0007229]; leukocyte migration [GO:0050900]; lung development [GO:0030324]; maternal process involved in female pregnancy [GO:0060135]; memory [GO:0007613]; mesodermal cell differentiation [GO:0048333]; negative regulation of cell projection organization [GO:0031345]; negative regulation of Rho protein signal transduction [GO:0035024]; nephron development [GO:0072006]; neuron migration [GO:0001764]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron projection development [GO:0010976]; regulation of BMP signaling pathway [GO:0030510]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulation of Wnt signaling pathway [GO:0030111]; renal filtration [GO:0097205]; response to drug [GO:0042493]; response to gonadotropin [GO:0034698]; skin development [GO:0043588]glycoprotein binding [GO:0001948]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]'basolateral plasma membrane [GO:0016323]; cell periphery [GO:0071944]; cell surface [GO:0009986]; excitatory synapse [GO:0060076]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; integrin alpha3-beta1 complex [GO:0034667]; integrin complex [GO:0008305]; invadopodium me< mbrane [GO:0071438]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synaptic membrane [GO:0097060]FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:15181153}.Q9BZM5N2DL2NKG2D ligand 2HSUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted.antigen processing and presentation [GO:0019882]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]oanchored component of plasma membrane [GO:0046658]; cell surface [GO:0009986]; extracellular space [GO:0005615]FUNCTION: Ligand for the KLRK1/NKG2D receptor, together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to KLRK1/NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, interacts with soluble CMV glycoprotein UL16. The interaction with UL16 blocked the interaction with the KLRK1/NKG2D receptor, providing a mechanism by which CMV infected cells might escape the immune system. UL16 also causes ULBP2 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. {ECO:0000269|PubMed:11777960}.Q9Y2Q5LTOR2!Ragulator complex protein LAMTOR2SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.activation of MAPKK activity [GO:0000186]; cell growth [GO:0016049]; cellular protein localization [GO:0034613]; cellular response to amino acid stimulus [GO:0071230]; positive regulation of GTPase activity [GO:0043547]; positive regulation of TOR signaling [GO:0032008]extracellular exosome [GO:0070062]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; Ragulator complex [GO:0071986]FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980}.Q96Q83ALKB38Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3cell proliferation [GO:0008283]; DNA dealkylation involved in DNA repair [GO:0006307]; DNA repair [GO:0006281]; oxidative single-stranded DNA demethylation [GO:0035552]cytosine C-5 DNA demethylase activity [GO:0051747]; DNA-N1-methyladenine dioxygenase activity [GO:0043734]; ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]bcytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]2FUNCTION: Dioxygenase that repairs alkylated DNA containing 1-methyladenine (1meA) and 3-methylcytosine (3meC) by oxidative demethylation. Has a strong preference for single-stranded DNA. Able to process alkylated 3mC within double-stranded regions via its interaction with ASCC3, which promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3. May also act on RNA. Requires molecular oxygen, alpha-ketoglutarate and iron. {ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517, ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:22055184}.Q9NP81SYSM"Serine--tRNA ligase, mitochondrialgene expression [GO:0010467]; selenocysteinyl-tRNA(Sec) biosynthetic process [GO:0097056]; seryl-tRNA aminoacylation [GO:0006434]; tRNA aminoacylation for protein translation [GO:0006418]dATP binding [GO:0005524]; poly(A) RNA binding [GO:0044822]; serine-tRNA ligase activity [GO:0004828]FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity). {ECO:0000250}.Q2TAA5ALG11<GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferaseSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:20080937}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:20080937}; Multi-pass membrane protein {ECO:0000305|PubMed:20080937}.cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]NGDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0004377]9FUNCTION: Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain. {ECO:0000269|PubMed:20080937}.P01023A2MGAlpha-2-macroglobulin<SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6203908}.$blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of complement activation, lectin pathway [GO:0001869]; negative regulation of endopeptidase activity [GO:0010951]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; stem cell differentiation [GO:0048863]\calcium-dependent protein binding [GO:0048306]; enzyme binding [GO:0019899]; growth factor binding [GO:0019838]; interleukin-1 binding [GO:0019966]; interleukin-8 binding [GO:0019959]; protease binding [GO:0002020]; receptor binding [GO:0005102]; serine-type endopeptidase inhibitor activity [GO:0004867]; tumor necrosis factor binding [GO:0043120]blood microparticle [GO:0072562]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; platelet alpha granule lumen [GO:0031093]Q9UKL0RCOR1REST corepressor 1SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:15897453}. Note=Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.Fblood coagulation [GO:0007596]; chromatin organization [GO:0006325]; histone H4 deacetylation [GO:0070933]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; transcription regulatory region DNA binding [GO:0044212]^nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]TFUNCTION: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, < thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033}.Q96LA8ANM6&Protein arginine N-methyltransferase 6<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11724789}.base-excision repair [GO:0006284]; cell growth [GO:0016049]; cellular senescence [GO:0090398]; chromatin organization [GO:0006325]; histone H3-R2 methylation [GO:0034970]; histone H4-R3 methylation [GO:0043985]; histone methylation [GO:0016571]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [GO:0019919]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]chromatin binding [GO:0003682]; histone-arginine N-methyltransferase activity [GO:0008469]; histone binding [GO:0042393]; histone methyltransferase activity [GO:0042054]; histone methyltransferase activity (H2A-R3 specific) [GO:0070612]; histone methyltransferase activity (H3-R2 specific) [GO:0070611]; histone methyltransferase activity (H4-R3 specific) [GO:0044020]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-arginine omega-N monomethyltransferase activity [GO:0035241]ZFUNCTION: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator. May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC). {ECO:0000250, ECO:0000269|PubMed:11724789, ECO:0000269|PubMed:16157300, ECO:0000269|PubMed:16159886, ECO:0000269|PubMed:16600869, ECO:0000269|PubMed:17267505, ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460, ECO:0000269|PubMed:18079182, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:19509293, ECO:0000269|PubMed:20047962}.Q8TDB6DTX3L!E3 ubiquitin-protein ligase DTX3L Deltex(5)lSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes at sites of DNA damage in a PARP1-dependent manner.cellular response to DNA damage stimulus [GO:0006974]; double-strand break repair [GO:0006302]; histone monoubiquitination [GO:0010390]histone binding [GO:0042393]; ligase activity [GO:0016874]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]$FUNCTION: Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. {ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:19818714, ECO:0000269|PubMed:23230272}.Q9UI14PRAF1!Prenylated Rab acceptor protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Note=According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles. {ECO:0000250}.cell junction [GO:0030054]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]0FUNCTION: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI (By similarity). {ECO:0000250}.Q9H6A9PCX3Pecanex-like protein 3Q9H773DCTP1dCTP pyrophosphatase 1`nucleoside triphosphate catabolic process [GO:0009143]; protein homotetramerization [GO:0051289]dCTP diphosphatase activity [GO:0047840]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleoside-triphosphate diphosphatase activity [GO:0047429]; pyrimidine deoxyribonucleotide binding [GO:0032556]FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases (By similarity). {ECO:0000250}.Q9Y484WIPI47WD repeat domain phosphoinositide-interacting protein 4autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to nitrogen starvation [GO:0006995]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; protein lipidation [GO:0006497]; protein localization to pre-autophagosomal structure [GO:0034497]FUNCTION: Plays an important role in the autophagy pathway, which is the major intracellular degradation system by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. {ECO:0000269|PubMed:23435086}.Q86WT6TRI69"E3 ubiquitin-protein ligase TRIM69SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23131556}. Nucleus {ECO:0000269|PubMed:23131556}. Nucleus speckle {ECO:0000269|PubMed:23131556}.fcytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]uFUNCTION: May have E3 ubiquitin-protein ligase activity. May play a role in ap< optosis. {ECO:0000269|PubMed:23131556}.P78316NOP14Nucleolar protein 14^endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000472]; maturation of SSU-rRNA [GO:0030490]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]Zenzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; snoRNA binding [GO:0030515]90S preribosome [GO:0030686]; membrane [GO:0016020]; mitochondrion [GO:0005739]; Noc4p-Nop14p complex [GO:0030692]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity). {ECO:0000250}.O60506HNRPQ)Heterogeneous nuclear ribonucleoprotein QSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303}. Microsome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleoplasm {ECO:0000250}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleoplasm {ECO:0000250}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm {ECO:0000250}. Note=Expressed predominantly in the nucleoplasm. {ECO:0000250}.;cellular response to interferon-gamma [GO:0071346]; CRD-mediated mRNA stabilization [GO:0070934]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of translation [GO:0017148]; osteoblast differentiation [GO:0001649]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; viral process [GO:0016032]ynucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]Acatalytic step 2 spliceosome [GO:0071013]; CRD-mediated mRNA stability complex [GO:0070937]; endoplasmic reticulum [GO:0005783]; GAIT complex [GO:0097452]; histone pre-mRNA 3'end processing complex [GO:0071204]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]~FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648, ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23071094}.Q01973ROR13Tyrosine-protein kinase transmembrane receptor ROR1}peptidyl-tyrosine phosphorylation [GO:0018108]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147]cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]GFUNCTION: Tyrosine-protein kinase receptor whose role is not yet clear.Q9NVA2 Septin-118SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, synapse. Cell projection, dendritic spine. Cell projection, axon {ECO:0000250}. Note=Partly colocalizes with stress fibers and microtubules. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria.axon [GO:0030424]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; stress fiber [GO:0001725]; synapse [GO:0045202]FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy. {ECO:0000250, ECO:0000269|PubMed:15196925, ECO:0000269|PubMed:19234302, ECO:0000305}.P19256LFA3(Lymphocyte function-associated antigen 3SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-anchor.fblood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cellular response to interferon-gamma [GO:0071346]; cellular response to tumor necrosis factor [GO:0071356]; heterotypic cell-cell adhesion [GO:0034113]; leukocyte migration [GO:0050900]; positive regulation of interleukin-8 secretion [GO:2000484]; single organismal cell-cell adhesion [GO:0016337]anchored component of membrane [GO:0031225]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells.P07948LYNTyrosine-protein kinase LynSUBCELLULAR LOCATION: Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Note=Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts.axon guidance [GO:0007411]; B cell homeostasis [GO:0001782]; B cell receptor signaling pathway [GO:0050853]; blood coagulation [GO:0007596]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to extracellular stimulus [GO:0031668]; cellular response to heat [GO:0034605]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to retinoic acid [GO:0071300]; cytokine secretion [GO:0050663]; dendritic cell differentiation [GO:0097028]; ephrin receptor signaling pathway [GO:< 0048013]; erythrocyte differentiation [GO:0030218]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; Fc receptor mediated inhibitory signaling pathway [GO:0002774]; Fc receptor mediated stimulatory signaling pathway [GO:0002431]; histamine secretion by mast cell [GO:0002553]; immune response-regulating cell surface receptor signaling pathway [GO:0002768]; innate immune response [GO:0045087]; JAK-STAT cascade involved in growth hormone signaling pathway [GO:0060397]; leukocyte migration [GO:0050900]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of immune response [GO:0050777]; negative regulation of intracellular signal transduction [GO:1902532]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of mast cell proliferation [GO:0070667]; negative regulation of myeloid leukocyte differentiation [GO:0002762]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of toll-like receptor 2 signaling pathway [GO:0034136]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]; neuron projection development [GO:0031175]; oligodendrocyte development [GO:0014003]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of B cell receptor signaling pathway [GO:0050861]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular component movement [GO:0051272]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060369]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of neuron projection development [GO:0010976]; positive regulation of oligodendrocyte progenitor proliferation [GO:0070447]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of stress-activated protein kinase signaling cascade [GO:0070304]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of B cell apoptotic process [GO:0002902]; regulation of B cell receptor signaling pathway [GO:0050855]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cytokine production [GO:0001817]; regulation of cytokine secretion [GO:0050707]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of erythrocyte differentiation [GO:0045646]; regulation of inflammatory response [GO:0050727]; regulation of mast cell activation [GO:0033003]; regulation of mast cell degranulation [GO:0043304]; regulation of monocyte chemotaxis [GO:0090025]; regulation of platelet aggregation [GO:0090330]; regulation of protein phosphorylation [GO:0001932]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; response to amino acid [GO:0043200]; response to axon injury [GO:0048678]; response to carbohydrate [GO:0009743]; response to drug [GO:0042493]; response to hormone [GO:0009725]; response to insulin [GO:0032868]; response to organic cyclic compound [GO:0014070]; response to sterol depletion [GO:0006991]; response to toxic substance [GO:0009636]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; T cell costimulation [GO:0031295]; tolerance induction to self antigen [GO:0002513]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; viral process [GO:0016032]TATP binding [GO:0005524]; enzyme binding [GO:0019899]; glycosphingolipid binding [GO:0043208]; ion channel binding [GO:0044325]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; receptor signaling protein tyrosine kinase activity [GO:0004716]!cell-cell adherens junction [GO:0005913]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; Golgi apparatus [GO:0005794]; integrin alpha2-beta1 complex [GO:0034666]; mast cell granule [GO:0042629]; membrane raft [GO:0045121]; mitochondrial crista [GO:0030061]; mitochondrial intermembrane space [GO:0005758]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. {ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10891478, ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15795233, ECO:0000269|PubMed:16467205, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829, ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:18577747, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19290919, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20037584, ECO:0000269< |PubMed:7687428}.P29323EPHB2Ephrin type-B receptor 2SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.angiogenesis [GO:0001525]; axonal fasciculation [GO:0007413]; axon guidance [GO:0007411]; camera-type eye morphogenesis [GO:0048593]; central nervous system projection neuron axonogenesis [GO:0021952]; commissural neuron axon guidance [GO:0071679]; corpus callosum development [GO:0022038]; dendritic spine development [GO:0060996]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; inner ear morphogenesis [GO:0042472]; learning [GO:0007612]; negative regulation of axonogenesis [GO:0050771]; nervous system development [GO:0007399]; optic nerve morphogenesis [GO:0021631]; palate development [GO:0060021]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphorylation [GO:0016310]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of synapse assembly [GO:0051965]; regulation of body fluid levels [GO:0050878]; retinal ganglion cell axon guidance [GO:0031290]; urogenital system development [GO:0001655]ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; protein tyrosine kinase activity [GO:0004713]; transmembrane-ephrin receptor activity [GO:0005005]axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]FFUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor. {ECO:0000269|PubMed:15300251}.Q9Y4D7PLXD1 Plexin-D1^SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.angiogenesis [GO:0001525]; axon guidance [GO:0007411]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; endothelial cell migration [GO:0043542]; outflow tract morphogenesis [GO:0003151]; patterning of blood vessels [GO:0001569]; positive regulation of protein binding [GO:0032092]; regulation of angiogenesis [GO:0045765]; regulation of cell migration [GO:0030334]; semaphorin-plexin signaling pathway [GO:0071526]; synapse assembly [GO:0007416]Wprotein domain specific binding [GO:0019904]; semaphorin receptor activity [GO:0017154]lintegral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]6FUNCTION: Cell surface receptor for SEMA4A and for class 3 semaphorins, such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell signaling, and in regulating the migration of a wide spectrum of cell types. Regulates the migration of thymocytes in the medulla. Regulates endothelial cell migration. Plays an important role in ensuring the specificity of synapse formation. Required for normal development of the heart and vasculature (By similarity). Mediates anti-angiogenic signaling in response to SEMA3E. {ECO:0000250, ECO:0000269|PubMed:20385769}.P48382RFX5DNA-binding protein RFX5negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters.Q9NSI2F207AProtein FAM207AQ9NYH9UTP63U3 small nucleolar RNA-associated protein 6 homologematuration of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]Q96FQ6S10AGProtein S100-A16SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17030513}. Cytoplasm {ECO:0000269|PubMed:17030513}. Note=Primarily nucleolar. Translocates from the nucleolus to the cytoplasm in response to an increase of intracellular calcium levels.$response to calcium ion [GO:0051592]rcalcium ion binding [GO:0005509]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]dFUNCTION: Calcium-binding protein. Binds one calcium ion per monomer. {ECO:0000269|PubMed:17030513}.P01008ANT3Antithrombin-IIIblood coagulation [GO:0007596]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of inflammatory response [GO:0050728]; regulation of blood coagulation, intrinsic pathway [GO:2000266]; response to nutrient [GO:0007584]vheparin binding [GO:0008201]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867]blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]%FUNCTION: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. {ECO:0000269|PubMed:15853774}.Q4ADV7RIC1#RAB6A-GEF complex partner protein 1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23091056}. Membrane {ECO:0000269|PubMed:23091056}; Single-pass membrane protein {ECO:0000255}.negative regulation of cellular protein catabolic process [GO:1903363]; positive regulation of GTPase activity [GO:0043547]; retrograde transport, endosome to Golgi [GO:0042147]\Rab GTPase binding [GO:0017137]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; protein complex [GO:0043234]; RIC1-RGP1 guanyl-nucleotide exchange factor complex [GO:0034066]FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates RAB6A by exchanging bound GDP for free GTP and may thereby required for efficient fusion of endosome-derived vesicles with the Golgi compartment. The RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate receptors. Required for phosphorylation and localization of GJA1. {ECO:0000269|PubMed:16112082, ECO:0000269|PubMed:23091056}.Q9Y508RN114"E3 ubiquitin-protein ligase RNF114eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23645206}. Nucleus {ECO:0000269|PubMed:23645206}.cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; spermatogenesis [GO:0007283]ligase activity [GO:0016874]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein l< igase activity [GO:0061630]; zinc ion binding [GO:0008270]Hcytoplasm [GO:0005737]; intracellular [GO:0005622]; nucleus [GO:0005634]9FUNCTION: E3 ubiquitin-protein ligase promoting the ubiquitination and degradation of the CDK inhibitor CDKN1A and probably also CDKN1B and CDKN1C. These activities stimulate cell cycle's G1-to-S phase transition and suppress cellular senescence. May play a role in spermatogenesis. {ECO:0000269|PubMed:23645206}.Q9Y6J0CABIN#Calcineurin-binding protein cabin-1;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9655484}.cell surface receptor signaling pathway [GO:0007166]; chromatin modification [GO:0016568]; DNA replication-independent nucleosome assembly [GO:0006336]; negative regulation of catalytic activity [GO:0043086]; negative regulation of cell death [GO:0060548]Haggresome [GO:0016235]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]FUNCTION: May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes. {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:9655484}.Q9ULG1INO80DNA helicase INO80SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746, ECO:0000269|PubMed:16298340, ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:20971067}. Note=Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner.cell division [GO:0051301]; cellular response to ionizing radiation [GO:0071479]; cellular response to UV [GO:0034644]; chromatin remodeling [GO:0006338]; DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; mitotic sister chromatid segregation [GO:0000070]; positive regulation of cell growth [GO:0030307]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; spindle assembly [GO:0051225]; transcription, DNA-templated [GO:0006351]; UV-damage excision repair [GO:0070914]alpha-tubulin binding [GO:0043014]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]JIno80 complex [GO:0031011]; microtubule [GO:0005874]; nucleus [GO:0005634]0FUNCTION: DNA helicase and probable main scaffold component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; according to PubMed:20687897 the contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Recruited by YY1 to YY1-activated genes, where it acts as an essential coactivator. Binds DNA. In vitro, has double-stranded DNA-dependent ATPase activity. Involved in UV-damage excision repair, DNA replication and chromosome segregation during normal cell division cycle. {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:16298340, ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:20237820, ECO:0000269|PubMed:20687897, ECO:0000269|PubMed:20855601, ECO:0000269|PubMed:21303910}.P60903S10AAProtein S100-A10establishment of protein localization to plasma membrane [GO:0090002]; membrane budding [GO:0006900]; membrane raft assembly [GO:0001765]; positive regulation of binding [GO:0051099]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein heterotetramerization [GO:0051290]rcalcium ion binding [GO:0005509]; ion channel binding [GO:0044325]; protein homodimerization activity [GO:0042803]Wextracellular exosome [GO:0070062]; extrinsic component of plasma membrane [GO:0019897]FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.Q9UQ03COR2B Coronin-2B,actin cytoskeleton organization [GO:0030036]Nactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; membrane [GO:0016020]LFUNCTION: May play a role in the reorganization of neuronal actin structure.P55011S12A2!Solute carrier family 12 member 2"ammonium transmembrane transport [GO:0072488]; ammonium transport [GO:0015696]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; ion transport [GO:0006811]; mammary duct terminal end bud growth [GO:0060763]; multicellular organism growth [GO:0035264]; potassium ion homeostasis [GO:0055075]; potassium ion import [GO:0010107]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725]; transepithelial ammonium transport [GO:0070634]; transepithelial chloride transport [GO:0030321]; transmembrane transport [GO:0055085]; transport [GO:0006810]Cammonium transmembrane transporter activity [GO:0008519]; potassium:chloride symporter activity [GO:0015379]; potassium ion symporter activity [GO:0022820]; sodium:chloride symporter activity [GO:0015378]; sodium:potassium:chloride symporter activity [GO:0008511]; sodium ion transmembrane transporter activity [GO:0015081]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume.O95807TM50ATransmembrane protein 50AQ99523SORTSortilinSUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin.Tendocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; endosome transport via multivesicular body sorting pathway [GO:0032509]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glucose import [GO:0046323]; Golgi to endosome transport [GO:0006895]; G-protein coupled receptor signaling pathway [GO:0007186]; multicellular organismal development [GO:0007275]; myotube differentiation [GO:0014902]; negative regulation of lipoprotein lipase activity [GO:0051005]; nerve growth factor signaling pathway [GO:0038180]; neuropeptide signaling pathway [GO:0007218]; neurotrophin TRK receptor signaling pathway [GO:0048011]; ossification [GO:0001503]; plasma membrane to endosome transport [GO:0048227]; regulation of gene expression [GO:0010468]; response to insulin [GO:0032868]; vesicle organization [GO:0016050]enzyme binding [GO:0019899]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor activity [GO:0010465];< neurotensin receptor activity, non-G-protein coupled [GO:0030379]^cell surface [GO:0009986]; clathrin-coated vesicle [GO:0030136]; coated pit [GO:0005905]; cytoplasmic membrane-bounded vesicle [GO:0016023]; dendrite [GO:0030425]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; neuronal cell body [GO:0043025]; nuclear membrane [GO:0031965]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network transport vesicle [GO:0030140]FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10085125, ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:12209882, ECO:0000269|PubMed:12598608, ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763, ECO:0000269|PubMed:15313463, ECO:0000269|PubMed:15930396, ECO:0000269|PubMed:15987945}.Q659C4LAR1BLa-related protein 1BPactivation of mitophagy in response to mitochondrial depolarization [GO:0098779]P49366DHYSDeoxyhypusine synthasecellular protein metabolic process [GO:0044267]; deoxyhypusine biosynthetic process from spermidine [GO:0050983]; glucose homeostasis [GO:0042593]; peptidyl-lysine modification to peptidyl-hypusine [GO:0008612]; positive regulation of cell proliferation [GO:0008284]; positive regulation of T cell proliferation [GO:0042102]; post-translational protein modification [GO:0043687]; protein homotetramerization [GO:0051289]; translation [GO:0006412],deoxyhypusine synthase activity [GO:0034038]FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.Q9Y315DEOCDeoxyribose-phosphate aldolase5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25229427}. Cytoplasmic granule {ECO:0000269|PubMed:25229427}. Nucleus {ECO:0000269|PubMed:25229427}. Note=Recruited to stress granules but not to processing bodies upon arsenite or clotrimazole treatment or energy deprivation. {ECO:0000269|PubMed:25229427}.carbohydrate catabolic process [GO:0016052]; deoxyribonucleoside catabolic process [GO:0046121]; deoxyribonucleotide catabolic process [GO:0009264]; deoxyribose phosphate catabolic process [GO:0046386]4deoxyribose-phosphate aldolase activity [GO:0004139]:FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation. {ECO:0000269|PubMed:25229427}.Q9H845ACAD95Acyl-CoA dehydrogenase family member 9, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20816094}.fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; lipid homeostasis [GO:0055088]; mitochondrial respiratory chain complex I assembly [GO:0032981]Gdendrite [GO:0030425]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Required for mitochondrial complex I assembly (PubMed:20816094, PubMed:24158852). Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA than on stearoyl-CoA. However, it does not play a primary role in long-chain fatty acid oxidation in vivo (PubMed:20816094, PubMed:24158852). Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0). {ECO:0000269|PubMed:20816094, ECO:0000269|PubMed:24158852}.O15440MRP5)Multidrug resistance-associated protein 5#carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan biosynthetic process [GO:0030213]; hyaluronan metabolic process [GO:0030212]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; transport [GO:0006810]{FUNCTION: Acts as a multispecific organic anion pump which can transport nucleotide analogs. {ECO:0000269|PubMed:10840050}.P61952GBG11BGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; G-protein coupled receptor signaling pathway [GO:0007186]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]EGTPase activity [GO:0003924]; signal transducer activity [GO:0004871]Kheterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886]Q17RW2COOA1Collagen alpha-1(XXIV) chainjextracellular matrix organization [GO:0030198]; hematopoietic progenitor cell differentiation [GO:0002244]collagen trimer [GO:0005581]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development. {ECO:0000269|PubMed:12874293}.O43464HTRA2$Serine protease HTRA2, mitochondrialQSUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.adult walking behavior [GO:0007628]; cellular protein catabolic process [GO:0044257]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heat [GO:0034605]; cellular response to interferon-beta [GO:0035458]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; ceramide metabolic process [GO:0006672]; execution phase of apoptosis [GO:0097194]; forebrain development [GO:0030900]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; mitochondrion organization [GO:0007005]; negative regulation of cell cycle [GO:0045786]; negative regulation of neuron death [GO:1901215]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; neuron development [GO:0048666]; pentacyclic triterpenoid metabolic process [GO:0019742]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell death [GO:0010942]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; regulation of mitochondrion degradation [GO:1903146]; regulation of multicellular organism growth [GO:0040014]; response to herbicide [GO:0009635]peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008< 236]; unfolded protein binding [GO:0051082]CD40 receptor complex [GO:0035631]; chromatin [GO:0000785]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]7FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive. {ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:19502560}.P33991MCM4%DNA replication licensing factor MCM4Q13459MYO9BUnconventional myosin-IXb$SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region.sactin filament-based movement [GO:0030048]; establishment of cell polarity [GO:0030010]; lamellipodium morphogenesis [GO:0072673]; macrophage chemotaxis [GO:0048246]; monocyte chemotaxis [GO:0002548]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]actin binding [GO:0003779]; ADP binding [GO:0043531]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; microfilament motor activity [GO:0000146]7actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filamentous actin [GO:0031941]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; membrane [GO:0016020]; myosin complex [GO:0016459]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]tFUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho.O94886CSCL1CSC1-like protein 1SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:20957757}; Multi-pass membrane protein {ECO:0000269|PubMed:20957757}.pextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]O75146HIP1R0Huntingtin-interacting protein 1-related proteinSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.vapoptotic process [GO:0006915]; clathrin-mediated endocytosis [GO:0072583]; receptor-mediated endocytosis [GO:0006898]clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]kFUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:14732715}.Q8N122RPTOR%Regulatory-associated protein of mTOR mTor ComplexSUBCELLULAR LOCATION: Cytoplasm. Lysosome. Cytoplasmic granule. Note=Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased.cell cycle arrest [GO:0007050]; cell growth [GO:0016049]; cellular response to amino acid stimulus [GO:0071230]; cellular response to heat [GO:0034605]; cellular response to nutrient levels [GO:0031669]; gene expression [GO:0010467]; insulin receptor signaling pathway [GO:0008286]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription from RNA polymerase III promoter [GO:0045945]; regulation of cell size [GO:0008361]; regulation of cellular response to heat [GO:1900034]; TOR signaling [GO:0031929]; transcription initiation from RNA polymerase II promoter [GO:0006367]]14-3-3 protein binding [GO:0071889]; protein complex binding [GO:0032403]; protein kinase binding [GO:0019901]; RNA polymerase III type 1 promoter DNA binding [GO:0001030]; RNA polymerase III type 2 promoter DNA binding [GO:0001031]; RNA polymerase III type 3 promoter DNA binding [GO:0001032]; TFIIIC-class transcription factor binding [GO:0001156] cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; TORC1 complex [GO:0031931]FUNCTION: Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis. {ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:23727834}.Q14240IF4A2"Eukaryotic initiation factor 4A-II"cellular protein metabolic process [GO:0044267]; cytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; negative regulation of RNA-directed RNA polymerase activity [GO:1900260]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of translational initiation [GO:0006446]; RNA secondary structure unwinding [GO:0010501]; translation [GO:0006412]; translational initiation [GO:0006413]; viral process [GO:0016032]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]; translation initiation factor activity [GO:0003743]cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow < efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.Q00013EM55#55 kDa erythrocyte membrane proteinSUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell projection, stereocilium {ECO:0000250}. Note=Colocalizes with WHRN at stereocilium tip during hair cell development (By similarity). Colocalizes with MPP5 in the retina, at the outer limiting membrane (OLM). Colocalizes with WHRN in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies and at the connecting cilium (CC). Colocalizes with NF2 in non-myelin-forming Schwann cells. {ECO:0000250}.{nucleotide phosphorylation [GO:0046939]; regulation of neutrophil chemotaxis [GO:0090022]; signal transduction [GO:0007165]&guanylate kinase activity [GO:0004385]cortical cytoskeleton [GO:0030863]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; membrane [GO:0016020]; stereocilium [GO:0032420]FUNCTION: Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity (By similarity). {ECO:0000250}.Q92604LGAT13Acyl-CoA:lysophosphatidylglycerol acyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15485873}; Multi-pass membrane protein {ECO:0000269|PubMed:15485873}.glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylglycerol acyl-chain remodeling [GO:0036148]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]pFUNCTION: Lysophoshatidylglycerol (LPG) specific acyltransferase that recognizes various acyl-CoAs and LPGs as substrates but demonstrates a clear preference for long chain saturated fatty acyl-CoAs and oleoyl-CoA as acyl donors. Prefers oleoyl-LPG over palmitoyl-LPG as an acyl receptor and oleoyl-CoA over lauroyl-CoA as an acyl donor. {ECO:0000269|PubMed:15485873}.Q9P227RHG23 Rho GTPase-activating protein 23Q9Y6K5OAS32'-5'-oligoadenylate synthase 3cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of viral genome replication [GO:0045071]; nucleobase-containing compound metabolic process [GO:0006139]; regulation of ribonuclease activity [GO:0060700]; response to virus [GO:0009615]; type I interferon signaling pathway [GO:0060337]2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV). {ECO:0000269|PubMed:19056102, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:9880533}.Q5VZE5NAA354N-alpha-acetyltransferase 35, NatC auxiliary subunitdnegative regulation of apoptotic process [GO:0043066]; smooth muscle cell proliferation [GO:0048659]FUNCTION: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells. {ECO:0000269|PubMed:19398576}.Q9Y6N5SQRD-Sulfide:quinone oxidoreductase, mitochondrialCcellular nitrogen compound metabolic process [GO:0034641]; hydrogen sulfide metabolic process [GO:0070813]; small molecule metabolic process [GO:0044281]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]; sulfur amino acid catabolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]Rquinone binding [GO:0048038]; sulfide:quinone oxidoreductase activity [GO:0070224]-FUNCTION: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). {ECO:0000269|PubMed:22852582}.Q9P0U1TOM72Mitochondrial import receptor subunit TOM7 homologSUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:12198123}; Single-pass membrane protein {ECO:0000269|PubMed:12198123}._activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cellular protein metabolic process [GO:0044267]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]; regulation of protein stability [GO:0031647]FUNCTION: Required for assembly and stability of the TOM complex. Positive regulator of PARK2 translocation to damaged mitochondria. Acts probably by stabilizing PINK1 on the outer membrane of depolarized mitochondria. {ECO:0000269|PubMed:18331822, ECO:0000269|PubMed:24270810}.Q00536CDK16Cyclin-dependent kinase 16SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY.exocytosis [GO:0006887]; growth hormone secretion [GO:0030252]; neuron projection development [GO:0031175]; protein phosphorylation [GO:0006468]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; spermatogenesis [GO:0007283]ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine/threonine kinase activity [GO:0004674]cell junction [GO:0030054]; cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; microtubule cytoskeleton [GO:0015630]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; transport vesicle [GO:0030133]3FUNCTION: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250, ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068}.O94955RHBT3+Rho-related BTB domain-containing protein 3DSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19490898}.lretrograde transport, endosome to Golgi [GO:0042147]; small GTPase mediated signal transduction [GO:0007264]WATPase activity [GO:0016887]; ATP binding [GO:0005524]; Rab GTPase binding [GO:0017137]@extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]FUNCTION: Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsi< c ATPase activity due to autoinhibition, which is relieved by Rab9. {ECO:0000269|PubMed:19490898}.Q9Y672ALG6@Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferaseWcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; oligosaccharide-lipid intermediate biosynthetic process [GO:0006490]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity [GO:0042281]; glucosyltransferase activity [GO:0046527]FUNCTION: Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol.P37268FDFTSqualene synthasecellular lipid metabolic process [GO:0044255]; cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate metabolic process [GO:0045338]; isoprenoid biosynthetic process [GO:0008299]; small molecule metabolic process [GO:0044281]; steroid biosynthetic process [GO:0006694]farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; oxidoreductase activity [GO:0016491]; squalene synthase activity [GO:0051996]Q99996AKAP9A-kinase anchor protein 9SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Golgi apparatus. Note=Cytoplasmic in parietal cells.cellular response to cAMP [GO:0071320]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of potassium ion transmembrane transporter activity [GO:1901018]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane repolarization [GO:0060306]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; Sertoli cell development [GO:0060009]; signal transduction [GO:0007165]; spermatogenesis [GO:0007283]; synaptic transmission [GO:0007268]; transport [GO:0006810]ion channel binding [GO:0044325]; potassium channel regulator activity [GO:0015459]; protein complex scaffold [GO:0032947]; protein kinase A regulatory subunit binding [GO:0034237]; receptor binding [GO:0005102]:centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cis-Golgi network [GO:0005801]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; pericentriolar material [GO:0000242]; voltage-gated potassium channel complex [GO:0008076]FUNCTION: Binds to type II regulatory subunits of protein kinase A. Scaffolding protein that assembles several protein kinases and phosphatases on the centrosome and Golgi apparatus. May be required to maintain the integrity of the Golgi apparatus. Isoform 4 is associated with the N-methyl-D-aspartate receptor and is specifically found in the neuromuscular junction (NMJ) as well as in neuronal synapses, suggesting a role in the organization of postsynaptic specializations. {ECO:0000269|PubMed:15047863}.A4D1E9GTPBAGTP-binding protein 10[SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17054726}. Chromosome {ECO:0000269|PubMed:17054726}. Note=Found in the dense fibrillar compartment region of the nucleolus. At the onset of mitosis moves to the chromosome surface and remains there until anaphase. Gradually re-assembles into the nucleolus at late anaphase to telophase.|GTPase activity [GO:0003924]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]Kchromosome [GO:0005694]; mitochondrion [GO:0005739]; nucleolus [GO:0005730] FUNCTION: May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nuceleolar architecture is observed. {ECO:0000269|PubMed:17054726}.Q9NR61DLL4Delta-like protein 4Delta(DLL1/3/4)/JAG1/4angiogenesis [GO:0001525]; blood circulation [GO:0008015]; blood vessel lumenization [GO:0072554]; blood vessel remodeling [GO:0001974]; cardiac atrium morphogenesis [GO:0003209]; cardiac ventricle morphogenesis [GO:0003208]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; dorsal aorta morphogenesis [GO:0035912]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell proliferation [GO:0008285]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch receptor processing [GO:0007220]; Notch signaling involved in heart development [GO:0061314]; Notch signaling pathway [GO:0007219]; patterning of blood vessels [GO:0001569]; pericardium morphogenesis [GO:0003344]; positive regulation of gene expression [GO:0010628]; positive regulation of neural precursor cell proliferation [GO:2000179]; regulation of neural retina development [GO:0061074]; regulation of neurogenesis [GO:0050767]; signal transduction [GO:0007165]; ventral spinal cord interneuron fate commitment [GO:0060579]; ventricular trabecula myocardium morphogenesis [GO:0003222]; visual perception [GO:0007601]<calcium ion binding [GO:0005509]; Notch binding [GO:0005112]FUNCTION: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation is required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate. {ECO:0000269|PubMed:17728344, ECO:0000269|PubMed:20616313}.Q4V9L6TM119Transmembrane protein 119'osteoblast differentiation [GO:0001649]WFUNCTION: May promote the differentiation of myoblasts into osteoblasts. {ECO:0000250}.P13747HLAE5HLA class I histocompatibility antigen, alpha chain EHadaptive immune response [GO:0002250]; antibacterial humoral response [GO:0019731]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; CD8-positive, alpha-beta T cell activation [GO:0036037]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; positive regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000566]; positive regulation of immunoglobulin secretion [GO:0051024]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of natural killer cell mediated immunity [GO:0002717]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of TRAIL production [GO:0032759]; positive regulation of tumor necrosis factor production [GO:0032760]; protection from natural killer cell mediated cytotoxicity [GO:0042270]; regulation of immune response [GO:0050776]; regulation of natural killer cell mediated immunity [GO:0002715]; type I interferon signaling pathway [GO:0060337]beta-2-microglobulin binding [GO:0030881]; MHC class I protein < binding [GO:0042288]; natural killer cell lectin-like receptor binding [GO:0046703]; peptide antigen binding [GO:0042605]; receptor binding [GO:0005102]cell surface [GO:0009986]; early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; MHC class Ib protein complex [GO:0032398]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]pFUNCTION: Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules.Q8IYL3CA174UPF0688 protein C1orf174<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22361696}.Q8IX04UEVLD)Ubiquitin-conjugating enzyme E2 variant 3carbohydrate metabolic process [GO:0005975]; carboxylic acid metabolic process [GO:0019752]; cellular protein modification process [GO:0006464]; protein transport [GO:0015031]boxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616][FUNCTION: Possible negative regulator of polyubiquitination. {ECO:0000269|PubMed:12427560}.Q9Y6Q2STON1Stonin-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11381094}. Membrane {ECO:0000269|PubMed:11381094}. Note=Some fraction is membrane-associated.nendocytosis [GO:0006897]; intracellular protein transport [GO:0006886]; regulation of endocytosis [GO:0030100]%clathrin adaptor complex [GO:0030131]DFUNCTION: May be involved in the endocytic machinery. {ECO:0000250}.Q9NUN5LMBD1(Probable lysosomal cobalamin transporterSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19136951}; Multi-pass membrane protein {ECO:0000269|PubMed:19136951}.cobalamin metabolic process [GO:0009235]; insulin receptor internalization [GO:0038016]; negative regulation of glucose import [GO:0046325]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of protein kinase B signaling [GO:0051898]; small molecule metabolic process [GO:0044281]; viral process [GO:0016032]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]cobalamin binding [GO:0031419]clathrin-coated endocytic vesicle [GO:0045334]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886] FUNCTION: Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors. Isoform 3 may play a role in the assembly of hepatitis delta virus (HDV). {ECO:0000269|PubMed:15956556, ECO:0000269|PubMed:19136951}.Q9H5V8CDCP1CUB domain-containing protein 1SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Shedding may also lead to a soluble peptide.; SUBCELLULAR LOCATION: Isoform 3: Secreted.lextracellular region [GO:0005576]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]#FUNCTION: May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis. {ECO:0000269|PubMed:11466621, ECO:0000269|PubMed:12799299, ECO:0000269|PubMed:15153610, ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16404722, ECO:0000269|PubMed:8647901}.Q8IUH3RBM45RNA-binding protein 45SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12220514}. Nucleus {ECO:0000269|PubMed:12220514}. Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus.FUNCTION: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development. {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000269|PubMed:12220514}.P04818TYSYThymidylate synthaseSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21876188}. Cytoplasm {ECO:0000269|PubMed:21876188}. Mitochondrion {ECO:0000269|PubMed:21876188}. Mitochondrion matrix {ECO:0000269|PubMed:21876188}. Mitochondrion inner membrane {ECO:0000269|PubMed:21876188}.8aging [GO:0007568]; cartilage development [GO:0051216]; circadian rhythm [GO:0007623]; deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; developmental growth [GO:0048589]; dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; dUMP metabolic process [GO:0046078]; G1/S transition of mitotic cell cycle [GO:0000082]; immortalization of host cell by virus [GO:0019088]; intestinal epithelial cell maturation [GO:0060574]; mitotic cell cycle [GO:0000278]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; organ regeneration [GO:0031100]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside biosynthetic process [GO:0046134]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to folic acid [GO:0051593]; response to glucocorticoid [GO:0051384]; response to organophosphorus [GO:0046683]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; small molecule metabolic process [GO:0044281]; tetrahydrofolate metabolic process [GO:0046653]; uracil metabolic process [GO:0019860]cofactor binding [GO:0048037]; drug binding [GO:0008144]; folic acid binding [GO:0005542]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; thymidylate synthase activity [GO:0004799]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]sFUNCTION: Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:0000269|PubMed:21876188}.P04004VTNC Vitronectincell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-matrix adhesion [GO:0007160]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; immune response [GO:0006955]; innate immune response [GO:0045087]; negative regulation of blood coagulation [GO:0030195]; negative regulation of endopeptidase activity [GO:0010951]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein binding [GO:0032092]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; positive regulation of wound healing [GO:0090303]; regulation of complement activation [GO:0030449]; smooth muscle cell-matrix adhesion [GO:0061302]extracellular matrix binding [GO:0050840]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; polysaccharide binding [GO:0030247]; scavenger receptor activity [GO:0005044]alphav-beta3 integrin-vitronectin complex [GO:0071062]; blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.Q5RKV6EXOS6< Exosome complex component MTR3gSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Nucleus {ECO:0000305}.PDNA deamination [GO:0045006]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; isotype switching [GO:0045190]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA 3'-end processing [GO:0031125]; rRNA catabolic process [GO:0016075]; U4 snRNA 3'-end processing [GO:0034475]cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. {ECO:0000269|PubMed:21255825}.Q9Y2I8WDR37WD repeat-containing protein 37Q9Y4B5MTCL1"Microtubule cross-linking factor 1SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}. Apical cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:23902687}. Midbody {ECO:0000269|PubMed:23902687}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23902687}. Note=Colocalized with microtubules at the base of cilia. Gradually accumulates on the apicobasal microtubule bundles during epithelial cell polarization (By similarity). Colocalized with the apicobasal microtubule bundles running beneath the lateral membrane. Colocalized with microtubule bundles in the spindle pole in mitotic cells and in the midbodies at the end of cytokinesis. {ECO:0000250}.&establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; microtubule bundle formation [GO:0001578]; positive regulation of microtubule motor activity [GO:2000576]; positive regulation of protein targeting to membrane [GO:0090314]; regulation of autophagy [GO:0010506]rmicrotubule binding [GO:0008017]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; microtubule bundle [GO:0097427]; midbody [GO:0030496]; spindle pole [GO:0000922]/FUNCTION: Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells. {ECO:0000269|PubMed:23902687}.P36776LONM#Lon protease homolog, mitochondrialiSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:7961901}.aging [GO:0007568]; cellular response to oxidative stress [GO:0034599]; chaperone-mediated protein complex assembly [GO:0051131]; misfolded or incompletely synthesized protein catabolic process [GO:0006515]; mitochondrial DNA metabolic process [GO:0032042]; mitochondrial genome maintenance [GO:0000002]; mitochondrion organization [GO:0007005]; oxidation-dependent protein catabolic process [GO:0070407]; protein homooligomerization [GO:0051260]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of mitochondrial DNA replication [GO:0090296]; response to aluminum ion [GO:0010044]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP-dependent peptidase activity [GO:0004176]; DNA polymerase binding [GO:0070182]; G-quadruplex DNA binding [GO:0051880]; mitochondrial heavy strand promoter anti-sense binding [GO:0070362]; mitochondrial light strand promoter anti-sense binding [GO:0070361]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein. {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12198491, ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247, ECO:0000269|PubMed:8248235}.Q6ZT21TMPPE8Transmembrane protein with metallophosphoesterase domainQ12840KIF5AKinesin heavy chain isoform 5ASUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Concentrated in the cell body of the neurons, particularly in the perinuclear region. {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; protein localization [GO:0008104]; small GTPase mediated signal transduction [GO:0007264]; synaptic transmission [GO:0007268]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; motor activity [GO:0003774]cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL). {ECO:0000250}.Q12923PTN131Tyrosine-protein phosphatase non-receptor type 13SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11356191}. Cell projection, lamellipodium {ECO:0000269|PubMed:11356191}. Note=Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover.peptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]; regulation of phosphatidylinositol 3-kinase signaling [GO:0014066]< yphosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; protein tyrosine phosphatase activity [GO:0004725]cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]7FUNCTION: Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317). {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}.Q99501GA2L1GAS2-like protein 1cell cycle arrest [GO:0007050]; cellular response to starvation [GO:0009267]; cellular response to thyroid hormone stimulus [GO:0097067]; microtubule bundle formation [GO:0001578]; negative regulation of cell growth [GO:0030308]; negative regulation of erythrocyte differentiation [GO:0045647]; negative regulation of gene expression [GO:0010629]; negative regulation of microtubule depolymerization [GO:0007026]; regulation of cell cycle [GO:0051726]{cytoskeletal adaptor activity [GO:0008093]; microtubule binding [GO:0008017]; thyroid hormone receptor binding [GO:0046966]vFUNCTION: Seems to be involved in the cross-linking of microtubules and microfilaments. {ECO:0000269|PubMed:12584248}.Q9BVS5TR61B8tRNA (adenine(58)-N(1))-methyltransferase, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23097428}.Umitochondrial tRNA methylation [GO:0070901]; protein homooligomerization [GO:0051260]:tRNA (adenine-N1-)-methyltransferase activity [GO:0016429]Mmitochondrion [GO:0005739]; tRNA (m1A) methyltransferase complex [GO:0031515]FUNCTION: Methyltransferase that catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion, including tRNA(Leu) (decephering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (decephering codons UCA, UCU, UCG or UCC). {ECO:0000269|PubMed:23097428}.Q86W26NAL100NACHT, LRR and PYD domains-containing protein 10SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22672233}. Cell membrane {ECO:0000269|PubMed:22672233}. Note=Cytoplasmic protein which is recruited to the cell membrane by NOD1 following invasive bacterial infection.defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; dendritic cell migration [GO:0036336]; helper T cell enhancement of adaptive immune response [GO:0035397]; innate immune response [GO:0045087]; positive regulation of interleukin-6 secretion [GO:2000778]; positive regulation of interleukin-8 secretion [GO:2000484]; positive regulation of T-helper 17 type immune response [GO:2000318]; positive regulation of T-helper 1 type immune response [GO:0002827]Kcytoplasm [GO:0005737]; extrinsic component of plasma membrane [GO:0019897]kFUNCTION: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID. Displays anti-inflammatory activity. Plays a role in adaptive immunity through control of dendritic cell-mediated transport of antigen to the lymph nodes from peripheral sites. Required for immunity against C.albicans infection. Involved in the innate immune response by contributing to proinflammatory cytokine release in response to invasive bacterial infection. {ECO:0000269|PubMed:15096476, ECO:0000269|PubMed:20393137, ECO:0000269|PubMed:22672233}.O43790KRT86Keratin, type II cuticular Hb6cextracellular exosome [GO:0070062]; extracellular space [GO:0005615]; keratin filament [GO:0045095]Q7Z6B7SRGP1)SLIT-ROBO Rho GTPase-activating protein 1Laxon guidance [GO:0007411]; cell migration [GO:0016477]; negative regulation of cell migration [GO:0030336]; positive regulation of GTPase activity [GO:0043547]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]GGTPase activator activity [GO:0005096]; Rac GTPase binding [GO:0048365]eFUNCTION: GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42. {ECO:0000269|PubMed:11672528}.Q92997DVL32Segment polarity protein dishevelled homolog DVL-3DSHs(3)7canonical Wnt signaling pathway [GO:0060070]; cochlea morphogenesis [GO:0090103]; intracellular signal transduction [GO:0035556]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; non-canonical Wnt signaling pathway [GO:0035567]; non-canonical Wnt signaling pathway via JNK cascade [GO:0038031]; outflow tract septum morphogenesis [GO:0003148]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription, DNA-templated [GO:0045893]; response to drug [GO:0042493]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]beta-catenin binding [GO:0008013]; frizzled binding [GO:0005109]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; receptor binding [GO:0005102]\FUNCTION: May play a role in the signal transduction pathway mediated by multiple Wnt genes.Q9UBY8CLN8 Protein CLN8&SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10861296}; Multi-pass membrane protein {ECO:0000269|PubMed:10861296}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:10861296}; Multi-pass membrane protein {ECO:0000269|PubMed:10861296}.adult walking behavior [GO:0007628]; age-dependent response to oxidative stress [GO:0001306]; associative learning [GO:0008306]; cellular protein catabolic process [GO:0044257]; ceramide biosynthetic process [GO:0046513]; ceramide metabolic process [GO:0006672]; cholesterol metabolic process [GO:0008203]; L-glutamate uptake involved in synaptic transmission [GO:0051935]; lipid biosynthetic process [GO:0008610]; lipid transport [GO:0006869]; lysosome organization [GO:0007040]; mitochondrial membrane organization [GO:0007006]; musculoskeletal movement [GO:0050881]; negative regulation of apoptotic process [GO:0043066]; negative regulation of proteolysis [GO:0045861]; negative regulation of transferase activity [GO:0051348]; nervous system development [GO:0007399]; neurofilament cytoskeleton organization [GO:0060052]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; phospholipid metabolic process [GO:0006644]; photoreceptor cell maintenance [GO:0045494]; protein catabolic process [GO:0030163]; regulation of cell size [GO:0008361]; retina development in camera-type eye [GO:0060041]; social behavior [GO:0035176]; somatic motor neuron differentiation [GO:0021523]; visual perception [GO:0007601]'endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]FUNCTION: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death. {ECO:0000269|PubMed:19431184}.O00425IF2B33Insulin-like growth factor 2 mRNA-binding protein 3SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. Colocalized with CD44 mRNA in RNP granules. In response to cellular< stress, such as oxidative stress, recruited to stress granules.anatomical structure morphogenesis [GO:0009653]; gene expression [GO:0010467]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; regulation of cytokine biosynthetic process [GO:0042035]; translation [GO:0006412]mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; translation regulator activity [GO:0045182]FUNCTION: RNA-binding factor that may recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:23640942}.Q96QE5TEFM.Transcription elongation factor, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:21278163}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:21278163}.DNA metabolic process [GO:0006259]; oxidative phosphorylation [GO:0006119]; regulation of transcription, DNA-templated [GO:0006355]; transcription from mitochondrial promoter [GO:0006390]ZDNA polymerase processivity factor activity [GO:0030337]; poly(A) RNA binding [GO:0044822]mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; ribonucleoprotein complex [GO:0030529]FUNCTION: Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery. {ECO:0000269|PubMed:21278163}.O75376NCOR1Nuclear receptor corepressor 1ESUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation [GO:0002361]; cellular lipid metabolic process [GO:0044255]; cholesterol homeostasis [GO:0042632]; chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; definitive erythrocyte differentiation [GO:0060318]; gene expression [GO:0010467]; negative regulation of JNK cascade [GO:0046329]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation of histone deacetylation [GO:0031065]; regulation of fatty acid transport [GO:2000191]; regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter [GO:0072362]; regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter [GO:0072368]; regulation of multicellular organism growth [GO:0040014]; small molecule metabolic process [GO:0044281]; spindle assembly [GO:0051225]; thalamus development [GO:0021794]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]histone deacetylase binding [GO:0042826]; histone deacetylase regulator activity [GO:0035033]; nuclear hormone receptor binding [GO:0035257]; RNA polymerase II activating transcription factor binding [GO:0001102]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]; transcription regulatory region DNA binding [GO:0044212]cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; transcriptional repressor complex [GO:0017053]; transcription factor complex [GO:0005667][FUNCTION: Mediates transcriptional repression by certain nuclear receptors. Part of a complex which promotes histone deacetylation and the formation of repressive chromatin structures which may impede the access of basal transcription factors. Participates in the transcriptional repressor activity produced by BCL6. {ECO:0000269|PubMed:14527417}.P19388RPAB1:DNA-directed RNA polymerases I, II, and III subunit RPABC1cytosol [GO:0005829]; DNA-directed RNA polymerase I complex [GO:0005736]; DNA-directed RNA polymerase II, core complex [GO:0005665]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity). {ECO:0000250}.P05165PCCA4Propionyl-CoA carboxylase alpha chain, mitochondrialATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin carboxylase activity [GO:0004075]; enzyme binding [GO:0019899]; metal ion binding [GO:0046872]; propionyl-CoA carboxylase activity [GO:0004658]7cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]Q8TBQ9KISHAProtein kish-ASUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19942856}; Single-pass type I membrane protein {ECO:0000269|PubMed:19942856}.]FUNCTION: Involved in the early part of the secretory pathway. {ECO:0000269|PubMed:19942856}.Q9H3M7TXNIPThioredoxin-interacting proteincell cycle [GO:0007049]; cellular response to tumor cell [GO:0071228]; innate immune response [GO:0045087]; keratinocyte differentiation [GO:0030216]; negative regulation of cell division [GO:0051782]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; protein import into nucleus [GO:0006606]; regulation of cell proliferation [GO:0042127]; response to calcium ion [GO:0051592]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to mechanical stimulus [GO:0009612]; response to progesterone [GO:0032570]; transcription, DNA-templated [GO:0006351]Uenzyme inhibitor activity [GO:0004857]; ubiquitin protein ligase binding [GO:0031625]rcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; nucleus [GO:0005634]LFUNCTION: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1). {< ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:21460850}.Q8NB46ANR52JSerine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit CQ8WWY3PRP31+U4/U6 small nuclear ribonucleoprotein Prp31uSUBCELLULAR LOCATION: Nucleus speckle. Nucleus, Cajal body. Note=Predominantly found in speckles and in Cajal bodies.amRNA splicing, via spliceosome [GO:0000398]; spliceosomal tri-snRNP complex assembly [GO:0000244]lpoly(A) RNA binding [GO:0044822]; ribonucleoprotein complex binding [GO:0043021]; snRNP binding [GO:0070990]Cajal body [GO:0015030]; MLL1 complex [GO:0071339]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; U2-type spliceosomal complex [GO:0005684]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U4atac snRNP [GO:0005690]; U4 snRNP [GO:0005687]FUNCTION: Involved in pre-mRNA splicing. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. {ECO:0000269|PubMed:11867543}.Q6UWF9F180AProtein FAM180AQ8N8A6DDX51 ATP-dependent RNA helicase DDX51LRNA secondary structure unwinding [GO:0010501]; rRNA processing [GO:0006364]gFUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. {ECO:0000250}.P62312LSM6(U6 snRNA-associated Sm-like protein LSm6USUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12515382}. Nucleus {ECO:0000250}.qexonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; maturation of SSU-rRNA [GO:0030490]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; RNA splicing [GO:0008380]; tRNA processing [GO:0008033]Rcytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; small nuclear ribonucleoprotein complex [GO:0030532]; small nucleolar ribonucleoprotein complex [GO:0005732]; spliceosomal complex [GO:0005681]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U6 snRNP [GO:0005688]FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). {ECO:0000250}.Q53F19CQ085 Uncharacterized protein C17orf85Q8NFJ9BBS1Bardet-Biedl syndrome 1 proteinSUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.hcilium assembly [GO:0042384]; Golgi to plasma membrane protein transport [GO:0043001]; nonmotile primary cilium assembly [GO:0035058]; organelle organization [GO:0006996]; photoreceptor cell maintenance [GO:0045494]; protein localization to cilium [GO:0061512]; response to stimulus [GO:0050896]; retina homeostasis [GO:0001895]; visual perception [GO:0007601]patched binding [GO:0005113]; RNA polymerase II repressing transcription factor binding [GO:0001103]; smoothened binding [GO:0005119]axoneme [GO:0005930]; BBSome [GO:0034464]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary membrane [GO:0060170]; cytosol [GO:0005829]FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.Q92597NDRG1 Protein NDRG1SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane. Note=Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granular staining in proximal tubular cells of the kidney and salivary gland ducts. Recruits to the membrane of recycling/sorting and late endosomes via binding to phosphatidylinositol 4-phosphate. Associates with microtubules. Colocalizes with TUBG1 in the centrosome. Cytoplasmic location increased with hypoxia. Phosphorylated form found associated with centromeres during S-phase of mitosis and with the plasma membrane.hcellular response to hypoxia [GO:0071456]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; mast cell activation [GO:0045576]; negative regulation of cell proliferation [GO:0008285]; peripheral nervous system myelin maintenance [GO:0032287]; positive regulation of spindle checkpoint [GO:0090232]; response to metal ion [GO:0010038]cadherin binding [GO:0045296]; gamma-tubulin binding [GO:0043015]; microtubule binding [GO:0008017]; Rab GTPase binding [GO:0017137]|cell-cell adherens junction [GO:0005913]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]FUNCTION: Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy. {ECO:0000269|PubMed:15247272, ECO:0000269|PubMed:15377670, ECO:0000269|PubMed:17786215, ECO:0000269|PubMed:9766676}.P63272SPT4H$Transcription elongation factor SPT4;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8649394}.8chromatin remodeling [GO:0006338]; gene expression [GO:0010467]; negative regulation of DNA-templated transcription, elongation [GO:0032785]; negative regulation of transcription elongation from RNA polymerase II promoter [GO:0034244]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation < of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9857195}.O95786DDX58)Probable ATP-dependent RNA helicase DDX58SUBCELLULAR LOCATION: Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cell junction, tight junction. Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.cytoplasmic pattern recognition receptor signaling pathway in response to virus [GO:0039528]; detection of virus [GO:0009597]; innate immune response [GO:0045087]; negative regulation of type I interferon production [GO:0032480]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of gene expression [GO:0010628]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell migration [GO:0030334]; regulation of type III interferon production [GO:0034344]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RIG-I signaling pathway [GO:0039529]; viral process [GO:0016032]ATP binding [GO:0005524]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; ruffle membrane [GO:0032587]FUNCTION: Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:15208624, ECO:0000269|PubMed:15708988, ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19122199, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21742966}.Q15084PDIA6Protein disulfide-isomerase A6SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}. Cell membrane. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.cell redox homeostasis [GO:0045454]; cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976]Mendoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; plasma membrane [GO:0005886]FUNCTION: May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936}.Q6ICL7S35E4"Solute carrier family 35 member E4*anion transmembrane transport [GO:0098656]Q9UMS6SYNP2Synaptopodin-2SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. Localizes to the Z-disk in mature striated muscle. The nuclear export is XPO1-dependent (By similarity). Localized in a fiber-like pattern. partly overlapping with filamentous actin. {ECO:0000250, ECO:0000269|PubMed:18371299}.N14-3-3 protein binding [GO:0071889]; muscle alpha-actinin binding [GO:0051371]< gactin cytoskeleton [GO:0015629]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; Z disc [GO:0030018]JFUNCTION: Has an actin-binding and actin-bundling activity. {ECO:0000250}.Q14202ZMYM3Zinc finger MYM-type protein 3cytoskeleton organization [GO:0007010]; multicellular organismal development [GO:0007275]; regulation of cell morphogenesis [GO:0022604]yFUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.Q96LZ7RMD2+Regulator of microtubule dynamics protein 2SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. Also detected as large dots in the perinuclear region.xcytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; microtubule [GO:0005874]; spindle pole [GO:0000922]Q15554TERF2!Telomeric repeat-binding factor 2SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20655466}. Chromosome, telomere {ECO:0000269|PubMed:20655466}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.+cell cycle [GO:0007049]; cellular senescence [GO:0090398]; in utero embryonic development [GO:0001701]; negative regulation of beta-galactosidase activity [GO:1903770]; negative regulation of cell aging [GO:0090344]; negative regulation of cellular senescence [GO:2000773]; negative regulation of gene expression [GO:0010629]; negative regulation of telomere maintenance [GO:0032205]; negative regulation of telomere maintenance via semi-conservative replication [GO:0032214]; negative regulation of telomere single strand break repair [GO:1903824]; positive regulation of gene expression [GO:0010628]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of telomere maintenance [GO:0032206]; protection from non-homologous end joining at telomere [GO:0031848]; protein localization to chromosome, telomeric region [GO:0070198]; regulation of telomere maintenance [GO:0032204]; telomere capping [GO:0016233]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]; telomeric loop formation [GO:0031627]double-stranded telomeric DNA binding [GO:0003691]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]; telomeric DNA binding [GO:0042162])chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; male germ cell nucleus [GO:0001673]; nuclear chromosome, telomeric region [GO:0000784]; nuclear telomere cap complex [GO:0000783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telosome [GO:0070187]FFUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:20655466, ECO:0000269|PubMed:9476899}.Q53QV2LBH Protein LBHeSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17390236}. Cytoplasm {ECO:0000269|PubMed:17390236}.multicellular organismal development [GO:0007275]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of blood coagulation [GO:0030193]; regulation of gene expression [GO:0010468]; transcription, DNA-templated [GO:0006351]FUNCTION: Transcriptional activator which may act in mitogen-activated protein kinase signaling pathway. {ECO:0000269|PubMed:17390236}.Q14919NC2ADr1-associated corepressorDNA binding [GO:0003677]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]FUNCTION: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. {ECO:0000269|PubMed:8608938, ECO:0000269|PubMed:8670811}.Q969E8TSR2(Pre-rRNA-processing protein TSR2 homologDFUNCTION: May be involved in 20S pre-rRNA processing. {ECO:0000305}.Q9H974QTRD1.Queuine tRNA-ribosyltransferase subunit QTRTD1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03043}. Note=May associate with the mitochondrion outer membrane. {ECO:0000255|HAMAP-Rule:MF_03043}.+queuosine biosynthetic process [GO:0008616]Tqueuine tRNA-ribosyltransferase activity [GO:0008479]; zinc ion binding [GO:0008270]FUNCTION: Interacts with QTRT1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_03043}.Q86SX6GLRX5-Glutaredoxin-related protein 5, mitochondrial=cell redox homeostasis [GO:0045454]; hemopoiesis [GO:0030097]2 iron, 2 sulfur cluster binding [GO:0051537]; electron carrier activity [GO:0009055]; metal ion binding [GO:0046872]; protein disulfide oxidoreductase activity [GO:0015035]hdendrite [GO:0030425]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1.Q9HAU0PKHA57Pleckstrin homology domain-containing family A member 5>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22037487}.,reproductive system development [GO:0061458] 1-phosphatidylinositol binding [GO:0005545]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]Q8N1W1ARG28)Rho guanine nucleotide exchange factor 28SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with the microtubule radial and cortical systems. {ECO:0000250}.%axon guidance [GO:0007411]; central nervous system neuron axonogenesis [GO:0021955]; ephrin receptor signaling pathway [GO:0048013]; intracellular signal transduction [GO:0035556]; neurofilament cytoskeleton organization [GO:0060052]; regulation< of Rho protein signal transduction [GO:0035023]umetal ion binding [GO:0046872]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]; RNA binding [GO:0003723]FUNCTION: Functions as a RHOA-specific guanine nucleotide exchange factor regulating signaling pathways downstream of integrins and growth factor receptors. Functions in axonal branching, synapse formation and dendritic morphogenesis. Functions also in focal adhesion formation, cell motility and B-lymphocytes activation. May regulate NEFL expression and aggregation and play a role in apoptosis (By similarity). {ECO:0000250}.P45983MK08"Mitogen-activated protein kinase 8eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21148294}. Nucleus {ECO:0000269|PubMed:21148294}. apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to mechanical stimulus [GO:0071260]; cellular response to nitric oxide [GO:0071732]; dendrite morphogenesis [GO:0048813]; Fc-epsilon receptor signaling pathway [GO:0038095]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; JNK cascade [GO:0007254]; JUN phosphorylation [GO:0007258]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein binding [GO:0032091]; neuron migration [GO:0001764]; neurotrophin TRK receptor signaling pathway [GO:0048011]; ossification [GO:0001503]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cyclase activity [GO:0031281]; positive regulation of deacetylase activity [GO:0090045]; positive regulation of determination of dorsal identity [GO:2000017]; positive regulation of gene expression [GO:0010628]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; positive regulation of protein metabolic process [GO:0051247]; programmed cell death [GO:0012501]; programmed necrotic cell death [GO:0097300]; protein phosphorylation [GO:0006468]; regulation of circadian rhythm [GO:0042752]; regulation of histone deacetylation [GO:0031063]; regulation of protein localization [GO:0032880]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; response to cadmium ion [GO:0046686]; response to stress [GO:0006950]; response to UV [GO:0009411]; rhythmic process [GO:0048511]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]ATP binding [GO:0005524]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; histone deacetylase regulator activity [GO:0035033]; JUN kinase activity [GO:0004705]; protein serine/threonine kinase activity [GO:0004674]`cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). {ECO:0000269|PubMed:22441692}.; FUNCTION: JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.Q8IY22CMIPC-Maf-inducing protein=SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Isoform 2 is translocated to the nucleus and is specifically recruited during minimal change nephrotic syndrome (MCNS). Detected in nuclear and cytoplasmic compartments during MCNS relapse. Expressed in cytoplasm only during MCNS remission and absent in normal patients.FFUNCTION: Plays a role in T-cell signaling pathway. Isoform 2 may play a role in T-helper 2 (Th2) signaling pathway and seems to represent the first proximal signaling protein that links T-cell receptor-mediated signal to the activation of c-Maf Th2 specific factor. {ECO:0000269|PubMed:12939343, ECO:0000269|PubMed:15128042}.Q15047SETB1)Histone-lysine N-methyltransferase SETDB1SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin.bone development [GO:0060348]; chromatin organization [GO:0006325]; histone H3-K9 trimethylation [GO:0036124]; inner cell mass cell proliferation [GO:0001833]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]qDNA binding [GO:0003677]; histone-lysine N-methyltransferase activity [GO:0018024]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins. {ECO:0000269|PubMed:12869583< , ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:17952062}.Q9NYC9DYH9Dynein heavy chain 9, axonemalcell projection organization [GO:0030030]; microtubule-based movement [GO:0007018]; movement of cell or subcellular component [GO:0006928]; spermatogenesis [GO:0007283]faxoneme [GO:0005930]; cytoskeleton [GO:0005856]; dynein complex [GO:0030286]; microtubule [GO:0005874]FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.P31689DNJA1!DnaJ homolog subfamily A member 1SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10816573}; Lipid-anchor {ECO:0000305|PubMed:10816573}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}. Note=Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proportion is associated with nuclei. {ECO:0000250}.androgen receptor signaling pathway [GO:0030521]; DNA damage response, detection of DNA damage [GO:0042769]; negative regulation of apoptotic process [GO:0043066]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of apoptotic process [GO:0043065]; protein folding [GO:0006457]; protein localization to mitochondrion [GO:0070585]; protein refolding [GO:0042026]; regulation of protein transport [GO:0051223]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]; spermatogenesis [GO:0007283]; sperm motility [GO:0030317]; toxin transport [GO:1901998]wATP binding [GO:0005524]; C3HC4-type RING finger domain binding [GO:0055131]; chaperone binding [GO:0051087]; G-protein coupled receptor binding [GO:0001664]; Hsp70 protein binding [GO:0030544]; low-density lipoprotein particle receptor binding [GO:0050750]; metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}.Q9NW08RPC2,DNA-directed RNA polymerase III subunit RPC2dcytosol [GO:0005829]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleoplasm [GO:0005654]"FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370}.P02649APOEApolipoprotein Ealpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering [GO:0097113]; artery morphogenesis [GO:0048844]; cellular calcium ion homeostasis [GO:0006874]; cGMP-mediated signaling [GO:0019934]; cholesterol biosynthetic process [GO:0006695]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance [GO:0034382]; cytoskeleton organization [GO:0007010]; fatty acid homeostasis [GO:0055089]; G-protein coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; intracellular transport [GO:0046907]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process [GO:0042159]; lipoprotein metabolic process [GO:0042157]; long-chain fatty acid transport [GO:0015909]; low-density lipoprotein particle remodeling [GO:0034374]; maintenance of location in cell [GO:0051651]; negative regulation of beta-amyloid formation [GO:1902430]; negative regulation of blood coagulation [GO:0030195]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of cholesterol efflux [GO:0090370]; negative regulation of dendritic spine development [GO:0061000]; negative regulation of dendritic spine maintenance [GO:1902951]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of inflammatory response [GO:0050728]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of lipid transport across blood brain barrier [GO:1903001]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron death [GO:1901215]; negative regulation of phospholipid efflux [GO:1902999]; negative regulation of platelet activation [GO:0010544]; negative regulation of postsynaptic membrane organization [GO:1901627]; negative regulation of presynaptic membrane organization [GO:1901630]; neuron projection regeneration [GO:0031102]; nitric oxide mediated signal transduction [GO:0007263]; N-methyl-D-aspartate receptor clustering [GO:0097114]; phospholipid efflux [GO:0033700]; phototransduction, visible light [GO:0007603]; positive regulation by host of viral process [GO:0044794]; positive regulation of beta-amyloid formation [GO:1902004]; positive regulation of cGMP biosynthetic process [GO:0030828]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol esterification [GO:0010873]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of lipid transport across blood brain barrier [GO:1903002]; positive regulation of low-density lipoprotein particle receptor catabolic process [GO:0032805]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of neurofibrillary tangle assembly [GO:1902998]; positive regulation of neuron death [GO:1901216]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of postsynaptic membrane organization [GO:1901628]; positive regulation of presynaptic membrane organization [GO:1901631]; protein import [GO:0017038]; receptor-mediated endocytosis [GO:0006898]; regulation of axon extension [GO:0030516]; regulation of beta-amyl< oid clearance [GO:1900221]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of gene expression [GO:0010468]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neuron death [GO:1901214]; regulation of tau-protein kinase activity [GO:1902947]; response to dietary excess [GO:0002021]; response to reactive oxygen species [GO:0000302]; retinoid metabolic process [GO:0001523]; reverse cholesterol transport [GO:0043691]; small molecule metabolic process [GO:0044281]; synaptic transmission, cholinergic [GO:0007271]; triglyceride catabolic process [GO:0019433]; triglyceride metabolic process [GO:0006641]; vasodilation [GO:0042311]; very-low-density lipoprotein particle clearance [GO:0034447]; very-low-density lipoprotein particle remodeling [GO:0034372]; virion assembly [GO:0019068]antioxidant activity [GO:0016209]; beta-amyloid binding [GO:0001540]; cholesterol binding [GO:0015485]; cholesterol transporter activity [GO:0017127]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; lipoprotein particle binding [GO:0071813]; low-density lipoprotein particle receptor binding [GO:0050750]; metal chelating activity [GO:0046911]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803]; tau protein binding [GO:0048156]; very-low-density lipoprotein particle receptor binding [GO:0070326]blood microparticle [GO:0072562]; chylomicron [GO:0042627]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.P53814SMTN SmoothelinXSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Exhibits a filamentous organization.Mmuscle organ development [GO:0007517]; smooth muscle contraction [GO:0006939]lactin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]1FUNCTION: Structural protein of the cytoskeleton.Q68DH5LMBD2!LMBR1 domain-containing protein 2Q6AZY7SCAR3#Scavenger receptor class A member 38SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9580669}; Single-pass type II membrane protein {ECO:0000269|PubMed:9580669}. Golgi apparatus membrane {ECO:0000269|PubMed:9580669}; Single-pass type II membrane protein {ECO:0000269|PubMed:9580669}. Note=Endoplasmic reticulum and/or Golgi.qreceptor-mediated endocytosis [GO:0006898]; response to oxidative stress [GO:0006979]; UV protection [GO:0009650]collagen trimer [GO:0005581]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]FUNCTION: Seems to protect cells by scavenging oxidative molecules or harmful products of oxidation. {ECO:0000269|PubMed:9580669}.Q8NDI1EHBP1EH domain-binding protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676205}. Membrane {ECO:0000269|PubMed:14676205}. Note=Mostly found in cytosol and plasma membrane.FUNCTION: May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. {ECO:0000269|PubMed:14676205}.P23219PGH1Prostaglandin G/H synthase 1SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.aging [GO:0007568]; arachidonic acid metabolic process [GO:0019369]; cyclooxygenase pathway [GO:0019371]; inflammatory response [GO:0006954]; learning [GO:0007612]; lipid metabolic process [GO:0006629]; maintenance of blood-brain barrier [GO:0035633]; memory [GO:0007613]; negative regulation of epinephrine secretion [GO:0032811]; negative regulation of norepinephrine secretion [GO:0010700]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of vasoconstriction [GO:0045907]; prostaglandin biosynthetic process [GO:0001516]; regulation of blood pressure [GO:0008217]; regulation of cell proliferation [GO:0042127]; response to corticosterone [GO:0051412]; response to fatty acid [GO:0070542]; response to organonitrogen compound [GO:0010243]; response to oxidative stress [GO:0006979]; sensory perception of pain [GO:0019233]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]dioxygenase activity [GO:0051213]; heme binding [GO:0020037]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; photoreceptor outer segment [GO:0001750].FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells.Q9H5Q4TFB2M.Dimethyladenosine transferase 2, mitochondrial'gene expression [GO:0010467]; mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription from mitochondrial promoter [GO:0006390]; transcription initiation from mitochondrial promoter [GO:0006391]poly(A) RNA binding [GO:0044822]; rRNA (adenine-N6,N6-)-dimethyltransferase activity [GO:0000179]; transcription cofactor activity [GO:0003712]BFUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. Also required for basal transcription of mitochondrial DNA, probably via its interaction with POLRMT and TFAM. Stimulates transcription independently of the methyltransferase activity. Compared to TFB1M, it activates transcription of mitochondrial DNA more efficiently, while it has less methyltransferase activity. {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033, ECO:0000269|PubMed:20410300}.O60237MYPT2,Protein phosphatase 1 regulatory subunit 12BPP1R12a/b/c(6)qSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923170}. Note=Along actomyosin filaments and stress fibers.G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; positive regulation of catalytic activity [GO:0043085]; regulation of muscle contraction [GO:0006937]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]Senzyme activator activity [GO:0008047]; phosphatase regulator activity [GO:0019208]FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus. {ECO:0000269|PubMed:11067852, ECO:0000269|PubMed:9570949}.Q9NSI6BRWD1.Bromodomain and WD repeat-containing protein 17SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.cytoskeleton organization [GO:0007010]; regulation of cell shape [GO:0008360]; regulation< of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351] FUNCTION: May be a transcriptional activator. May be involved in chromatin remodeling (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}.Q9BUR5APOOApolipoprotein OSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25764979}; Single-pass membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:25764979}. Mitochondrion {ECO:0000269|PubMed:25781180}. Golgi apparatus membrane {ECO:0000269|PubMed:25764979}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25764979}. Note=Exists in three distinct forms: a glycosylated and secreted form, an ER/Golgi-resident form and a non-glycosylated mitochondrial form. {ECO:0000269|PubMed:25764979}.<cristae formation [GO:0042407]; lipid transport [GO:0006869]endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; high-density lipoprotein particle [GO:0034364]; integral component of mitochondrial inner membrane [GO:0031305]; low-density lipoprotein particle [GO:0034362]; MICOS complex [GO:0061617]; mitochondrion [GO:0005739]; very-low-density lipoprotein particle [GO:0034361]BFUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a crucial role in crista junction formation and mitochondrial function (PubMed:25764979). Can promote cardiac lipotoxicity by enhancing mitochondrial respiration and fatty acid metabolism in cardiac myoblasts (PubMed:24743151). Promotes cholesterol efflux from macrophage cells. Detected in HDL, LDL and VLDL. Secreted by a microsomal triglyceride transfer protein (MTTP)-dependent mechanism, probably as a VLDL-associated protein that is subsequently transferred to HDL (PubMed:16956892). {ECO:0000269|PubMed:16956892, ECO:0000269|PubMed:24743151, ECO:0000269|PubMed:25764979}.O94915FRYLProtein furry homolog-likeactin filament reorganization [GO:0090527]; cell morphogenesis [GO:0000902]; neuron projection development [GO:0031175]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]?cell cortex [GO:0005938]; site of polarized growth [GO:0030427]FUNCTION: Plays a key role in maintaining the integrity of polarized cell extensions during morphogenesis, regulates the actin cytoskeleton and plays a key role in patterning sensory neuron dendritic fields by promoting avoidance between homologous dendrites as well as by limiting dendritic branching (By similarity). May function as a transcriptional activator. {ECO:0000250, ECO:0000269|PubMed:16061630}.Q96IZ0PAWR$PRKC apoptosis WT1 regulator protein?SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis (By similarity). Nuclear localization includes nucleoplasm and PML nuclear bodies. {ECO:0000250}.actin filament bundle assembly [GO:0051017]; activation of cysteine-type endopeptidase activity [GO:0097202]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; calcium ion import into cell [GO:1990035]; cellular response to estradiol stimulus [GO:0071392]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to interleukin-1 [GO:0071347]; cellular response to vitamin E [GO:0071306]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; interleukin-2 biosynthetic process [GO:0042094]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of calcium ion import [GO:0090281]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of action potential [GO:0045760]; positive regulation of amyloid precursor protein biosynthetic process [GO:0042986]; positive regulation of apoptotic process [GO:0043065]; positive regulation of hindgut contraction [GO:0060450]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of neutrophil extravasation [GO:2000391]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of relaxation of smooth muscle [GO:1901082]; regulation of neuronal action potential [GO:0098908]; response to iron(II) ion [GO:0010040]; response to lipopolysaccharide [GO:0032496]; response to wounding [GO:0009611]; transcription, DNA-templated [GO:0006351]actin binding [GO:0003779]; enzyme binding [GO:0019899]; leucine zipper domain binding [GO:0043522]; transcription corepressor activity [GO:0003714]actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}.Q9H089LSG1Large subunit GTPase 1 homologSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16209721}. Endoplasmic reticulum {ECO:0000269|PubMed:16209721}. Nucleus, Cajal body {ECO:0000269|PubMed:16209721}. Note=Shuttles between the Cajal bodies in the nucleus and the endoplasmic reticulum.]nuclear export [GO:0051168]; protein transport [GO:0015031]; ribosome biogenesis [GO:0042254]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (Probable). {ECO:0000305|PubMed:16209721}.Q14699RFTN1RaftlinSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12805216}; Lipid-anchor {ECO:0000269|PubMed:12805216}. Note=Associates with lipid rafts.B cell receptor signaling pathway [GO:0050853]; dsRNA transport [GO:0033227]; growth [GO:0040007]; interleukin-17 production [GO:0032620]; membrane raft assembly [GO:0001765]; protein localization to membrane raft [GO:1903044]; protein transport into membrane raft [GO:0032596]; response to exogenous dsRNA [GO:0043330]; T cell antigen processing and presentation [GO:0002457]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 3 signaling pathway [GO:0034138](double-stranded RNA binding [GO:0003725]cytoplasm [GO:0005737]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: May play a pivotal role in the formation and/or maintenance of lipid rafts. May regulate B-cell antigen receptor-mediated signaling. {ECO:0000269|PubMed:12805216}.Q9BVL4SELOSelenoprotein OQ86V85GP180 Integral membrane protein GPR180]G-protein coupled receptor signaling pathway [GO:0007186]; respo< nse to pheromone [GO:0019236]Q86Y22CONA1Collagen alpha-1(XXIII) chainSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]collagen trimer [GO:0005581]; endoplasmic reticulum lumen [GO:0005788]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]Q96H72S39ADZinc transporter ZIP13SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:21917916}; Multi-pass membrane protein {ECO:0000269|PubMed:21917916}.cellular zinc ion homeostasis [GO:0006882]; connective tissue development [GO:0061448]; zinc II ion transmembrane transport [GO:0071577]hprotein homodimerization activity [GO:0042803]; zinc ion transmembrane transporter activity [GO:0005385]Golgi apparatus [GO:0005794]; integral component of Golgi membrane [GO:0030173]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]KFUNCTION: Acts as a zinc-influx transporter. {ECO:0000269|PubMed:21917916}.Q8IWB1IPRI9Inositol 1,4,5-trisphosphate receptor-interacting proteinBSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16990268}.3membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release. {ECO:0000269|PubMed:16990268}.Q8N543OGFD1Prolyl 3-hydroxylase OGFOD1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Mainly nuclear. A portion relocalizes to cytoplasmic stress granules upon stress.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.cell proliferation [GO:0008283]; peptidyl-proline hydroxylation [GO:0019511]; protein hydroxylation [GO:0018126]; regulation of translational termination [GO:0006449]; stress granule assembly [GO:0034063]iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; peptidyl-proline 3-dioxygenase activity [GO:0031544]; peptidyl-proline dioxygenase activity [GO:0031543]Ucytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634])FUNCTION: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit RPS23, thereby regulating protein translation termination efficiency. Involved in stress granule formation. {ECO:0000269|PubMed:20154146, ECO:0000269|PubMed:24550447, ECO:0000269|PubMed:24550462}.Q9ULJ6ZMIZ1+Zinc finger MIZ domain-containing protein 1mSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14609956}. Cytoplasm {ECO:0000269|PubMed:14609956}.artery morphogenesis [GO:0048844]; cell aging [GO:0007569]; developmental growth [GO:0048589]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]; vasculogenesis [GO:0001570]; vitellogenesis [GO:0007296]FUNCTION: Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation.Q8NHU6TDRD7!Tudor domain-containing protein 7SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21436445}. Note=Localizes to cytoplasmic RNA granules. Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids (By similarity). {ECO:0000250}.germ cell development [GO:0007281]; lens fiber cell differentiation [GO:0070306]; lens morphogenesis in camera-type eye [GO:0002089]; posttranscriptional regulation of gene expression [GO:0010608]; spermatogenesis [GO:0007283]chromatoid body [GO:0033391]; cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; P granule [GO:0043186]; ribonucleoprotein granule [GO:0035770]FUNCTION: Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis. {ECO:0000269|PubMed:21436445}.Q8IW35CEP97Centrosomal protein of 97 kDawSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17719545}.centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]; protein complex [GO:0043234]FUNCTION: Acts as a key negative regulator of ciliogenesis in collaboration with CCP110 by capping the mother centriole thereby preventing cilia formation. Required for recruitment of CCP110 to the centrosome. {ECO:0000269|PubMed:17719545}.Q9H334FOXP1Forkhead box protein P1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25027557}.Fanatomical structure morphogenesis [GO:0009653]; chemokine (C-C motif) ligand 2 secretion [GO:0035926]; endothelial cell activation [GO:0042118]; interleukin-21 secretion [GO:0072619]; macrophage activation [GO:0042116]; monocyte activation [GO:0042117]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of transcription, DNA-templated [GO:0045892]; osteoclast development [GO:0036035]; osteoclast differentiation [GO:0030316]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of defense response to bacterium [GO:1900424]; regulation of endothelial tube morphogenesis [GO:1901509]; regulation of inflammatory response [GO:0050727]; regulation of interleukin-12 secretion [GO:2001182]; regulation of interleukin-1 beta secretion [GO:0050706]; regulation of macrophage colony-stimulating factor production [GO:1901256]; regulation of monocyte differentiation [GO:0045655]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of tumor necrosis factor production [GO:0032680]; response to lipopolysaccharide [GO:0032496]; T follicular helper cell differentiation [GO:0061470]; transcription, DNA-templated [GO:0006351]androgen receptor binding [GO:0050681]; metal ion binding [GO:0046872]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981] FUNCTION: Transcriptional repressor (PubMed:18347093). Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (By similarity). Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal chord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintainance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18 (By similarity). Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting< B-cell expansion by inhibition of caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor (PubMed:15286807, PubMed:18799727, PubMed:18347093). Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B (PubMed:24023716). Can negatively regulate androgen receptor signaling (PubMed:18640093). {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:15286807, ECO:0000269|PubMed:18640093, ECO:0000269|PubMed:18799727, ECO:0000269|PubMed:24023716, ECO:0000269|PubMed:25267198, ECO:0000305|PubMed:18347093, ECO:0000305|PubMed:24023716}.; FUNCTION: Isoform 8: Involved in transcriptional regulation in embryonic stem cells (ESCs). Stimulates expression of transcription factors that are required for pluripotency and decreases expression of differentiation-associated genes. Has distinct DNA-binding specifities as compared to the canonical form and preferentially binds DNA with the sequence 5'-CGATACAA-3' (or closely related sequences) (PubMed:21924763). Promotes ESC self-renewal and pluripotency (By similarity). {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:21924763}.Q15398DLGP5 Disks large-associated protein 5SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells.cell proliferation [GO:0008283]; dephosphorylation [GO:0016311]; mitotic chromosome movement towards spindle pole [GO:0007079]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; signaling [GO:0023052]0phosphoprotein phosphatase activity [GO:0004721]~cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle pole centrosome [GO:0031616]FUNCTION: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269|PubMed:12527899, ECO:0000269|PubMed:14699157, ECO:0000269|PubMed:15145941}.Q5HYI7MTX3 Metaxin-3XFUNCTION: Could function in transport of proteins into the mitochondrion. {ECO:0000250}.Q9Y4G6TLN2Talin-2SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell junction, synapse. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Focal adhesion plaques and synapses.|cell adhesion [GO:0007155]; cell-cell junction assembly [GO:0007043]; cytoskeletal anchoring at plasma membrane [GO:0007016]zactin binding [GO:0003779]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]actin cytoskeleton [GO:0015629]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; synapse [GO:0045202] FUNCTION: As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity). {ECO:0000250}.Q9HBH1DEFM"Peptide deformylase, mitochondrialco-translational protein modification [GO:0043686]; N-terminal protein amino acid modification [GO:0031365]; peptidyl-methionine modification [GO:0018206]; positive regulation of cell proliferation [GO:0008284]; translation [GO:0006412]Hiron ion binding [GO:0005506]; peptide deformylase activity [GO:0042586]hFUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. {ECO:0000250}.Q8TED0UTP154U3 small nucleolar RNA-associated protein 15 homologcell junction [GO:0030054]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]; t-UTP complex [GO:0034455]Q8WV22NSE1;Non-structural maintenance of chromosomes element 1 homologpSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086888}. Chromosome, telomere {ECO:0000305|PubMed:18086888}.cellular protein metabolic process [GO:0044267]; double-strand break repair via homologous recombination [GO:0000724]; intracellular signal transduction [GO:0035556]; positive regulation of response to DNA damage stimulus [GO:2001022]; postreplication repair [GO:0006301]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein ubiquitination [GO:0016567]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Smc5-Smc6 complex [GO:0030915]FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NDNL2. Is involved in positive regulation of response to DNA damage stimulus. {ECO:0000269|PubMed:18086888, ECO:0000269|PubMed:20864041}.P48553TPC10/Trafficking protein particle complex subunit 10early endosome to Golgi transport [GO:0034498]; intra-Golgi vesicle-mediated transport [GO:0006891]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]:sodium ion transmembrane transporter activity [GO:0015081]Qintegral component of membrane [GO:0016021]; TRAPPII protein complex [GO:1990071]Q9UEE9CFDP1"Craniofacial development protein 1XSUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.cell adhesion [GO:0007155]; multicellular organismal development [GO:0007275]; negative regulation of fibroblast apoptotic process [GO:2000270]; regulation of cell proliferation [GO:0042127]; regulation of cell shape [GO:0008360]-condensed chromosome kinetochore [GO:0000777]>FUNCTION: May play a role during embryogenesis. {ECO:0000250}.Q9BYI3HYCCIHyccinSUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=According to PubMed:10910037, it is mainly cytoplasmic while according to PubMed:16951682, it is a membrane protein.FUNCTION: May have a role in the beta-catenin/Lef signaling pathway. May have a role in the process of myelination of the central and peripheral nervous system. {ECO:0000269|PubMed:16951682}.O00458IFRD1,Interferon-related developmental regulator 1myoblast fate determination [GO:0007518]; negative regulation of axon extension [GO:0030517]; negative regulation of collateral sprouting [GO:0048671]; skeletal muscle tissue regeneration [GO:0043403]; striated muscle tissue development [GO:0014706]FUNCTION: Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity). {ECO:0000250}.Q13432U119AProtein unc-119 homolog ASUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23535298}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:23535298}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23535298}. Note=Localizes to the centrosome in interphase cells and begins to translocate from the spindle pole to the spindle midzone after the onset of mitosis; it then localizes to the intercellular bridge in telophase cells and to the midbody in cytokinetic cells. {ECO:0000269|PubMed:23535298}.< lendocytosis [GO:0006897]; lipoprotein transport [GO:0042953]; negative regulation of caveolin-mediated endocytosis [GO:2001287]; negative regulation of clathrin-mediated endocytosis [GO:1900186]; phototransduction [GO:0007602]; positive regulation of protein tyrosine kinase activity [GO:0061098]; synaptic transmission [GO:0007268]; visual perception [GO:0007601]centrosome [GO:0005813]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; spindle midzone [GO:0051233]; spindle pole [GO:0000922]FUNCTION: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A. {ECO:0000269|PubMed:12496276, ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972, ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:23535298, ECO:0000305|PubMed:22960633}.Q9BYN0SRXN1Sulfiredoxin-1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15448164}.)response to oxidative stress [GO:0006979]ATP binding [GO:0005524]; oxidoreductase activity, acting on a sulfur group of donors [GO:0016667]; sulfiredoxin activity [GO:0032542]FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. {ECO:0000269|PubMed:15448164, ECO:0000269|PubMed:15590625}.O15294OGT1PUDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitSUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Membrane. Note=Associates with the mitochondrial inner membrane.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus. Cell membrane. Note=Mostly in the nucleus. Retained in the nucleus via interaction with HCFC1. After insulin induction, translocated from the nucleus to the cell membrane via phophatidylinisotide binding. Colocalizes with AKT1 at the plasma membrane.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus.apoptotic process [GO:0006915]; cellular response to retinoic acid [GO:0071300]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; histone H3-K4 trimethylation [GO:0080182]; histone H4-K16 acetylation [GO:0043984]; histone H4-K5 acetylation [GO:0043981]; histone H4-K8 acetylation [GO:0043982]; negative regulation of protein ubiquitination [GO:0031397]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of catalytic activity [GO:0043085]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of histone H3-K27 methylation [GO:0061087]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of proteolysis [GO:0045862]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein O-linked glycosylation [GO:0006493]; regulation of gluconeogenesis involved in cellular glucose homeostasis [GO:0090526]; regulation of glycolytic process [GO:0006110]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of Rac protein signal transduction [GO:0035020]; response to insulin [GO:0032868]; response to nutrient [GO:0007584]; signal transduction [GO:0007165] acetylglucosaminyltransferase activity [GO:0008375]; enzyme activator activity [GO:0008047]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein N-acetylglucosaminyltransferase activity [GO:0016262]; protein O-GlcNAc transferase activity [GO:0097363]cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone acetyltransferase complex [GO:0000123]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; MLL5-L complex [GO:0070688]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (PubMed:12150998, PubMed:18288188, PubMed:19377461, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863). {ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20018868, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:22923583, ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24474760}.; FUNCTION: Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.Q96PE7MCEE*Methylmalonyl-CoA epimerase, mitochondrialcellular lipid metabolic process [GO:0044255]; fatty acid beta-oxidation [GO:0006635]; L-methylmalonyl-CoA metabolic process [GO:0046491]; short-chain fatty acid catabolic process [GO:0019626]; small molecule metabolic process [GO:0044281]Qmetal ion binding [GO:0046872]; methylmalonyl-CoA epimerase activity [GO:0004493]Q9UGM6SYWM&Tryptophan--tRNA ligase, mitochondrialgene expression [GO:0010467]; tRNA aminoacylation for protein translation [GO:0006418]; tryptophanyl-tRNA aminoacylation [GO:0006436]; vasculogenesis [GO:0001570]Q86W56PARGPoly(ADP-ribose) glycohydrolaseSUBCELLULAR LOCATION: Isoform 1: Nucleus {ECO:0000269|PubMed:16460818, ECO:0000269|PubMed:21398629}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:16460818}. Note=Translocates to the nucleus in response to DNA damage.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Mitochondrion.; SUBCELLULAR LOCATION: Isoform 5: Mitochondrion matrix.base-excision repair< [GO:0006284]; carbohydrate metabolic process [GO:0005975]; detection of bacterium [GO:0016045]; DNA repair [GO:0006281]5poly(ADP-ribose) glycohydrolase activity [GO:0004649]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. {ECO:0000269|PubMed:23102699}.Q14123PDE1CICalcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C7activation of phospholipase C activity [GO:0007202]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; neurotrophin TRK receptor signaling pathway [GO:0048011]; signal transduction [GO:0007165]ncalmodulin-dependent cyclic-nucleotide phosphodiesterase activity [GO:0004117]; metal ion binding [GO:0046872]FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP.Q6IC98GRAM4 GRAM domain-containing protein 4SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Colocalizes with COX4I1. {ECO:0000269|PubMed:15565177}.Pintegral component of membrane [GO:0016021]; mitochondrial membrane [GO:0031966]yFUNCTION: Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53. {ECO:0000269|PubMed:15565177}.P12110CO6A2Collagen alpha-2(VI) chainSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8305732}. Membrane {ECO:0000269|PubMed:8305732}; Peripheral membrane protein {ECO:0000269|PubMed:8305732}. Note=Recruited on membranes by CSPG4. axon guidance [GO:0007411]; cell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; protein heterotrimerization [GO:0070208]; response to glucose [GO:0009749]^collagen trimer [GO:0005581]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; proteinaceous extracellular matrix [GO:0005578]; protein complex [GO:0043234]; sarcolemma [GO:0042383]5FUNCTION: Collagen VI acts as a cell-binding protein.O75071EFC144EF-hand calcium-binding domain-containing protein 14Q96MU7YTDC1YTH domain-containing protein 1{SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20167602}. Note=Localizes to a novel subnuclear structure, the YT bodies.rN6-methyladenosine-containing RNA binding [GO:1990247]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]/nuclear body [GO:0016604]; nucleus [GO:0005634]FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552). Regulates alternative splice site selection (PubMed:20167602). {ECO:0000269|PubMed:20167602, ECO:0000269|PubMed:25242552}.Q9BY12SCAPE@S phase cyclin A-associated protein in the endoplasmic reticulumSUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17698606}. Nucleus {ECO:0000269|PubMed:17698606}. Note=Predominantly located in the endoplasmic reticulum, only a small portion is detected in the nucleus.jcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]yFUNCTION: CCNA2/CDK2 regulatory protein that transiently maintains CCNA2 in the cytoplasm. {ECO:0000269|PubMed:17698606}.O60508PRP17Pre-mRNA-processing factor 17;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9830021}.fcatalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]FUNCTION: Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing. {ECO:0000269|PubMed:9830021}.Q2M296MTHSD;Methenyltetrahydrofolate synthase domain-containing proteinQ9GZM8NDEL1(Nuclear distribution protein nudE-like 1bSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Colocalizes with DISC1 in the perinuclear region, including the centrosome (By similarity). Localizes to the interphase centrosome and the mitotic spindle. Localizes to the kinetochore in a CENPF-dependent manner. {ECO:0000250}.wactivation of GTPase activity [GO:0090630]; cell migration [GO:0016477]; central nervous system neuron axonogenesis [GO:0021955]; centrosome localization [GO:0051642]; cerebral cortex radially oriented cell migration [GO:0021799]; chromosome segregation [GO:0007059]; establishment of chromosome localization [GO:0051303]; establishment of mitotic spindle orientation [GO:0000132]; inner cell mass cell proliferation [GO:0001833]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; mitotic centrosome separation [GO:0007100]; neurofilament cytoskeleton organization [GO:0060052]; neuron migration [GO:0001764]; neuron projection extension [GO:1990138]; nuclear envelope disassembly [GO:0051081]; positive regulation of axon extension [GO:0045773]; positive regulation of axon regeneration [GO:0048680]; positive regulation of GTPase activity [GO:0043547]; regulation of intracellular protein transport [GO:0033157]; regulation of neuron projection development [GO:0010975]; retrograde axon cargo transport [GO:0008090]; small GTPase mediated signal transduction [GO:0007264]; vesicle transport along microtubule [GO:0047496]Fmicrotubule binding [GO:0008017]; oligopeptidase activity [GO:0070012]waxon hillock [GO:0043203]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; microtubule [GO:0005874]; neurofilament cytoskeleton [GO:0060053]; nuclear envelope [GO:0005635]; nucleolus [GO:0005730]; spindle [GO:0005819]FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. {ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:16291< 865, ECO:0000269|PubMed:17600710}.P51668UB2D1"Ubiquitin-conjugating enzyme E2 D1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18845142}.9anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; BMP signaling pathway [GO:0030509]; cellular response to hypoxia [GO:0071456]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly checkpoint [GO:0007094]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; ubiquitin-dependent protein catabolic process [GO:0006511]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]; ubiquitin ligase complex [GO:0000151]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4. {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18359941, ECO:0000269|PubMed:19103148, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386}.Q9Y2Y1RPC10-DNA-directed RNA polymerase III subunit RPC10HSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}.ndefense response to virus [GO:0051607]; gene expression [GO:0010467]; innate immune response [GO:0045087]; positive regulation of type I interferon production [GO:0032481]; termination of RNA polymerase III transcription [GO:0006386]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription from RNA polymerase III promoter [GO:0006383]|cytosol [GO:0005829]; DNA-directed RNA polymerase III complex [GO:0005666]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). {ECO:0000250}.Q8NFF5FAD1 FAD synthaseFAD biosynthetic process [GO:0006747]; riboflavin metabolic process [GO:0006771]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]GATP binding [GO:0005524]; FMN adenylyltransferase activity [GO:0003919]mcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; plasma membrane [GO:0005886]vFUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.Q9NSV4DIAP3Protein diaphanous homolog 3SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18755006, ECO:0000269|PubMed:19457867}. Note=During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis.actin cytoskeleton organization [GO:0030036]; small GTPase mediated signal transduction [GO:0007264]; spermatogenesis [GO:0007283]FUNCTION: Binds to GTP-bound form of Rho and to profilin. Acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. It is required for cytokinesis, stress fiber formation, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). {ECO:0000250}.Q9BQD3KXDL1KxDL motif-containing protein 1BLOC-1 complex [GO:0031083]=FUNCTION: Involved in endosomal cargo sorting. {ECO:0000250}.Q9Y4A5TRRAP6Transformation/transcription domain-associated proteinXSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9708738}.~chromatin organization [GO:0006325]; DNA repair [GO:0006281]; histone acetylation [GO:0016573]; histone deubiquitination [GO:0016578]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; mitotic cell cycle checkpoint [GO:0007093]; phosphorylation [GO:0016310]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]kinase activity [GO:0016301]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]Golgi apparatus [GO:0005794]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PCAF complex [GO:0000125]; STAGA complex [GO:0030914]; Swr1 complex [GO:0000812]; transcription factor TFTC complex [GO:0033276]1FUNCTION: Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. {ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:12138177, ECO:0000269|PubMed:12660246, ECO:0000269|PubMed:12743606, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:9708738}.P60891PRPS1$Ribose-phosphate pyrophosphokinase 15-phosphoribose 1-diphosphate biosynthetic process [GO:0006015]; AMP biosynthetic process [GO:0006167]; carbohydrate metabolic process [GO:0005975]; hypoxanthine biosynthetic process [GO:0046101]; nervous system development [GO:0007399]; organ regeneration [GO:0031100]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide < biosynthetic process [GO:0006164]; pyrimidine nucleotide biosynthetic process [GO:0006221]; small molecule metabolic process [GO:0044281]; urate biosynthetic process [GO:0034418]3ADP binding [GO:0043531]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; GDP binding [GO:0019003]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; ribose phosphate diphosphokinase activity [GO:0004749]Kcytosol [GO:0005829]; ribose phosphate diphosphokinase complex [GO:0002189]Q9UPQ8DOLKDolichol kinaseVcellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; dolichyl diphosphate biosynthetic process [GO:0006489]; dolichyl monophosphate biosynthetic process [GO:0043048]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]%dolichol kinase activity [GO:0004168]nendoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]FUNCTION: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. {ECO:0000250}.A8MWD9RUXGL:Putative small nuclear ribonucleoprotein G-like protein 15Ysmall nucleolar ribonucleoprotein complex [GO:0005732]; spliceosomal complex [GO:0005681]DFUNCTION: Associated with snRNP U1, U2, U4/U6 and U5. {ECO:0000250}.Q9H173SIL1Nucleotide exchange factor SIL1mSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12356756, ECO:0000269|PubMed:16282978}.yintracellular protein transport [GO:0006886]; protein folding [GO:0006457]; regulation of catalytic activity [GO:0050790]FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5. {ECO:0000269|PubMed:12356756}.O15155BET1 BET1 homologSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus (By similarity). {ECO:0000250}.cis-Golgi network [GO:0005801]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna [GO:0031985]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity). {ECO:0000250}.Q9Y2D5AKAP2A-kinase anchor protein 2)FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (By similarity). {ECO:0000250}.Q96FJ0STALPAMSH-like proteaseFUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains. {ECO:0000269|PubMed:18758443}.Q8WUI4HDAC7Histone deacetylase 7sSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. Treatment with EDN1 results in shuttling from the nucleus to the perinuclear region. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation.cell-cell junction assembly [GO:0007043]; cellular protein metabolic process [GO:0044267]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of NIK/NF-kappaB signaling [GO:1901223]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; transcription, DNA-templated [GO:0006351]; vasculogenesis [GO:0001570]14-3-3 protein binding [GO:0071889]; activating transcription factor binding [GO:0033613]; chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; NAD-dependent histone deacetylase activity (H3-K14 specific) [GO:0032041]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; repressing transcription factor binding [GO:0070491]; transcription corepressor activity [GO:0003714]pcytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene. Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:12239305, ECO:0000269|PubMed:17360565}.Q86XL3ANKL22Ankyrin repeat and LEM domain-containing protein 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22770216}; Single-pass type III membrane protein {ECO:0000269|PubMed:22770216}.xcell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope reassembly [GO:0007084]; negative regulation of phosphorylation [GO:0042326]; positive regulation of protein dephosphorylation [GO:0035307]; regulation of catalytic activity [GO:0050790]; regulation of protein phosphatase type 2A activity [GO:0034047]FUNCTION: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. {ECO:0000269|PubMed:22770216}.Q14676MDC1+Mediator of DNA damage checkpoint protein 1ASUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12475977, ECO:0000269|PubMed:12499369, ECO:0000269|PubMed:12551934, ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903, ECO:0000269|PubMed:14695167, ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652, ECO:0000269|PubMed:20008512}. Chromosome {ECO:0000250}. Note=Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires 'Ser-139' phosphorylation of H2AFX. Colocalizes with APTX at sites of DNA double-strand breaks.;cellular protein metabolic process [GO:0044267]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; intra-S DNA damage checkpoint [GO:0031573]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]HFHA domain binding [GO:0070975]; protein C-terminus binding [GO:0008022]dchromosome [GO:0005694]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Required for checkpoin< t mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. May serve as a scaffold for the recruitment of DNA repair and signal transduction proteins to discrete foci of DNA damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also required for downstream events subsequent to the recruitment of these proteins. These include phosphorylation and activation of the ATM, CHEK1 and CHEK2 kinases, and stabilization of TP53 and apoptosis. ATM and CHEK2 may also be activated independently by a parallel pathway mediated by TP53BP1. {ECO:0000269|PubMed:12475977, ECO:0000269|PubMed:12499369, ECO:0000269|PubMed:12551934, ECO:0000269|PubMed:12607003, ECO:0000269|PubMed:12607004, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12611903, ECO:0000269|PubMed:14695167, ECO:0000269|PubMed:15201865, ECO:0000269|PubMed:15377652}.Q9H0N0RAB6CRas-related protein Rab-6CmSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.cell cycle process [GO:0022402]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; Rab protein signal transduction [GO:0032482]; regulation of centrosome duplication [GO:0010824]; response to drug [GO:0042493]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]; small GTPase mediated signal transduction [GO:0007264]gcentrosome [GO:0005813]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; nucleus [GO:0005634]FUNCTION: May be involved in the regulation of centrosome duplication and cell cycle progression. {ECO:0000269|PubMed:17426708, ECO:0000269|PubMed:18992151, ECO:0000269|PubMed:20064528}.P35610SOAT1Sterol O-acyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16154994}; Multi-pass membrane protein {ECO:0000269|PubMed:16154994}.cholesterol efflux [GO:0033344]; cholesterol esterification [GO:0034435]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; macrophage derived foam cell differentiation [GO:0010742]; positive regulation of amyloid precursor protein biosynthetic process [GO:0042986]; very-low-density lipoprotein particle assembly [GO:0034379]cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase.O95881TXD12(Thioredoxin domain-containing protein 12PSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12761212}.?protein-disulfide reductase (glutathione) activity [GO:0019153]hFUNCTION: Possesses significant protein thiol-disulfide oxidase activity. {ECO:0000269|PubMed:12761212}.Q9UKV8AGO2Protein argonaute-2SUBCELLULAR LOCATION: Cytoplasm, P-body. Nucleus. Note=Translational repression of mRNAs results in their recruitment to P-bodies. Translocation to the nucleus requires IMP8.2epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; innate immune response [GO:0045087]; miRNA loading onto RISC involved in gene silencing by miRNA [GO:0035280]; miRNA metabolic process [GO:0010586]; mRNA cleavage involved in gene silencing by miRNA [GO:0035279]; mRNA cleavage involved in gene silencing by siRNA [GO:0090625]; negative regulation of translational initiation [GO:0045947]; negative regulation of translation involved in gene silencing by miRNA [GO:0035278]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; post-embryonic development [GO:0009791]; posttranscriptional gene silencing [GO:0016441]; pre-miRNA processing [GO:0031054]; production of miRNAs involved in gene silencing by miRNA [GO:0035196]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; RNA secondary structure unwinding [GO:0010501]; siRNA loading onto RISC involved in RNA interference [GO:0035087]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; translational initiation [GO:0006413]core promoter binding [GO:0001047]; double-stranded RNA binding [GO:0003725]; endoribonuclease activity [GO:0004521]; endoribonuclease activity, cleaving miRNA-paired mRNA [GO:0090624]; endoribonuclease activity, cleaving siRNA-paired mRNA [GO:0070551]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; pre-miRNA binding [GO:0070883]; protein C-terminus binding [GO:0008022]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA polymerase II core binding [GO:0000993]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197]; translation initiation factor activity [GO:0003743]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; micro-ribonucleoprotein complex [GO:0035068]; mRNA cap binding complex [GO:0005845]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; polysome [GO:0005844]; ribonucleoprotein complex [GO:0030529]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578] FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. {ECO:0000269|PubMed:15105377, ECO:0000269|PubMed:15260970, ECO:0000269|PubMed:15284456, ECO:0000269|PubMed:15337849, ECO:0000269|PubMed:15800637, ECO:0000269|PubMed:16081698, ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387, ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:16756390, ECO:0000269|PubMed:16936728, ECO:0000269|PubMed:17382880, ECO:0000269|PubMed:17507929, ECO:0000269|Pu< bMed:17524464, ECO:0000269|PubMed:17531811, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18048652, ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:18690212, ECO:0000269|PubMed:18771919, ECO:0000269|PubMed:19167051, ECO:0000269|PubMed:23746446}.Q9BQ70TCF25Transcription factor 25TCF|SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574069, ECO:0000269|PubMed:18068114}. Note=Some staining in the cytosol.heart development [GO:0007507]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]FUNCTION: May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development. {ECO:0000269|PubMed:16574069}.Q5T6F2UBAP2Ubiquitin-associated protein 2Q9UJK0TSR3(Ribosome biogenesis protein TSR3 homolog#maturation of SSU-rRNA [GO:0030490]rFUNCTION: Probable pre-rRNA processing protein involved in ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_03146}.O95219SNX4Sorting nexin-4SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:17994011}; Peripheral membrane protein {ECO:0000269|PubMed:17994011}; Cytoplasmic side {ECO:0000269|PubMed:17994011}. Note=Also detected on a juxtanuclear endocytic recycling compartment (ERC).endocytic recycling [GO:0032456]; endocytosis [GO:0006897]; positive regulation of histamine secretion by mast cell [GO:1903595]; protein transport [GO:0015031]; vesicle organization [GO:0016050]cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extrinsic component of membrane [GO:0019898]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; SNARE complex [GO:0031201]FUNCTION: May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation. {ECO:0000269|PubMed:17994011}.P12107COBA1Collagen alpha-1(XI) chaincartilage condensation [GO:0001502]; chondrocyte development [GO:0002063]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; embryonic skeletal system morphogenesis [GO:0048704]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; inner ear morphogenesis [GO:0042472]; ossification [GO:0001503]; proteoglycan metabolic process [GO:0006029]; sensory perception of sound [GO:0007605]; tendon development [GO:0035989]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; visual perception [GO:0007601]extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; protein binding, bridging [GO:0030674]qcollagen type XI trimer [GO:0005592]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]mFUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.Q6JQN1ACD10'Acyl-CoA dehydrogenase family member 102acyl-CoA dehydrogenase activity [GO:0003995]; electron carrier activity [GO:0009055]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; hydrolase activity [GO:0016787]; oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor [GO:0052890]kFUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2-methyl-C15-CoA. {ECO:0000269|PubMed:21237683}.Q9P2R6RERE0Arginine-glutamic acid dipeptide repeats proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10814707, ECO:0000269|PubMed:11331249}. Note=Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs._branching morphogenesis of a nerve [GO:0048755]; cerebellar granule cell precursor proliferation [GO:0021930]; cerebellar Purkinje cell layer maturation [GO:0021691]; chromatin remodeling [GO:0006338]; dendrite morphogenesis [GO:0048813]; NLS-bearing protein import into nucleus [GO:0006607]; radial glia guided migration of Purkinje cell [GO:0021942]dchromatin binding [GO:0003682]; poly-glutamine tract binding [GO:0008267]; RNA polymerase II transcription coactivator activity [GO:0001105]; RNA polymerase II transcription corepressor activity [GO:0001106]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]>histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]FUNCTION: Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death. {ECO:0000269|PubMed:11331249}.Q96KB5TOPK<Lymphokine-activated killer T-cell-originated protein kinase(cellular response to UV [GO:0034644]; mitotic nuclear division [GO:0007067]; negative regulation of inflammatory response [GO:0050728]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of stress-activated MAPK cascade [GO:0032873]\FUNCTION: Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. {ECO:0000269|PubMed:10781613, ECO:0000269|PubMed:17482142}.Q9P2K3RCOR3REST corepressor 3fFUNCTION: May act as a component of a corepressor complex that represses transcription. {ECO:0000305}.Q8WWB7NCUG1Lysosomal protein NCU-G1SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:19556463}; Single-pass type I membrane protein {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:19556463}.intracellular receptor signaling pathway [GO:0030522]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]Bligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0004879]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region DNA binding [GO:0044212]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; nucleus [GO:0005634]Q9UHA4LTOR3!Ragulator complex protein LAMTOR3 Scaffold-ERKSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.cellular protein localization [GO:0034613]; cellular response to amino acid stimulus [GO:0071230]; positive regulation of GTPase activity [GO:0043547]; positive regulation of TOR signaling [GO:0032008]_extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Ragulator complex [GO:0071986]Q9H019MFR1L&Mitochondrial fission regulator 1-likeDaerobic respiration [GO:0009060]; mitochondrial fission [GO:0000266]Q96LD4TRI47&Tripartite motif-containing protein 47eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11511098}. Nucleus {ECO:0000269|PubMed:11511098}.Q6ECI4ZN470Zinc finger protein 470<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15302581}.Q96T37RBM15Putative RNA-binding protein 15SUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Peripheral membrane protein. Note=Colocalizes at the nuclear pore with DBP5 and NXF1.Rnegative regulation of myeloid cell differentiation [GO:0045638]; patterning of blood vessels [GO:0001569]; placenta blood vessel development [GO:0060674]; positive regulation of transcription of Notch receptor target [GO:0007221]; spleen development [GO:0048536]; ventricular septum morphogenesis [GO:0060412]; viral proc< ess [GO:0016032]FUNCTION: May function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing. High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing. May be implicated in HOX gene regulation. {ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495}.Q13332PTPRS,Receptor-type tyrosine-protein phosphatase SMcell adhesion [GO:0007155]; cerebellum development [GO:0021549]; cerebral cortex development [GO:0021987]; corpus callosum development [GO:0022038]; establishment of endothelial intestinal barrier [GO:0090557]; extracellular matrix organization [GO:0030198]; hippocampus development [GO:0021766]; spinal cord development [GO:0021510]Itransmembrane receptor protein tyrosine phosphatase activity [GO:0005001]7FUNCTION: Interacts with LAR-interacting protein LIP.1.Q9UNK0STX8 Syntaxin-8SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Preferentially associated with the early endosome. To lesser extends, also present in late endosome, the plasma membrane and coated pits (By similarity). {ECO:0000250}. early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of protein localization to plasma membrane [GO:1903076]; transport [GO:0006810]; vesicle fusion [GO:0006906]tchloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]; vesicle [GO:0031982]FUNCTION: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.Q8WUU5GATD1,GATA zinc finger domain-containing protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21965549}.sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]FUNCTION: Component of some chromatin complex recruited to chromatin sites methylated 'Lys-4' of histone H3 (H3K4me). {ECO:0000269|PubMed:20850016}.Q133622A5GOSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform6SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; negative regulation of cell proliferation [GO:0008285]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of protein phosphatase type 2A activity [GO:0034047]; signal transduction [GO:0007165]schromosome, centromeric region [GO:0000775]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]FUNCTION: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation. {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:17245430}.O15014ZN609Zinc finger protein 609Q7Z5K2WAPL Wings apart-like protein homolog"SUBCELLULAR LOCATION: Isoform 2: Nucleus.; SUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasm. Note=Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase.3cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; negative regulation of chromatin binding [GO:0035562]; negative regulation of DNA replication [GO:0008156]; negative regulation of sister chromatid cohesion [GO:0045875]; positive regulation of fibroblast proliferation [GO:0048146]; protein localization to chromatin [GO:0071168]; regulation of chromosome condensation [GO:0060623]; regulation of cohesin localization to chromatin [GO:0071922]; response to toxic substance [GO:0009636]; viral process [GO:0016032]Ychromatin [GO:0000785]; chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cohesin complex [GO:0008278]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]FUNCTION: Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. {ECO:0000269|PubMed:15150110, ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203}.Q06547GABP1!GA-binding protein subunit beta-1mitochondrion organization [GO:0007005]; organelle organization [GO:0006996]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region DNA binding [GO:0044212]FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene. {ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:8816484}.P23508CRCM Colorectal mutant cancer proteinSUBCELLULAR LOCATION: Cell membrane. Cell projection, lamellipodium. Nucleus {ECO:0000269|PubMed:24824780}. Cytoplasm {ECO:0000269|PubMed:24824780}. Note=Colocalizes with actin at the leading edge of polarized cells.?establishment of protein localization [GO:0045184]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of epithelial cell proliferation [GO:0050680]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]7FUNCTION: Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}.Q96A73P33MXPutative monooxy< genase p33MONOXFUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth.P05997CO5A2Collagen alpha-2(V) chainaxon guidance [GO:0007411]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; eye morphogenesis [GO:0048592]; negative regulation of endodermal cell differentiation [GO:1903225]; ossification [GO:0001503]; skeletal system development [GO:0001501]; skin development [GO:0043588]Xextracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]collagen type V trimer [GO:0005588]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]jFUNCTION: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices (By similarity). {ECO:0000250}.Q7Z417NUFP2:Nuclear fragile X mental retardation-interacting protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837692}. Cytoplasm {ECO:0000269|PubMed:12837692}. Note=Distribution is cell cycle-modulated, being cytoplasmic in the G2/M phase and accumulating in nucleus during the G1 phase.dcytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; polysomal ribosome [GO:0042788]3FUNCTION: Binds RNA. {ECO:0000269|PubMed:12837692}.P08779K1C16Keratin, type I cytoskeletal 16aging [GO:0007568]; cell proliferation [GO:0008283]; cytoskeleton organization [GO:0007010]; epidermis development [GO:0008544]; establishment of skin barrier [GO:0061436]; hair cycle [GO:0042633]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intermediate filament cytoskeleton organization [GO:0045104]; keratinization [GO:0031424]; keratinocyte differentiation [GO:0030216]; keratinocyte migration [GO:0051546]; morphogenesis of an epithelium [GO:0002009]; negative regulation of cell migration [GO:0030336]wcytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; nucleus [GO:0005634]FUNCTION: Epidermis-specific type I keratin that plays a key role in skin. Acts as a regulator of innate immunity in response to skin barrier breach: required for some inflammatory checkpoint for the skin barrier maintenance. {ECO:0000250|UniProtKB:Q9Z2K1}.Q8WXH0SYNE2 Nesprin-2SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:15671068}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton. Mitochondrion. Nucleus, nucleoplasm. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000305|PubMed:15671068}. Note=Different isoform patterns are found in the different compartments of the cell. The isoforms having the C-terminal transmembrane span can be found in several organellar membranes like the nuclear envelope, the sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal adhesions at the cell membrane. The largest part of the outer nuclear membrane-associated protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. Remains associated with the nuclear envelope during its breakdown in mitotic cells. Shorter solubles isoforms can be found in the cytoplasm and within the nucleus.; SUBCELLULAR LOCATION: Isoform 8: Cell junction, focal adhesion {ECO:0000269|PubMed:22768332}. Note=In U2OS cells. {ECO:0000269|PubMed:22768332}.centrosome localization [GO:0051642]; cytoskeletal anchoring at nuclear membrane [GO:0090286]; establishment or maintenance of cell polarity [GO:0007163]; fibroblast migration [GO:0010761]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear migration along microfilament [GO:0031022]; positive regulation of cell migration [GO:0030335]; protein localization to nucleus [GO:0034504]baggresome [GO:0016235]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; filopodium membrane [GO:0031527]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intermediate filament cytoskeleton [GO:0045111]; lamellipodium membrane [GO:0031258]; LINC complex [GO:0034993]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear lumen [GO:0031981]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018]FUNCTION: Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000269|PubMed:12118075, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:20724637}.Q96RE7NACC1&Nucleus accumbens-associated protein 1|SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Distribution in the cytoplasm is dependent on phosphorylation. {ECO:0000250}. negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell proliferation [GO:0008284]; protein homooligomerization [GO:0051260]; transcription, DNA-templated [GO:0006351]RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]cell junction [GO:0030054]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. {ECO:0000269|PubMed:17130457, ECO:0000269|PubMed:17804717}.Q8NAV1PR38APre-mRNA-splicing factor 38AZnuclear membrane [GO:0031965]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]Q5TID7CC181)Coiled-coil domain-containing protein 181P018911A688HLA class I histocompatibility antigen, A-68 alpha chainvantigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cytokine-mediated signaling pathway [GO:0019221]; interferon-ga< mma-mediated signaling pathway [GO:0060333]; regulation of immune response [GO:0050776]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]qbeta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; poly(A) RNA binding [GO:0044822]cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]PFUNCTION: Involved in the presentation of foreign antigens to the immune system.Q8TAA3PSA7L$Proteasome subunit alpha type-7-like:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; programmed cell death [GO:0012501]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular amino acid metabolic process [GO:0006521]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]; spermatoproteasome complex [GO:1990111]FUNCTION: Component of the spermatoproteasome, a form of the proteasome specifically found in testis that promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH (By similarity). {ECO:0000250}.Q9UBL6CPNE7Copine-7cellular response to calcium ion [GO:0071277]; glycerophospholipid biosynthetic process [GO:0046474]; lipid metabolic process [GO:0006629]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]ncytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May function in membrane trafficking. Exhibits calcium-dependent phospholipid binding properties (By similarity). {ECO:0000250}.Q96HY7DHTK1HProbable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23141294}.generation of precursor metabolites and energy [GO:0006091]; glycolytic process [GO:0006096]; hematopoietic progenitor cell differentiation [GO:0002244]; tricarboxylic acid cycle [GO:0006099]uoxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976]Kmitochondrion [GO:0005739]; oxoglutarate dehydrogenase complex [GO:0045252]IFUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.P62166NCS1Neuronal calcium sensor 1SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cytoplasm, perinuclear region. Cell membrane; Peripheral membrane protein. Note=Associated with Golgi stacks. Post-synaptic densities of dendrites, and in the pre-synaptic nerve terminal at neuromuscular junctions.phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of exocytosis [GO:0045921]; regulation of neuron projection development [GO:0010975]ycalcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; voltage-gated calcium channel activity [GO:0005245]axon [GO:0030424]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dense core granule [GO:0031045]; extracellular exosome [GO:0070062]; Golgi cisterna membrane [GO:0032580]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity). {ECO:0000250}.Q9NSP4CENPMCentromere protein MSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome, centromere, kinetochore. Note=Nuclear in non-confluent cells and cytoplasmic in confluent or dividing cells (By similarity). Localizes in the kinetochore domain of centromeres. {ECO:0000250}.]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]xFUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. {ECO:0000269|PubMed:16716197}.P56192SYMC$Methionine--tRNA ligase, cytoplasmicgene expression [GO:0010467]; methionyl-tRNA aminoacylation [GO:0006431]; tRNA aminoacylation for protein translation [GO:0006418]aATP binding [GO:0005524]; methionine-tRNA ligase activity [GO:0004825]; tRNA binding [GO:0000049]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]Q9NRA2S17A5SialinSUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Lysosome membrane; Multi-pass membrane protein.amino acid transport [GO:0006865]; anion transport [GO:0006820]; cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; ion transport [GO:0006811]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; proton transport [GO:0015992]; sialic acid transport [GO:0015739]; transmembrane transport [GO:0055085]isialic acid transmembrane transporter activity [GO:0015136]; sugar:proton symporter activity [GO:0005351]cell junction [GO:0030054]; cytoplasm [GO:0005737]; inte< gral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672]FUNCTION: Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO(3)(-)/H(+) cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva. {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:11751519, ECO:0000269|PubMed:15510212, ECO:0000269|PubMed:21781115, ECO:0000269|PubMed:22778404}.Q96BW1UPP(Uracil phosphoribosyltransferase homologeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17384901}. Nucleus {ECO:0000269|PubMed:17384901}.~female pregnancy [GO:0007565]; lactation [GO:0007595]; response to insulin [GO:0032868]; UMP biosynthetic process [GO:0006222]Q93073SBP2L8Selenocysteine insertion sequence-binding protein 2-likeFUNCTION: Binds SECIS (Sec insertion sequence) elements present on selenocysteine (Sec) protein mRNAs, but does not promote Sec incorporation into selenoproteins in vitro.Q9BVP2GNL3)Guanine nucleotide-binding protein-like 3SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Shuttles between the nucleus and nucleolus. {ECO:0000250}.cell proliferation [GO:0008283]; positive regulation of pri-miRNA transcription from RNA polymerase II promoter [GO:1902895]; regulation of cell proliferation [GO:0042127]; ribosome biogenesis [GO:0042254]extracellular space [GO:0005615]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity). {ECO:0000250}.Q9HBF4ZFYV1,Zinc finger FYVE domain-containing protein 1SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endoplasmic reticulum. Note=Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum.1-phosphatidylinositol binding [GO:0005545]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; zinc ion binding [GO:0008270]autophagosome [GO:0005776]; endoplasmic reticulum [GO:0005783]; ER-mitochondrion membrane contact site [GO:0044233]; extrinsic component of omegasome membrane [GO:0097629]; Golgi stack [GO:0005795]; perinuclear region of cytoplasm [GO:0048471]; pre-autophagosomal structure [GO:0000407]P30411BKRB2B2 bradykinin receptor9Endocrine and other factor-regulated calcium reabsorptionFacute inflammatory response to antigenic stimulus [GO:0002438]; arachidonic acid secretion [GO:0050482]; blood circulation [GO:0008015]; cell surface receptor signaling pathway [GO:0007166]; cellular response to hypoxia [GO:0071456]; G-protein coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; maintenance of blood-brain barrier [GO:0035633]; negative regulation of blood pressure [GO:0045776]; negative regulation of cell proliferation [GO:0008285]; negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator [GO:1902239]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of vascular permeability [GO:0043114]; regulation of vasoconstriction [GO:0019229]; response to drug [GO:0042493]; response to salt stress [GO:0009651]; smooth muscle contraction [GO:0006939]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vasoconstriction [GO:0042310]; vasodilation [GO:0042311]bradykinin receptor activity [GO:0004947]; phosphatidylinositol phospholipase C activity [GO:0004435]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; type 1 angiotensin receptor binding [GO:0031702]}cytosol [GO:0005829]; endosome [GO:0005768]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.Q9BUL8PDC10 Programmed cell death protein 10SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Partially co-localizes with endogenous PXN at the leading edges of migrating cells.cangiogenesis [GO:0001525]; establishment of Golgi localization [GO:0051683]; Golgi reassembly [GO:0090168]; intrinsic apoptotic signaling pathway in response to hydrogen peroxide [GO:0036481]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903588]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of gene expression [GO:0010629]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein stabilization [GO:0050821]; response to hydrogen peroxide [GO:0042542]; wound healing, spreading of cells [GO:0044319]|protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]FUNCTION: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity). {ECO:0000250}.O15131IMA6Importin subunit alpha-6fcytokine-mediated signaling pathway [GO:0019221]; NLS-bearing protein import into nucleus [GO:0006607]FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1 and STAT2 through ARM repeats 8-9. Recognizes influenza A virus nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.Q9BSA9< TM175Transmembrane protein 175Q9NX07TSAP1*tRNA selenocysteine 1-associated protein 1rSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Abundant in the nucleus. {ECO:0000250}.)selenocysteine incorporation [GO:0001514]|FUNCTION: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis (By similarity). {ECO:0000250}.Q86W50MET16!Methyltransferase-like protein 16g23S rRNA (adenine(1618)-N(6))-methyltransferase activity [GO:0052907]; poly(A) RNA binding [GO:0044822]Q2M3G4SHRM1Protein Shroom1Lactin filament bundle assembly [GO:0051017]; cell morphogenesis [GO:0000902]Pcytoplasm [GO:0005737]; microtubule [GO:0005874]; myosin II complex [GO:0016460]fFUNCTION: May be involved in the assembly of microtubule arrays during cell elongation. {ECO:0000250}.Q9H4A6GOLP3Golgi phosphoprotein 3SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion intermembrane space. Cell membrane {ECO:0000250}. Endosome {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. {ECO:0000305}. asymmetric Golgi ribbon formation [GO:0090164]; cell adhesion molecule production [GO:0060352]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; gene expression [GO:0010467]; glycoprotein biosynthetic process [GO:0009101]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; Golgi to plasma membrane protein transport [GO:0043001]; Golgi vesicle budding [GO:0048194]; lamellipodium assembly [GO:0030032]; leukocyte tethering or rolling [GO:0050901]; negative regulation of apoptotic process [GO:0043066]; positive regulation of protein secretion [GO:0050714]; positive regulation of TOR signaling [GO:0032008]; protein retention in Golgi apparatus [GO:0045053]; protein secretion [GO:0009306]; regulation of mitochondrion organization [GO:0010821]Renzyme binding [GO:0019899]; phosphatidylinositol-4-phosphate binding [GO:0070273]2cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi cisterna membrane [GO:0032580]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis. {ECO:0000269|PubMed:16263763, ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:22745132, ECO:0000269|PubMed:23027862, ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23500462}.Q9UKX5ITA11Integrin alpha-11cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-matrix adhesion [GO:0007160]; collagen-activated signaling pathway [GO:0038065]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; osteoblast differentiation [GO:0001649]; substrate-dependent cell migration [GO:0006929]collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; collagen receptor activity [GO:0038064]; metal ion binding [GO:0046872]focal adhesion [GO:0005925]; integrin alpha11-beta1 complex [GO:0034681]; integrin complex [GO:0008305]; membrane [GO:0016020]; plasma membrane [GO:0005886]>FUNCTION: Integrin alpha-11/beta-1 is a receptor for collagen.Q15582BGH35Transforming growth factor-beta-induced protein ig-h3SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Note=May be associated both with microfibrils and with the cell surface.&angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; cell proliferation [GO:0008283]; chondrocyte differentiation [GO:0002062]; extracellular matrix organization [GO:0030198]; negative regulation of cell adhesion [GO:0007162]; response to stimulus [GO:0050896]; visual perception [GO:0007601]gcollagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178]basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]; trans-Golgi network [GO:0005802]FUNCTION: Binds to type I, II, and IV collagens. This adhesion protein may play an important role in cell-collagen interactions. In cartilage, may be involved in endochondral bone formation.Q86XP3DDX42 ATP-dependent RNA helicase DDX42SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle. Nucleus, Cajal body. Note=Isoform 2 is present in Cajal bodies (CBs) and nuclear speckles.Qprotein localization [GO:0008104]; RNA secondary structure unwinding [GO:0010501]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm. {ECO:0000269|PubMed:16397294, ECO:0000269|PubMed:19377511}.Q9UBY9HSPB7Heat shock protein beta-7SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Nucleus, Cajal body {ECO:0000269|PubMed:19464326}. Note=Resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.vregulation of heart contraction [GO:0008016]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]actin cytoskeleton [GO:0015629]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]Q9ULV3CIZ1$Cip1-interacting zinc finger protein@FUNCTION: May regulate the subcellular localization of CIP/WAF1.Q8WZ82OVCA2(Ovarian cancer-associated gene 2 protein&response to retinoic acid [GO:0032526]Q9UPN3MACF1:Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5%SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. Cytoplasm. Golgi apparatus. Cell membrane. Cell projection, ruffle membrane. Note=The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Golgi apparatus. Note=Localizes to the tips of microtubules.Acell cycle arrest [GO:000705< 0]; establishment or maintenance of cell polarity [GO:0007163]; Golgi to plasma membrane protein transport [GO:0043001]; mesoderm formation [GO:0001707]; positive regulation of axon extension [GO:0045773]; positive regulation of Wnt signaling pathway [GO:0030177]; posttranslational protein targeting to membrane [GO:0006620]; regulation of epithelial cell migration [GO:0010632]; regulation of focal adhesion assembly [GO:0051893]; regulation of microtubule-based process [GO:0032886]; Wnt signaling pathway [GO:0016055]; wound healing [GO:0042060]actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATPase activity [GO:0016887]; calcium ion binding [GO:0005509]; poly(A) RNA binding [GO:0044822]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; neuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity). {ECO:0000250}.Q6ZS17FA65AProtein FAM65A{SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to the podocyte major processes and cell body. {ECO:0000250}.Q96GZ6S41A3!Solute carrier family 41 member 3O60462NRP2 Neuropilin-2SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform s9: Secreted {ECO:0000269|PubMed:11112349}.kangiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; nerve development [GO:0021675]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; semaphorin-plexin signaling pathway involved in neuron projection guidance [GO:1902285]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; receptor activity [GO:0004872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor-activated receptor activity [GO:0005021]extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.Q6P5Z2PKN3"Serine/threonine-protein kinase N3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10441506}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10441506}. Note=Nuclear and perinuclear Golgi region.nepithelial cell migration [GO:0010631]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]fATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]`Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]bFUNCTION: Contributes to invasiveness in malignant prostate cancer. {ECO:0000269|PubMed:15282551}.Q9BTY2FUCO2Plasma alpha-L-fucosidasefucose metabolic process [GO:0006004]; glycoside catabolic process [GO:0016139]; regulation of entry of bacterium into host cell [GO:2000535]; response to bacterium [GO:0009617](alpha-L-fucosidase activity [GO:0004560]FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.Q9H6U8ALG9"Alpha-1,2-mannosyltransferase ALG9cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0052926]; dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0052918]; mannosyltransferase activity [GO:0000030]FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides. {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070}.Q14108SCRB2Lysosome membrane protein 2SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}.Fcell adhesion [GO:0007155]; protein targeting to lysosome [GO:0006622];enzyme binding [GO:0019899]; receptor activity [GO:0004872]extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]mFUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA) targeting. {ECO:0000269|PubMed:18022370}.Q9H9E3COG4,Conserved oligomeric Golgi complex subunit 4SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:11703943}; Peripheral membrane protein {ECO:0000305|PubMed:11703943}; Cytoplasmic side {ECO:0000305|PubMed:11703943}.Golgi organization [GO:0007030]; Golgi vesicle prefusion complex stabilization [GO:0048213]; protein transport [GO:0015031]; retrograde transport, vesicle recycling within Golgi [GO:0000301]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]AGolgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1. {ECO:0000269|PubMed:19536132}.P54760EPHB4Ephrin type-B receptor 4SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8188704}; Single-pass type I membrane protein {ECO:0000269|PubMed:8188704}.=angiogenesis [GO:0001525]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell migration involved in sprouting angiogenesis [GO:0002042]; ephrin receptor signaling pathway [GO:0048013]; heart morphogenesis [GO:0003007]; peptidyl-tyrosine phosphorylation [GO:0018108]; protein autophosphorylation [GO:0046777]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]hFUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood < vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis. {ECO:0000269|PubMed:12734395, ECO:0000269|PubMed:16424904}.Q6PII3CC174)Coiled-coil domain-containing protein 174Q9UBT7CTNL1 Alpha-catulinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12270917}. Cell membrane {ECO:0000269|PubMed:12270917}; Peripheral membrane protein {ECO:0000269|PubMed:12270917}.Hcell adhesion [GO:0007155]; Rho protein signal transduction [GO:0007266]Mcytoskeleton [GO:0005856]; cytosol [GO:0005829]; plasma membrane [GO:0005886]FUNCTION: May modulate the Rho pathway signaling by providing a scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1).Q9UPU9SMAG1Protein Smaug homolog 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16221671}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}. Note=Enriched in synaptoneurosomes (By similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also frequently colocalizes in cytoplasmic stress granule-like foci with ELAVL1, TIA1 and TIAL1. {ECO:0000250}.`negative regulation of translation [GO:0017148]; positive regulation of translation [GO:0045727]Mpoly(A) RNA binding [GO:0044822]; translation repressor activity [GO:0030371]_cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; synapse [GO:0045202]hFUNCTION: Acts as a translational repressor of SRE-containing messengers. {ECO:0000269|PubMed:16221671}.Q8NBJ4GOLM1Golgi membrane protein 16SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10831838, ECO:0000269|PubMed:12191016}; Single-pass type II membrane protein {ECO:0000269|PubMed:10831838, ECO:0000269|PubMed:12191016}. Note=Early Golgi. Cycles via the cell surface and endosomes upon lumenal pH disruption.Unucleus organization [GO:0006997]; regulation of lipid metabolic process [GO:0019216]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]@FUNCTION: Unknown. Cellular response protein to viral infection.O60303K0556 Uncharacterized protein KIAA0556nextracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q6PK04CC137)Coiled-coil domain-containing protein 137A4D2B0MBLC12Metallo-beta-lactamase domain-containing protein 1O15533TPSNTapasinvSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.pamide transport [GO:0042886]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; immune response [GO:0006955]; peptide antigen stabilization [GO:0050823]; peptide transport [GO:0015833]; protein complex assembly [GO:0006461]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]MHC class I protein binding [GO:0042288]; peptide antigen binding [GO:0042605]; peptide antigen-transporting ATPase activity [GO:0015433]; TAP1 binding [GO:0046978]; TAP2 binding [GO:0046979]; unfolded protein binding [GO:0051082]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; integral component of membrane [GO:0016021]; MHC class I peptide loading complex [GO:0042824]FUNCTION: Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading). {ECO:0000269|PubMed:10636848}.Q9UIQ6LCAPLeucyl-cystinyl aminopeptidaseSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389728}; Single-pass type II membrane protein {ECO:0000269|PubMed:11389728}. Note=In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases.; SUBCELLULAR LOCATION: Leucyl-cystinyl aminopeptidase, pregnancy serum form: Secreted. Note=During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition.antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cell-cell signaling [GO:0007267]; female pregnancy [GO:0007565]; membrane organization [GO:0061024]; peptide catabolic process [GO:0043171]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217]; signal transduction [GO:0007165]; SMAD protein signal transduction [GO:0060395]aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; metallopeptidase activity [GO:0008237]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]Ycytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; early endosome lumen [GO:0031905]; extracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. {ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:11707427, ECO:0000269|PubMed:1731608}.Q9UM13APC10%Anaphase-promoting complex subunit 10Q6ZN30BNC2 Zinc finger protein basonuclin-2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15081112}.endochondral bone growth [GO:0003416]; mesenchyme development [GO:0060485]; palate development [GO:0060021]; regulation of transcription, DNA-templated [GO:0006355]; tongue development [GO:0043586]; transcription, DNA-templated [GO:0006351]FUNCTION: Probable transcription factor specific for skin keratinocytes. May play a role in the differentiation of spermatozoa and oocytes.Q86XA9HTR5A!HEAT repeat-containing protein 5AQ96T58MINTMsx2-interacting protein\SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11331609}. Note=Associates with chromatin.tnegative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation of neurogenesis [GO:0050769]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA polymerase II transcription factor binding [GO:0001085]; RNA polymerase II transcription factor binding transcription repressor activity [GO:0001191]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]; transcription corepressor activity [GO:0003714]lextracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; transcriptional repressor complex [GO:0017053]FUNCTION:< May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. {ECO:0000250, ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:12374742}.Q9BVJ6UT14A6U3 small nucleolar RNA-associated protein 14 homolog AAFUNCTION: May be required for ribosome biogenesis. {ECO:0000250}.Q96FX7TRM61CtRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61AFUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. {ECO:0000269|PubMed:16043508}.Q6Y1H2HACD24Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}.[cellular lipid metabolic process [GO:0044255]; fatty acid elongation [GO:0030497]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; triglyceride biosynthetic process [GO:0019432]; very long-chain fatty acid biosynthetic process [GO:0042761]P3-hydroxyacyl-CoA dehydratase activity [GO:0018812]; enzyme binding [GO:0019899]lFUNCTION: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.Q9H7Z3NRDE2Protein NRDE2 homologQ8N3G9TM130Transmembrane protein 130SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11256614}; Single-pass type I membrane protein {ECO:0000269|PubMed:11256614}.Q4L180FIL1L$Filamin A-interacting protein 1-likeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18794120}. Membrane {ECO:0000269|PubMed:18794120}. Nucleus {ECO:0000269|PubMed:18794120}.9FUNCTION: Acts as a regulator of the antiangiogenic activity on endothelial cells. When overexpressed in endothelial cells, leads to inhibition of cell proliferation and migration and an increase in apoptosis. Inhibits melanoma growth When expressed in tumor-associated vasculature. {ECO:0000269|PubMed:18794120}.Q8TER5ARH40)Rho guanine nucleotide exchange factor 40kSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16143467}. Note=Concentrated in the perinuclear region.OFUNCTION: May act as a guanine nucleotide exchange factor (GEF). {ECO:0000250}.P51784UBP11(Ubiquitin carboxyl-terminal hydrolase 11`SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Associates with chromatin.FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. {ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:17897950, ECO:0000269|PubMed:18408009, ECO:0000269|PubMed:19874889, ECO:0000269|PubMed:20233726}.P16260GDCGraves disease carrier proteinSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11158296}; Multi-pass membrane protein {ECO:0000269|PubMed:11158296}.coenzyme biosynthetic process [GO:0009108]; pantothenate metabolic process [GO:0015939]; small molecule metabolic process [GO:0044281]; transport [GO:0006810]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]qFUNCTION: Required for the accumulation of coenzyme A in the mitochondrial matrix. {ECO:0000269|PubMed:11158296}.P12109CO6A1Collagen alpha-1(VI) chainvaxon guidance [GO:0007411]; cell adhesion [GO:0007155]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; osteoblast differentiation [GO:0001649]; protein heterotrimerization [GO:0070208]3platelet-derived growth factor binding [GO:0048407]'collagen type VI trimer [GO:0005589]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; protein complex [GO:0043234]; sarcolemma [GO:0042383]Q9UQN3CHM2B&Charged multivesicular body protein 2bSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16041373}. Late endosome membrane {ECO:0000305|PubMed:16041373}; Peripheral membrane protein {ECO:0000305|PubMed:16041373}.cell separation after cytokinesis [GO:0000920]; cognition [GO:0050890]; endosomal transport [GO:0016197]; endosome organization [GO:0007032]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; neuron cellular homeostasis [GO:0070050]; nucleus organization [GO:0006997]; positive regulation of viral release from host cell [GO:1902188]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; intracellular [GO:0005622]; late endosome membrane [GO:0031902]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]#FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.Q4J6C6PPCELProlyl endopeptidase-likeGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16385448}._serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008]Mcytoskeleton [GO:0005856]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]FUNCTION: Probable serine peptidase whose precise substrate specifi< city remains unclear. Does not cleave peptides after a arginine or lysine residue. {ECO:0000269|PubMed:16143824, ECO:0000269|PubMed:16385448}.P61764STXB1Syntaxin-binding protein 1nSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20887364}. Membrane; Peripheral membrane protein.axon target recognition [GO:0007412]; energy reserve metabolic process [GO:0006112]; glutamate secretion [GO:0014047]; long term synaptic depression [GO:0060292]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of synaptic transmission, GABAergic [GO:0032229]; neuromuscular synaptic transmission [GO:0007274]; neurotransmitter secretion [GO:0007269]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; protein transport [GO:0015031]; regulation of insulin secretion [GO:0050796]; regulation of SNARE complex assembly [GO:0035542]; regulation of synaptic vesicle fusion to presynaptic membrane [GO:0031630]; regulation of synaptic vesicle priming [GO:0010807]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; synaptic vesicle maturation [GO:0016188]; vesicle docking involved in exocytosis [GO:0006904]identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; SNARE binding [GO:0000149]; syntaxin-1 binding [GO:0017075]; syntaxin binding [GO:0019905]!cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; protein complex [GO:0043234]; terminal bouton [GO:0043195]FUNCTION: May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions.Q96I25SPF45Splicing factor 457alternative mRNA splicing, via spliceosome [GO:0000380]FUNCTION: Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia. {ECO:0000269|PubMed:12015979, ECO:0000269|PubMed:17589525}.Q15019Septin-2;SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15774761}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15774761}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15774761}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15774761}. Cleavage furrow {ECO:0000269|PubMed:15774761}. Midbody {ECO:0000269|PubMed:15774761}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15774761}. Cell projection, cilium membrane {ECO:0000250}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. In epithelial cells, colocalizes with polyglutamylated tubulin around the trans-Golgi network, as well as juxatnuclear and proximal Golgi apparatus. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes.cell division [GO:0051301]; cilium assembly [GO:0042384]; mitotic nuclear division [GO:0007067]; neuron projection development [GO:0031175]; regulation of L-glutamate transport [GO:0002036]; regulation of protein localization [GO:0032880]; smoothened signaling pathway [GO:0007224]@enzyme regulator activity [GO:0030234]; GTP binding [GO:0005525]actin cytoskeleton [GO:0015629]; ciliary membrane [GO:0060170]; ciliary transition zone [GO:0035869]; cleavage furrow [GO:0032154]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; exocyst [GO:0000145]; extracellular exosome [GO:0070062]; midbody [GO:0030496]; myelin sheath [GO:0043209]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]; synapse [GO:0045202]FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. {ECO:0000269|PubMed:15774761, ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18209106, ECO:0000269|PubMed:19145258}.Q32P44EMAL30Echinoderm microtubule-associated protein-like 3Q9NZC3GDE1)Glycerophosphodiester phosphodiesterase 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Perinuclear vesicles and cell membrane. {ECO:0000250}.Mglycerol metabolic process [GO:0006071]; lipid metabolic process [GO:0006629]glycerophosphodiester phosphodiesterase activity [GO:0008889]; glycerophosphoinositol glycerophosphodiesterase activity [GO:0047395]; metal ion binding [GO:0046872]FUNCTION: Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways (By similarity). {ECO:0000250}.Q9P2K5MYEF2Myelin expression factor 2tmyotube differentiation [GO:0014902]; neuron differentiation [GO:0030182]; transcription, DNA-templated [GO:0006351][DNA binding [GO:0003677]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]FUNCTION: Transcriptional repressor of the myelin basic protein gene (MBP). Binds to the proximal MB1 element 5'-TTGTCC-3' of the MBP promoter. Its binding to MB1 and function are inhibited by PURA (By similarity). {ECO:0000250}.P78357CNTP1Contactin-associated protein 1axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cytoskeleton organization [GO:0007010]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; neuronal action potential propagation [GO:0019227]; neuron projection morphogenesis [GO:0048812]; paranodal junction assembly [GO:0030913]; positive regulation of signal transduction [GO:0009967]; protein localization to paranode region of axon [GO:0002175]; signal transduction [GO:0007165]freceptor activity [GO:0004872]; SH3/SH2 adaptor activity [GO:0005070]; SH3 domain binding [GO:0017124]integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; myelin sheath [GO:0043209]; paranode region of axon [GO:0033270]; voltage-gated potassium channel complex [GO:0008076]KFUNCTION: Seems to play a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibe< rs. Seems to demarcate the paranodal region of the axo-glial junction. In association with contactin may have a role in the signaling between axons and myelinating glial cells.Q15007FL2D Pre-mRNA-splicing regulator WTAPSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11001926, ECO:0000269|PubMed:24316715}. Nucleus speckle {ECO:0000269|PubMed:24407421}.cell cycle [GO:0007049]; mRNA methylation [GO:0080009]; mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]MIS complex [GO:0036396]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]@FUNCTION: Regulatory subunit of the WMM N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation of some adenosine residues of some mRNAs and plays a role in the efficiency of mRNA splicing, processing and mRNA stability. Required for accumulation of METTL3 and METTL14 to nuclear speckle (PubMed:24316715, PubMed:24407421, PubMed:24981863). Acts as a mRNA splicing regulator (PubMed:12444081). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (PubMed:17088532). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (PubMed:17095724). {ECO:0000269|PubMed:12444081, ECO:0000269|PubMed:17088532, ECO:0000269|PubMed:17095724, ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:24981863}.Q9UJG1MSPD1(Motile sperm domain-containing protein 1negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]P53801PTTG?Pituitary tumor-transforming gene 1 protein-interacting proteinSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:10781616}. Nucleus {ECO:0000269|PubMed:10781616}. Note=According to PubMed:10781616, it is found in the cytoplasm and the nucleus.qnegative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902254]; positive regulation of cellular protein catabolic process [GO:1903364]; positive regulation of protein ubiquitination [GO:0031398]; protein import into nucleus [GO:0006606]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]5FUNCTION: May facilitate PTTG1 nuclear translocation.Q13772NCOA4Nuclear receptor coactivator 4androgen receptor signaling pathway [GO:0030521]; male gonad development [GO:0008584]; positive regulation of transcription, DNA-templated [GO:0045893]; response to hormone [GO:0009725]; transcription, DNA-templated [GO:0006351]Wandrogen receptor binding [GO:0050681]; transcription coactivator activity [GO:0003713]FUNCTION: Enhances the androgen receptor transcriptional activity in prostate cancer cells. Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. {ECO:0000269|PubMed:10347167}.Q86UE8TLK2.Serine/threonine-protein kinase tousled-like 2 SUBCELLULAR LOCATION: Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.cell cycle [GO:0007049]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to gamma radiation [GO:0071480]; chromatin modification [GO:0016568]; chromosome segregation [GO:0007059]; intracellular signal transduction [GO:0035556]; negative regulation of autophagy [GO:0010507]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; peptidyl-serine phosphorylation [GO:0018105]; protein phosphorylation [GO:0006468]; regulation of chromatin assembly or disassembly [GO:0001672]fintermediate filament [GO:0005882]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]dFUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:9427565}.P08107HSP71Heat shock 70 kDa protein 1A/1BQ9NZB8MOCS1*Molybdenum cofactor biosynthesis protein 1Sulfur relay system(10)4 iron, 4 sulfur cluster binding [GO:0051539]; cyclic pyranopterin monophosphate synthase activity [GO:0061597]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]Wcytosol [GO:0005829]; molybdopterin synthase complex [GO:0019008]; nucleus [GO:0005634]FUNCTION: Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). {ECO:0000269|PubMed:11891227}.O94888UBXN7UBX domain-containing protein 7<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22537386}.xtranscription factor binding [GO:0008134]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]Gnucleoplasm [GO:0005654]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098]FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. {ECO:0000269|PubMed:22537386}.P07585PGS2Decorin_aging [GO:0007568]; carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate biosynthetic process [GO:0030208]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; glycosaminoglycan metabolic process [GO:0030203]; kidney development [GO:0001822]; organ morphogenesis [GO:0009887]; peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan [GO:0019800]; placenta development [GO:0001890]; positive regulation of autophagy [GO:0010508]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; skeletal muscle tissue development [GO:0007519]; small molecule metabolic process [GO:0044281]; wound healing [GO:0042060]sextracellular matrix binding [GO:0050840]; glycosaminoglycan binding [GO:0005539]; poly(A) RNA binding [GO:0044822]collagen type VI trimer [GO:0005589]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]3FUNCTION: May affect the rate of fibrils formation.P52701MSH6 DNA mismatch repair protein Msh6SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23622243}. Chromosome {ECO:0000269|PubMed:23622243}. Note=Associates with H3K36me3 via its PWWP domain.determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; isotype switching [GO:0045190]; meiotic mismatch repair [GO:0000710]; mismatch repair [GO:0006298]; negative regulation of DNA recombination [GO:0045910]; positive regulation of helicase activity [GO:0051096]; reciprocal meiotic recombination [GO:0007131]; response to UV [GO:0009411]; somatic hypermutation of immunoglobulin genes [GO:0016446]; somatic recombination of immunoglobulin gene segments [GO:0016447]; viral process [G< O:0016032]ATP binding [GO:0005524]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA-dependent ATPase activity [GO:0008094]; guanine/thymine mispair binding [GO:0032137]; methylated histone binding [GO:0035064]; mismatched DNA binding [GO:0030983]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; MutSalpha complex [GO:0032301]; nuclear chromatin [GO:0000790]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]&FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}.Q9NR34MA1C11Mannosyl-oligosaccharide 1,2-alpha-mannosidase ICcellular protein metabolic process [GO:0044267]; N-glycan processing [GO:0006491]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation [GO:0006487]; protein N-linked glycosylation via asparagine [GO:0018279]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of Golgi membrane [GO:0030173]FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc.Q9NU38PGM51Putative PGM5-like protein 1Q6XQN6PNCB$Nicotinate phosphoribosyltransferaseGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17604275}.ZNAD biosynthetic process [GO:0009435]; NAD metabolic process [GO:0019674]; nicotinamide metabolic process [GO:0006769]; nicotinate nucleotide salvage [GO:0019358]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ligase activity [GO:0016874]; nicotinate-nucleotide diphosphorylase (carboxylating) activity [GO:0004514]; nicotinate phosphoribosyltransferase activity [GO:0004516]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]qFUNCTION: Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. {ECO:0000269|PubMed:17604275}.; FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. {ECO:0000250}.Q7Z449CP2U1Cytochrome P450 2U1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14660610}; Multi-pass membrane protein {ECO:0000269|PubMed:14660610}. Microsome membrane {ECO:0000269|PubMed:14660610}.<arachidonic acid metabolic process [GO:0019369]; exogenous drug catabolic process [GO:0042738]; omega-hydroxylase P450 pathway [GO:0097267]; organic acid metabolic process [GO:0006082]; oxidation-reduction process [GO:0055114]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]karomatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; oxygen binding [GO:0019825]; steroid hydroxylase activity [GO:0008395]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Catalyzes the hydroxylation of arachidonic acid, docosahexaenoic acid and other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes. {ECO:0000269|PubMed:14660610}.P29966MARCS-Myristoylated alanine-rich C-kinase substratepSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.energy reserve metabolic process [GO:0006112]; regulation of insulin secretion [GO:0050796]; small molecule metabolic process [GO:0044281]Dactin filament binding [GO:0051015]; calmodulin binding [GO:0005516]actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; centrosome [GO:0005813]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; germinal vesicle [GO:0042585]; plasma membrane [GO:0005886]FUNCTION: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.Q96DX7TRI44&Tripartite motif-containing protein 44FUNCTION: May play a role in the process of differentiation and maturation of neuronal cells (By similarity). May regulate the activity of TRIM17. {ECO:0000250, ECO:0000269|PubMed:19358823}.P00813ADAAdenosine deaminaseSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side. Cell junction. Cytoplasmic vesicle lumen {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion.adenosine catabolic process [GO:0006154]; aging [GO:0007568]; dATP catabolic process [GO:0046061]; deoxyadenosine catabolic process [GO:0006157]; embryonic digestive tract development [GO:0048566]; germinal center B cell differentiation [GO:0002314]; histamine secretion [GO:0001821]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; negative regulation of circadian sleep/wake cycle, non-REM sleep [GO:0042323]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mature B cell apoptotic process [GO:0002906]; negative regulation of mucus secretion [GO:0070256]; negative regulation of penile erection [GO:0060407]; negative regulation of thymocyte apoptotic process [GO:0070244]; nucleobase-containing small molecule metabolic process [GO:0055086]; Peyer's patch development [GO:0048541]; placenta development [GO:0001890]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of germinal center formation [GO:0002636]; positive regulation of heart rate [GO:0010460]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of T cell differentiation in thymus [GO:< 0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide salvage [GO:0032261]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; regulation of cell-cell adhesion mediated by integrin [GO:0033632]; response to drug [GO:0042493]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to morphine [GO:0043278]; response to vitamin E [GO:0033197]; small molecule metabolic process [GO:0044281]; T cell activation [GO:0042110]; trophectodermal cell differentiation [GO:0001829]; xanthine biosynthetic process [GO:0046111]padenosine deaminase activity [GO:0004000]; purine nucleoside binding [GO:0001883]; zinc ion binding [GO:0008270]{cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle lumen [GO:0060205]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion. {ECO:0000269|PubMed:11772392}.Q6WKZ4RFIP1"Rab11 family-interacting protein 1SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15280022, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206}. Note=Rab11A rather than Rab4A mediates localization in the endocytic recycling compartment (ERC).; SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle, phagosome membrane. Note=Membrane-bound (isoform 2). Colocalizes with Rab11A at phagosomes (isoform 2).negative regulation of adiponectin secretion [GO:0070164]; protein transport [GO:0015031]; regulated secretory pathway [GO:0045055]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; phagocytic vesicle membrane [GO:0030670]; recycling endosome [GO:0055037])FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. {ECO:0000269|PubMed:11786538, ECO:0000269|PubMed:15181150, ECO:0000269|PubMed:15355514, ECO:0000269|PubMed:16920206}.O60312AT10A,Probable phospholipid-transporting ATPase VAintracellular protein transport [GO:0006886]; ion transmembrane transport [GO:0034220]; phospholipid translocation [GO:0045332]; regulation of cell shape [GO:0008360]; transmembrane transport [GO:0055085]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]Q9BRD0BUD13 BUD13 homologRmRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]Hnucleoplasm [GO:0005654]; nucleus [GO:0005634]; RES complex [GO:0070274]O95163ELP1Elongator complex protein 1chromatin organization [GO:0006325]; immune response [GO:0006955]; positive regulation of cell migration [GO:0030335]; protein complex assembly [GO:0006461]; protein phosphorylation [GO:0006468]; regulation of protein kinase activity [GO:0045859]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; signal transduction [GO:0007165]; transcription elongation from RNA polymerase II promoter [GO:0006368]]phosphorylase kinase regulator activity [GO:0008607]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; Elongator holoenzyme complex [GO:0033588]; histone acetyltransferase complex [GO:0000123]; nucleolus [GO:0005730]; transcription elongation factor complex [GO:0008023]FUNCTION: May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK).; FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration. Involved in neurogenesis (By similarity). Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (By similarity). {ECO:0000250|UniProtKB:Q7TT37}.O00308WWP2+NEDD4-like E3 ubiquitin-protein ligase WWP2YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:20858735}.cellular protein modification process [GO:0006464]; negative regulation of gene expression [GO:0010629]; negative regulation of protein transport [GO:0051224]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transporter activity [GO:0032410]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of ion transmembrane transport [GO:0034765]; regulation of membrane potential [GO:0042391]; regulation of potassium ion transmembrane transporter activity [GO:1901016]; viral entry into host cell [GO:0046718]Gligase activity [GO:0016874]; RNA polymerase II transcription factor binding [GO:0001085]; RNA polymerase II transcription factor binding transcription activator activity [GO:0001190]; transcription factor binding [GO:0008134]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900}.Q969G5PRDBP&Protein kinase C delta-binding protein?SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91VJ2}.circadian regulation of gene expression [GO:0032922]; cortical actin cytoskeleton organization [GO:0030866]; negative regulation of fermentation [GO:1901003]; negative regulation of protein kinase B signaling [GO:0051898]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]%protein kinase C binding [GO:0005080]Jcaveola [GO:0005901]; cytoplasm [GO:0005737]; protein complex [GO:0043234]NFUNCTION: Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2. Seems to have an immune potentiation function. {ECO:0000250|UniProtKB:Q91VJ2, ECO:0000250|UniProtKB:Q9Z1H9}.P19419ELK1#ETS domain-containing protein Elk-1cell differentiation [GO:0030154]; cellular response to gamma radiation [GO:0071480]; cellular response to testoste< rone stimulus [GO:0071394]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of neuron death [GO:1901216]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; response to light stimulus [GO:0009416]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; double-stranded DNA binding [GO:0003690]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]axon terminus [GO:0043679]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Stimulates transcription. Binds to purine-rich DNA sequences. Can form a ternary complex with the serum response factor and the ETS and SRF motifs of the fos serum response element.Q7L311ARMX2.Armadillo repeat-containing X-linked protein 2Q9Y561LRP123Low-density lipoprotein receptor-related protein 12 Receptors(21)SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12809483}; Single-pass type I membrane protein {ECO:0000269|PubMed:12809483}. Membrane, coated pit {ECO:0000269|PubMed:12809483}.endocytosis [GO:0006897]; receptor-mediated endocytosis [GO:0006898]; regulation of growth [GO:0040008]; signal transduction [GO:0007165]6low-density lipoprotein receptor activity [GO:0005041]xcoated pit [GO:0005905]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor. {ECO:0000269|PubMed:12809483}.Q16678CP1B1Cytochrome P450 1B1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Mitochondrion {ECO:0000250}.angiogenesis [GO:0001525]; arachidonic acid metabolic process [GO:0019369]; blood vessel morphogenesis [GO:0048514]; cell adhesion [GO:0007155]; cellular aromatic compound metabolic process [GO:0006725]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic cyclic compound [GO:0071407]; collagen fibril organization [GO:0030199]; endothelial cell-cell adhesion [GO:0071603]; endothelial cell migration [GO:0043542]; epoxygenase P450 pathway [GO:0019373]; estrogen metabolic process [GO:0008210]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; membrane lipid catabolic process [GO:0046466]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; nitric oxide biosynthetic process [GO:0006809]; omega-hydroxylase P450 pathway [GO:0097267]; oxidation-reduction process [GO:0055114]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JAK-STAT cascade [GO:0046427]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of reactive oxygen species metabolic process [GO:2000377]; response to toxic substance [GO:0009636]; retinal blood vessel morphogenesis [GO:0061304]; retinal metabolic process [GO:0042574]; retinol metabolic process [GO:0042572]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]; sterol metabolic process [GO:0016125]; toxin metabolic process [GO:0009404]; trabecular meshwork development [GO:0002930]; visual perception [GO:0007601]; xenobiotic metabolic process [GO:0006805]earomatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; oxygen binding [GO:0019825]Gendoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739] FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. {ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:15258110, ECO:0000269|PubMed:22888116, ECO:0000269|PubMed:23821647}.Q9NX61T161ATransmembrane protein 161Acellular response to oxidative stress [GO:0034599]; cellular response to UV [GO:0034644]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; positive regulation of DNA repair [GO:0045739]; response to retinoic acid [GO:0032526]FUNCTION: May play a role in protection against oxidative stress. Overexpression leads to reduced levels of oxidant-induced DNA damage and apoptosis. {ECO:0000269|PubMed:16551573}.P60520GBRL2:Gamma-aminobutyric acid receptor-associated protein-like 2SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22311637}.autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to nitrogen starvation [GO:0006995]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane fusion [GO:0061025]; mitochondrion degradation [GO:0000422]; negative regulation of proteasomal protein catabolic process [GO:1901799]; nucleophagy [GO:0044804]; positive regulation of ATPase activity [GO:0032781]; protein transport [GO:0015031]ATPase binding [GO:0051117]; beta-tubulin binding [GO:0048487]; GABA receptor binding [GO:0050811]; microtubule binding [GO:0008017]; SNARE binding [GO:0000149]?autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; Golgi memb< rane [GO:0000139]; intracellular [GO:0005622]; pre-autophagosomal structure [GO:0000407]FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000250, ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}.Q9H2C2ARV1 Protein ARV1bile acid metabolic process [GO:0008206]; cholesterol biosynthetic process [GO:0006695]; cholesterol transport [GO:0030301]; intracellular sterol transport [GO:0032366]; regulation of cholesterol metabolic process [GO:0090181]; regulation of plasma membrane sterol distribution [GO:0097036]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]; sterol metabolic process [GO:0016125]cortical endoplasmic reticulum [GO:0032541]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]EFUNCTION: May act as a mediator of sterol homeostasis. {ECO:0000305}.Q96QR8PURB*Transcriptional activator protein Pur-beta;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1448097}.cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; regulation of myeloid cell differentiation [GO:0045637]; transcription, DNA-templated [GO:0006351]double-stranded DNA binding [GO:0003690]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; single-stranded DNA binding [GO:0003697]; transcription factor binding [GO:0008134]]DNA replication factor A complex [GO:0005662]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts. Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250}.Q7L4I2RSRC2*Arginine/serine-rich coiled-coil protein 2O60942MCE1mRNA-capping enzyme7-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; polynucleotide 5' dephosphorylation [GO:0098507]; RNA processing [GO:0006396]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]KGTP binding [GO:0005525]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; protein tyrosine phosphatase activity [GO:0004725]; RNA guanylyltransferase activity [GO:0008192]; triphosphatase activity [GO:0050355]FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus. {ECO:0000269|PubMed:21636784, ECO:0000269|PubMed:9473487, ECO:0000269|PubMed:9512541}.O00255MEN1MeninSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12874027}. Note=Concentrated in nuclear body-like structures. Relocates to the nuclear matrix upon gamma irradiation.brain development [GO:0007420]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to glucose stimulus [GO:0071333]; cellular response to peptide hormone stimulus [GO:0071375]; decidualization [GO:0046697]; DNA repair [GO:0006281]; gene expression [GO:0010467]; histone lysine methylation [GO:0034968]; MAPK cascade [GO:0000165]; mitotic cell cycle [GO:0000278]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of JNK cascade [GO:0046329]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of telomerase activity [GO:0051974]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; osteoblast development [GO:0002076]; positive regulation of protein binding [GO:0032092]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of activin receptor signaling pathway [GO:0032925]; regulation of type B pancreatic cell proliferation [GO:0061469]; response to gamma radiation [GO:0010332]; response to UV [GO:0009411]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; type B pancreatic cell differentiation [GO:0003309]=chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; protein binding, bridging [GO:0030674]; protein N-terminus binding [GO:0047485]; R-SMAD binding [GO:0070412]; transcription regulatory region DNA binding [GO:0044212]; Y-form DNA binding [GO:0000403]chromatin [GO:0000785]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone methyltransferase complex [GO:0035097]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]AFUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair. {ECO:0000250, ECO:0000269|PubMed:11274402, ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727}.Q96Q11TRNT10CCA tRNA nucleotidyltransferase 1, mitochondrialprotein targeting to mitochondrion [GO:0006626]; tRNA 3'-end processing [GO:0042780]; tRNA 3'-terminal CCA addition [GO:0001680]"ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity [GO:0052929]; ATP binding [GO:0005524]; CTP:3'-cytidine-tRNA cytidylyltransferase activity [GO:0052928]; CTP:tRNA cytidylyltransferase activity [GO:0052927]< ; tRNA adenylyltransferase activity [GO:0004810]; tRNA binding [GO:0000049]6intracellular [GO:0005622]; mitochondrion [GO:0005739]dFUNCTION: Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.; FUNCTION: Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro). {ECO:0000269|PubMed:17204286}.Q8WUX9CHMP7%Charged multivesicular body protein 7SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16856878}. Note=Diffused localization, with some punctate distribution, especially in the perinuclear area.5cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; late endosome to vacuole transport [GO:0045324]; membrane organization [GO:0061024]; mitotic metaphase plate congression [GO:0007080]; nucleus organization [GO:0006997]; viral life cycle [GO:0019058]; viral process [GO:0016032]4cytosol [GO:0005829]; ESCRT III complex [GO:0000815]WFUNCTION: Plays a role in the endosomal sorting pathway. {ECO:0000269|PubMed:16856878}.Q9NV88INT9Integrator complex subunit 9<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15684398}.Qcytoplasm [GO:0005737]; integrator complex [GO:0032039]; nucleoplasm [GO:0005654]Q6NTF9RHBD2$Rhomboid domain-containing protein 2{SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]Q9H772GREM2 Gremlin-2BMP signaling pathway [GO:0030509]; cytokine-mediated signaling pathway [GO:0019221]; determination of dorsal identity [GO:0048263]; embryonic body morphogenesis [GO:0010172]; regulation of cytokine activity [GO:0060300]; sequestering of BMP from receptor via BMP binding [GO:0038098]UFUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells (By similarity). {ECO:0000250}.Q8IYS1P20D2)Peptidase M20 domain-containing protein 2<extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]Q9BXR0TGTQueuine tRNA-ribosyltransferaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Weakly associates with mitochondria, possibly via QTRTD1. {ECO:0000250}.Kqueuosine biosynthetic process [GO:0008616]; tRNA modification [GO:0006400]Umetal ion binding [GO:0046872]; queuine tRNA-ribosyltransferase activity [GO:0008479]}FUNCTION: Interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By similarity). {ECO:0000250}.Q8NDT2RB15B Putative RNA-binding protein 15BSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:16129689}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli.mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]kFUNCTION: May function in the regulation of alternative or illicit splicing. {ECO:0000269|PubMed:16129689}.Q9H0E2TOLIPToll-interacting proteinautophagy [GO:0006914]; cell-cell signaling [GO:0007267]; epithelial cell differentiation [GO:0030855]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; leukocyte activation [GO:0045321]; phosphorylation [GO:0016310]; positive regulation of protein sumoylation [GO:0033235]; protein localization to endosome [GO:0036010]; signal transduction [GO:0007165]mkinase binding [GO:0019900]; signal transducer activity [GO:0004871]; Toll-like receptor binding [GO:0035325]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; interleukin-18 receptor complex [GO:0045092]; interleukin-1 receptor complex [GO:0045323]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471][FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity (PubMed:11751856). Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (PubMed:25042851). {ECO:0000269|PubMed:11751856, ECO:0000269|PubMed:25042851}.P02549SPTA1$Spectrin alpha chain, erythrocytic 1FSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.actin filament capping [GO:0051693]; actin filament organization [GO:0007015]; axon guidance [GO:0007411]; hemopoiesis [GO:0030097]; lymphocyte homeostasis [GO:0002260]; plasma membrane organization [GO:0007009]; porphyrin-containing compound biosynthetic process [GO:0006779]; positive regulation of protein binding [GO:0032092]; positive regulation of T cell proliferation [GO:0042102]; regulation of cell shape [GO:0008360]actin cytoskeleton [GO:0015629]; cuticular plate [GO:0032437]; cytosol [GO:0005829]; intrinsic component of the cytoplasmic side of the plasma membrane [GO:0031235]; spectrin [GO:0008091]; spectrin-associated cytoskeleton [GO:0014731]FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.Q96E39RMXL1*RNA binding motif protein, X-linked-like-1mRNA processing [GO:0006397]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; RNA splicing [GO:0008380]}chromatin binding [GO:0003682]; core promoter binding [GO:0001047]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]XFUNCTION: RNA-binding protein which may be involved in pre-mRNA splicing. {ECO:0000250}.Q9NW13RBM28RNA-binding protein 28wSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:17081119, ECO:0000269|Ref.7}.9nucleolus [GO:0005730]; spliceosomal complex [GO:0005681]mFUNCTION: Nucleolar component of the spliceosomal ribonucleoprotein complexes. {ECO:0000269|PubMed:17081119}.Q15678PTN141Tyrosine-protein phosphatase non-receptor type 14SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus. Note=Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane.Llymphangiogenesis [GO:0001946]; negative regulation of cell proliferation [GO:0008285]; peptidyl-tyrosine dephosphorylation [GO:0035335]; protein dephosphorylation [GO:0006470]; regulation of protein export from nucleus [GO:0046825]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]protein tyrosine phosphatase activity [GO:0004725]; receptor tyrosine kinase binding [GO:0030971]; transcription cofactor activity [GO:0003712]acytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth a< nd also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor. {ECO:0000269|PubMed:10934049, ECO:0000269|PubMed:12808048, ECO:0000269|PubMed:17893246, ECO:0000269|PubMed:20826270, ECO:0000269|PubMed:22233626, ECO:0000269|PubMed:22525271, ECO:0000269|PubMed:22948661}.Q9NXN4GDAP28Ganglioside-induced differentiation-associated protein 2Q9Y2L1RRP44!Exosome complex exonuclease RRP449SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus. Note=Predominantly located in the nucleus. According to PubMed:12429849, found in the nucleolus and according to PubMed:20531386, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of DIS3."CUT catabolic process [GO:0071034]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA catabolic process [GO:0006402]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; positive regulation of GTPase activity [GO:0043547]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]3'-5'-exoribonuclease activity [GO:0000175]; endonuclease activity [GO:0004519]; guanyl-nucleotide exchange factor activity [GO:0005085]; RNA binding [GO:0003723]cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; membrane [GO:0016020]; nuclear exosome (RNase complex) [GO:0000176]; nucleoplasm [GO:0005654]FUNCTION: Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities. {ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20531386}.Q9UJX4APC5$Anaphase-promoting complex subunit 5Q86YV5SG223Tyrosine-protein kinase SgK223]ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]P52824DGKQDiacylglycerol kinase thetaSUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasm, cytoskeleton. Nucleus. Nucleus speckle. Note=Translocates to the nucleus in response to thrombin stimulation (By similarity). Translocates to the plasma membrane in response to steroid hormone receptor stimulation. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH. {ECO:0000250}.blood coagulation [GO:0007596]; cAMP-mediated signaling [GO:0019933]; G-protein coupled receptor signaling pathway [GO:0007186]; platelet activation [GO:0030168]; protein kinase C-activating G-protein coupled receptor signaling pathway [GO:0007205]; protein kinase C signaling [GO:0070528]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to ATP [GO:0033198]; thrombin receptor signaling pathway [GO:0070493]activating transcription factor binding [GO:0033613]; ATP binding [GO:0005524]; diacylglycerol kinase activity [GO:0004143]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; phospholipase binding [GO:0043274]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor (By similarity). May be involved in cAMP-induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:17664281}.Q9ULX9MAFFTranscription factor MafFblood coagulation [GO:0007596]; in utero embryonic development [GO:0001701]; parturition [GO:0007567]; regulation of epidermal cell differentiation [GO:0045604]; skeletal muscle cell differentiation [GO:0035914]; transcription from RNA polymerase II promoter [GO:0006366]tsequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700] FUNCTION: Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition. Since it lacks a putative transactivation domain, it may behave as a transcriptional repressor when it dimerize among himself. May also serve as a transcriptional activator by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. May be involved in the cellular stress response.O95755RAB36Ras-related protein Rab-36=SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.Q03111ENL Protein ENLnegative regulation of protein kinase activity [GO:0006469]; regulation of transcription, DNA-templated [GO:0006355]; transcription from RNA polymerase II promoter [GO:0006366]cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription elongation factor complex [GO:0008023]FUNCTION: Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948}.Q3MHD2LSM12Protein LSM12 homologQ9NVX0HAUS2"HAUS augmin-like complex subunit 2cell division [GO:0051301]; centrosome organization [GO:0051297]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; organelle organization [GO:0006996]; spindle assembly [GO:0051225]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; HAUS complex [GO:0070652]; nucleoplasm [GO:0005654]; spindle microtubule [GO:0005876]Q02388CO7A1Collagen alpha-1(VII) chaincell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; epidermis development [GO:0008544]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]basement membrane [GO:0005604]; collagen type VII trimer [GO:0005590]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]FUNCTION: Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.P35249RFC4Replication < factor C subunit 4ucytoplasm [GO:0005737]; DNA replication factor C complex [GO:0005663]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template.P49418AMPH AmphiphysinSUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.~endocytosis [GO:0006897]; learning [GO:0007612]; synaptic transmission [GO:0007268]; synaptic vesicle endocytosis [GO:0048488]actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; leading edge membrane [GO:0031256]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]FUNCTION: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.Q9P121NTRI Neurotrimincell adhesion [GO:0007155]; neuron recognition [GO:0008038]; regulation of neurogenesis [GO:0050767]; single organismal cell-cell adhesion [GO:0016337]anchored component of membrane [GO:0031225]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; plasma membrane [GO:0005886](FUNCTION: Neural cell adhesion molecule.Q8NBJ7SUMF2Sulfatase-modifying factor 2mSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010}.ecellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]FUNCTION: Lacks formyl-glycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1. {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010}.Q9BQG2NUD12'Peroxisomal NADH pyrophosphatase NUDT12?SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12790796}.GNAD catabolic process [GO:0019677]; NADP catabolic process [GO:0006742]tmetal ion binding [GO:0046872]; NAD+ diphosphatase activity [GO:0000210]; NADH pyrophosphatase activity [GO:0035529]-nucleus [GO:0005634]; peroxisome [GO:0005777]VFUNCTION: Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle. {ECO:0000269|PubMed:12790796}.Q99584S10ADProtein S100-A13uSUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is mediated by exposure to stress and requires copper ions.lcytokine secretion [GO:0050663]; interleukin-1 alpha secretion [GO:0050703]; mast cell degranulation [GO:0043303]; positive regulation of cell proliferation [GO:0008284]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; regulation of cell shape [GO:0008360]; response to copper ion [GO:0046688]; response to electrical stimulus [GO:0051602]calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; fibroblast growth factor binding [GO:0017134]; lipid binding [GO:0008289]; protein homodimerization activity [GO:0042803]; RAGE receptor binding [GO:0050786]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mast cell granule [GO:0042629]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity). {ECO:0000250}.Q8N3V7SYNPO SynaptopodinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Localized at the tight junction of cells. In brain, localized to the postsynaptic densities and in the perikarya. Associated with dendritic spines of a subset of synapses (By similarity). {ECO:0000250}.tpositive regulation of actin filament bundle assembly [GO:0032233]; regulation of stress fiber assembly [GO:0051492]actin cytoskeleton [GO:0015629]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; stress fiber [GO:0001725]EFUNCTION: Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity (By similarity). {ECO:0000250}.Q8TAL6FIBIN!Fin bud initiation factor homologSUBCELLULAR LOCATION: Secreted {ECO:0000250}. Golgi apparatus {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:21615908}.Q6ZWJ1STXB4Syntaxin-binding protein 4cellular response to DNA damage stimulus [GO:0006974]; glucose transport [GO:0015758]; insulin receptor signaling pathway [GO:0008286]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of keratinocyte proliferation [GO:0010838]; protein stabilization [GO:0050821]; protein targeting [GO:0006605]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]FUNCTION: Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity). {ECO:0000250}.Q16611BAK"Bcl-2 homologous antagonist/killer activation of cysteine-type endopeptidase activity [GO:0097202]; activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c [GO:0008635]; activation of signaling protein activity involved in unfolded protein response [GO:0006987]; aging [GO:0007568]; apoptotic process [GO:0006915]; apoptotic process involved in patterning of blood vessels [GO:1902262]; apoptotic signaling pathway [GO:0097190]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; B cell negative selection [GO:0002352]; blood vessel remodeling [GO:0001974]; brain development [GO:0007420]; cell proliferation [GO:0008283]; cellular response to mechanical stimulus [GO:0071260]; cellular response to UV [GO:0034644]; cytolysis [GO:0019835]; endocrine pancreas development [GO:0031018]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fibroblast apoptotic process [GO:0044346]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; limb morphogenesis [GO:0035108]; mitocho< ndrial fusion [GO:0008053]; myeloid cell homeostasis [GO:0002262]; negative regulation of cell proliferation [GO:0008285]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; negative regulation of gene expression [GO:0010629]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; organ regeneration [GO:0031100]; positive regulation of apoptotic process [GO:0043065]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of proteolysis [GO:0045862]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; post-embryonic camera-type eye morphogenesis [GO:0048597]; programmed cell death [GO:0012501]; regulation of cell cycle [GO:0051726]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of protein heterodimerization activity [GO:0043497]; regulation of protein homodimerization activity [GO:0043496]; release of cytochrome c from mitochondria [GO:0001836]; response to drug [GO:0042493]; response to ethanol [GO:0045471]; response to fungus [GO:0009620]; response to gamma radiation [GO:0010332]; response to hydrogen peroxide [GO:0042542]; response to mycotoxin [GO:0010046]; response to organic cyclic compound [GO:0014070]; response to UV-C [GO:0010225]; thymocyte apoptotic process [GO:0070242]; vagina development [GO:0060068]identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; integral component of mitochondrial outer membrane [GO:0031307]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; pore complex [GO:0046930]FFUNCTION: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis. {ECO:0000269|PubMed:17157251, ECO:0000269|PubMed:8521816}.P55769NH2L1NHP2-like protein 1SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:12429849, ECO:0000269|Ref.7}. Note=Concentrated in the dense fibrillar component of the nucleolus.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ribosome biogenesis [GO:0042254]; RNA splicing [GO:0008380]box C/D snoRNA binding [GO:0034512]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; U3 snoRNA binding [GO:0034511]; U4 snRNA binding [GO:0030621]box C/D snoRNP complex [GO:0031428]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; spliceosomal complex [GO:0005681]FUNCTION: Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding. {ECO:0000269|PubMed:10545122, ECO:0000269|PubMed:17412961}.Q9BX40LS14BProtein LSM14 homolog BYmulticellular organismal development [GO:0007275]; regulation of translation [GO:0006417]&ribonucleoprotein complex [GO:0030529]HFUNCTION: May play a role in control of mRNA translation. {ECO:0000250}.P12111CO6A3Collagen alpha-3(VI) chainaxon guidance [GO:0007411]; cell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; muscle organ development [GO:0007517]Hcollagen type VI trimer [GO:0005589]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; proteinaceous extracellular matrix [GO:0005578]; sarcolemma [GO:0042383]P51946CCNHCyclin-H7-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein phosphorylation [GO:0006468]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]ncyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; kinase activity [GO:0016301]cyclin-dependent protein kinase activating kinase holoenzyme complex [GO:0019907]; holo TFIIH complex [GO:0005675]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; TFIIK complex [GO:0070985]FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:7533895}.P57081WDR4AtRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4]SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:15861136}.hRNA (guanine-N7)-methylation [GO:0036265]; tRNA methylation [GO:0030488]; tRNA modification [GO:0006400]FUNCTION: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:12403464}.Q9BWH6RPAP1&RNA polymerase II-associated protein 1:transcription from RNA polymerase II promoter [GO:0006366]AFUNCTION: Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. Required for interaction of the RNA polymerase II complex with acetylated histone H3. {ECO:0000269|PubMed:17643375}.P52298NCBP2%Nuclear cap-binding protein subunit 2cSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8601613}. Cytoplasm {ECO:0000269|PubMed:8601613}.)7-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of mRNA 3'-end processing [GO:0031442]; positive regulation of RNA export from nucleus< [GO:0046833]; positive regulation of viral transcription [GO:0050434]; pre-mRNA cleavage required for polyadenylation [GO:0098789]; regulation of translational initiation [GO:0006446]; RNA splicing [GO:0008380]; snRNA export from nucleus [GO:0006408]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA 7-methylguanosine cap binding [GO:0000340]; RNA cap binding [GO:0000339]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mRNA cap binding complex [GO:0005845]; nuclear cap binding complex [GO:0005846]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]KFUNCTION: Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. {ECO:0000269|PubMed:11551508, ECO:0000269|PubMed:15361857, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:17363367, ECO:0000269|PubMed:17873884, ECO:0000269|PubMed:18369367, ECO:0000269|PubMed:19632182}.Q9UMX1SUFUSuppressor of fused homolog STK36/FuSu(2)eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559945}. Nucleus {ECO:0000269|PubMed:10559945}.cytoplasmic sequestering of transcription factor [GO:0042994]; heart looping [GO:0001947]; multicellular organismal development [GO:0007275]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000059]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:1901621]; negative regulation of transcription factor import into nucleus [GO:0042992]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neural tube closure [GO:0001843]; proteolysis [GO:0006508]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; skin development [GO:0043588]; smoothened signaling pathway involved in spinal cord motor neuron cell fate specification [GO:0021776]; smoothened signaling pathway involved in ventral spinal cord interneuron specification [GO:0021775]protein kinase binding [GO:0019901]; signal transducer activity [GO:0004871]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; primary cilium [GO:0072372]`FUNCTION: Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes (PubMed:15367681, PubMed:24311597, PubMed:24217340). Down-regulates GLI2-mediated transactivation of target genes (PubMed:24311597, PubMed:24217340). Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein (PubMed:10806483, PubMed:24217340). Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). Required for normal embryonic development. Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity). {ECO:0000250|UniProtKB:Q9Z0P7, ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:10564661, ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:12068298, ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15367681, ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597}.Q9GZN4BSSP4 Brain-specific serine protease 4=SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11602603}.FUNCTION: Preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. {ECO:0000269|PubMed:11602603}.P13473LAMP2+Lysosome-associated membrane glycoprotein 2WSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}. Endosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane.blood coagulation [GO:0007596]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; protein stabilization [GO:0050821]Uextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088]|FUNCTION: Implicated in tumor cell metastasis. May function in protection of the lysosomal membrane from autodigestion, maintenance of the acidic environment of the lysosome, adhesion when expressed on the cell surface (plasma membrane), and inter- and intracellular signal transduction. Protects cells from the toxic effects of methylating mutagens. {ECO:0000269|PubMed:8407947}.Q15596NCOA2Nuclear receptor coactivator 2bile acid and bile salt transport [GO:0015721]; bile acid metabolic proce< ss [GO:0008206]; cellular lipid metabolic process [GO:0044255]; cellular response to hormone stimulus [GO:0032870]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; locomotor rhythm [GO:0045475]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of glucose metabolic process [GO:0010906]; regulation of transcription, DNA-templated [GO:0006355]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]vchromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; ligand-dependent nuclear receptor binding [GO:0016922]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; nuclear hormone receptor binding [GO:0035257]; thyroid hormone receptor coactivator activity [GO:0030375]; transcription coactivator activity [GO:0003713]FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:9430642}.Q9NRA0SPHK2Sphingosine kinase 2jSUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Membrane.; SUBCELLULAR LOCATION: Isoform 2: Lysosome membrane.Fblood vessel development [GO:0001568]; brain development [GO:0007420]; cell proliferation [GO:0008283]; female pregnancy [GO:0007565]; lipid phosphorylation [GO:0046834]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell proliferation [GO:0008284]; small molecule metabolic process [GO:0044281]; sphinganine-1-phosphate biosynthetic process [GO:0006669]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingosine-1-phosphate signaling pathway [GO:0003376]; sphingosine biosynthetic process [GO:0046512]ATP binding [GO:0005524]; D-erythro-sphingosine kinase activity [GO:0017050]; Ras GTPase binding [GO:0017016]; sphinganine kinase activity [GO:0008481]; sphingosine-1-phosphate receptor activity [GO:0038036]Lcytosol [GO:0005829]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]5FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides. {ECO:0000269|PubMed:19168031}.Q9UI10EI2BD2Translation initiation factor eIF-2B subunit deltacellular protein metabolic process [GO:0044267]; cellular response to stimulus [GO:0051716]; gene expression [GO:0010467]; myelination [GO:0042552]; negative regulation of translational initiation [GO:0045947]; negative regulation of translational initiation in response to stress [GO:0032057]; oligodendrocyte development [GO:0014003]; ovarian follicle development [GO:0001541]; positive regulation of GTPase activity [GO:0043547]; regulation of translation [GO:0006417]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to peptide hormone [GO:0043434]; translation [GO:0006412]; translational initiation [GO:0006413]gtranslation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369]P52292IMA1Importin subunit alpha-1cSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus {ECO:0000269|PubMed:7604027}.cytokine-mediated signaling pathway [GO:0019221]; DNA metabolic process [GO:0006259]; NLS-bearing protein import into nucleus [GO:0006607]; regulation of DNA recombination [GO:0000018]; viral process [GO:0016032]histone deacetylase binding [GO:0042826]; nuclear localization sequence binding [GO:0008139]; poly(A) RNA binding [GO:0044822]; protein transporter activity [GO:0008565]GFUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.Q8IXZ2ZC3H3,Zinc finger CCCH domain-containing protein 3mRNA polyadenylation [GO:0006378]; poly(A)+ mRNA export from nucleus [GO:0016973]; regulation of mRNA export from nucleus [GO:0010793]Q7Z6L1TCPR13Tectonin beta-propeller repeat-containing protein 1SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane. Lysosome membrane. Note=Localizes to Lysosome membranes, and binds PtdIns(3)P at the surface of autophagosome. Localizes to autolysosomes, a vesicle formed by the fusion between autophagosomes and lysosomes.9autophagosome fusion [GO:0000046]; autophagy [GO:0006914]FUNCTION: Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. {ECO:0000269|PubMed:21575909, ECO:0000269|PubMed:22342342}.Q9Y6W3CAN7 Calpain-7\positive regulation of epithelial cell migration [GO:0010634]; self proteolysis [GO:0097264]calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; endopeptidase activity [GO:0004175]; MIT domain binding [GO:0090541]HFUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000250}.Q8WX92NELFBNegative elongation factor B<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739404}.Kcytoplasm [GO:0005737]; NELF complex [GO:0032021]; nucleoplasm [GO:0005654]FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. May be able to induce chromatin unfolding. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12612062}.Q9NXR1NDE1+Nuclear distribution protein nudE homolog 1@SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis.cell division [GO:0051301]; cell migration [GO:0016477]; centrosome duplication [GO:0051298]; centrosome localization [GO:0051642]; cerebral cortex development [GO:0021987]; chromosome segregation [GO:0007059]; establ< ishment of chromosome localization [GO:0051303]; establishment of mitotic spindle orientation [GO:0000132]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; mitotic centrosome separation [GO:0007100]; neuroblast proliferation [GO:0007405]; neuron migration [GO:0001764]; organelle organization [GO:0006996]; small GTPase mediated signal transduction [GO:0007264]; vesicle transport along microtubule [GO:0047496] centrosome [GO:0005813]; cleavage furrow [GO:0032154]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle pole centrosome [GO:0031616]jFUNCTION: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. {ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:21529752}.Q9Y606TRUA,tRNA pseudouridine synthase A, mitochondrialSUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:17056637}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:17056637}.|positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; tRNA pseudouridine synthesis [GO:0031119]ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; poly(A) RNA binding [GO:0044822]; pseudouridine synthase activity [GO:0009982]; pseudouridylate synthase activity [GO:0004730]mitochondrion [GO:0005739]; nuclear chromatin [GO:0000790]; nucleolus [GO:0005730]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]HFUNCTION: Converts specific uridines to PSI in a number of tRNA substrates. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Involved in regulation of nuclear receptor activity possibly through pseudouridylation of SRA1 RNA (By similarity). {ECO:0000250}.Q8IV03LUR1L#Leucine rich adaptor protein 1-likeQ9NSY1BMP2KBMP-2-inducible protein kinase.regulation of bone mineralization [GO:0030500]|ATP binding [GO:0005524]; phosphatase regulator activity [GO:0019208]; protein serine/threonine kinase activity [GO:0004674]8FUNCTION: May be involved in osteoblast differentiation.Q9H814PHAX)Phosphorylated adapter RNA export proteinSUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body. Cytoplasm. Note=Located in the nucleoplasm and Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies.gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; protein transport [GO:0015031]; snRNA export from nucleus [GO:0006408]; spliceosomal snRNP assembly [GO:0000387]>RNA binding [GO:0003723]; toxic substance binding [GO:0015643]Cajal body [GO:0015030]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]TFUNCTION: A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Plays also a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA. {ECO:0000250, ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:15574333}.Q5XXA6ANO1 Anoctamin-1SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm. Note=Cytoplasmic localization seen in neoplastic cells of head and neck squamous cell carcinoma (HNSCC) tumors.cation transmembrane transport [GO:0098655]; cation transport [GO:0006812]; cellular response to heat [GO:0034605]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; iodide transport [GO:0015705]; ion transmembrane transport [GO:0034220]; multicellular organismal development [GO:0007275]; phospholipase C-activating G-protein coupled receptor signaling pathway [GO:0007200]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; regulation of anion transmembrane transport [GO:1903959]; regulation of membrane potential [GO:0042391]; transmembrane transport [GO:0055085]calcium activated cation channel activity [GO:0005227]; chloride channel activity [GO:0005254]; intracellular calcium activated chloride channel activity [GO:0005229]; iodide transmembrane transporter activity [GO:0015111]; voltage-gated chloride channel activity [GO:0005247]apical plasma membrane [GO:0016324]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]@FUNCTION: Calcium-activated chloride channel (CaCC) which plays a role in transepithelial anion transport and smooth muscle contraction. Required for the normal functioning of the interstitial cells of Cajal (ICCs) which generate electrical pacemaker activity in gastrointestinal smooth muscles. Acts as a major contributor to basal and stimulated chloride conductance in airway epithelial cells and plays an important role in tracheal cartilage development. {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21984732, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:22946059}.P55196AFADAfadinZSUBCELLULAR LOCATION: Cell junction, adherens junction. Note=Not found at cell-matrix AJs.Qadherens junction organization [GO:0034332]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell-cell signaling [GO:0007267]; cell junction assembly [GO:0034329]; establishment of endothelial intestinal barrier [GO:0090557]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]Hprotein C-terminus binding [GO:0008022]; Ras GTPase binding [GO:0017016]apical part of cell [GO:0045177]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]0FUNCTION: Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytos< keleton.Q96I24FUBP3&Far upstream element-binding protein 3/positive regulation of gene expression [GO:0010628]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]'poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]sFUNCTION: May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression.Q8NBJ9SIDT2"SID1 transmembrane family member 2SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319}.Ecell morphogenesis [GO:0000902]; dsRNA transport [GO:0033227]; glucose homeostasis [GO:0042593]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; response to glucose [GO:0009749]; type B pancreatic cell development [GO:0003323]; type B pancreatic cell proliferation [GO:0044342]3RNA transmembrane transporter activity [GO:0051033]Q58A45PAN38PAB-dependent poly(A)-specific ribonuclease subunit PAN3SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:18625844}.deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606]; protein targeting [GO:0006605]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]]cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; PAN complex [GO:0031251]FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with PABP and to miRNA targets via its interaction with GW182 family proteins. {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:23932717}.P30040ERP29)Endoplasmic reticulum resident protein 29activation of MAPK activity [GO:0000187]; intracellular protein transport [GO:0006886]; negative regulation of gene expression [GO:0010629]; negative regulation of protein secretion [GO:0050709]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; protein folding [GO:0006457]; protein secretion [GO:0009306]; protein unfolding [GO:0043335]; regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902235]Nchaperone binding [GO:0051087]; protein homodimerization activity [GO:0042803]cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; membrane [GO:0016020]; smooth endoplasmic reticulum [GO:0005790]; transport vesicle [GO:0030133]FUNCTION: Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.P43246MSH2 DNA mismatch repair protein Msh2B cell differentiation [GO:0030183]; B cell mediated immunity [GO:0019724]; cell cycle arrest [GO:0007050]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; germ cell development [GO:0007281]; intra-S DNA damage checkpoint [GO:0031573]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; in utero embryonic development [GO:0001701]; isotype switching [GO:0045190]; maintenance of DNA repeat elements [GO:0043570]; male gonad development [GO:0008584]; meiotic gene conversion [GO:0006311]; meiotic mismatch repair [GO:0000710]; mismatch repair [GO:0006298]; negative regulation of DNA recombination [GO:0045910]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of reciprocal meiotic recombination [GO:0045128]; oxidative phosphorylation [GO:0006119]; positive regulation of helicase activity [GO:0051096]; postreplication repair [GO:0006301]; reciprocal meiotic recombination [GO:0007131]; response to UV-B [GO:0010224]; response to X-ray [GO:0010165]; somatic hypermutation of immunoglobulin genes [GO:0016446]; somatic recombination of immunoglobulin gene segments [GO:0016447]ATP binding [GO:0005524]; centromeric DNA binding [GO:0019237]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; double-strand/single-strand DNA junction binding [GO:0000406]; enzyme binding [GO:0019899]; guanine/thymine mispair binding [GO:0032137]; heteroduplex DNA loop binding [GO:0000404]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; Y-form DNA binding [GO:0000403]membrane [GO:0016020]; MutSalpha complex [GO:0032301]; MutSbeta complex [GO:0032302]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:17611581, ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679, ECO:0000269|PubMed:9822680}.Q08AF3SLFN5Schlafen family member 5OFUNCTION: May have a role in hematopoietic cell differentiation. {ECO:0000250}.O14683P5I11&Tumor protein p53-inducible protein 11Wnegative regulation of cell proliferation [GO:0008285]; response to stress [GO:0006950]P37108SRP14*Signal recognition particle 14 kDa protein2cellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; gen< e expression [GO:0010467]; protein targeting to ER [GO:0045047]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]7S RNA binding [GO:0008312]; endoplasmic reticulum signal peptide binding [GO:0030942]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intercellular bridge [GO:0045171]; nucleolus [GO:0005730]; nucleus [GO:0005634]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]Q14457BECN1Beclin-1PSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88597}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19050071}; Peripheral membrane protein {ECO:0000269|PubMed:19050071}. Endosome membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Mitochondrion membrane {ECO:0000269|PubMed:23878393}; Peripheral membrane protein {ECO:0000269|PubMed:23878393}. Endosome {ECO:0000250|UniProtKB:O88597}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells (By similarity). {ECO:0000250|UniProtKB:O88597, ECO:0000269|PubMed:19050071}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; beta-amyloid metabolic process [GO:0050435]; cellular defense response [GO:0006968]; cellular response to glucose starvation [GO:0042149]; cellular response to nitrogen starvation [GO:0006995]; CVT pathway [GO:0032258]; cytokinesis [GO:0000910]; defense response to virus [GO:0051607]; engulfment of apoptotic cell [GO:0043652]; late endosome to vacuole transport [GO:0045324]; lysosome organization [GO:0007040]; macroautophagy [GO:0016236]; mitotic metaphase plate congression [GO:0007080]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; neuron development [GO:0048666]; nucleophagy [GO:0044804]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of autophagy [GO:0010508]; positive regulation of macroautophagy [GO:0016239]; positive regulation of mitochondrion degradation [GO:1903599]; receptor catabolic process [GO:0032801]; regulation of catalytic activity [GO:0050790]; regulation of cytokinesis [GO:0032465]; viral process [GO:0016032]2phosphatidylinositol 3-kinase binding [GO:0043548]dautophagosome [GO:0005776]; cytoplasmic membrane-bounded vesicle [GO:0016023]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extrinsic component of membrane [GO:0019898]; mitochondrial membrane [GO:0031966]; phagocytic vesicle [GO:0045335]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]; pre-autophagosomal structure [GO:0000407]; trans-Golgi network [GO:0005802]FUNCTION: Plays a central role in autophagy (PubMed:23184933). Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). Protects against infection by a neurovirulent strain of Sindbis virus (PubMed:9765397). May play a role in antiviral host defense. {ECO:0000269|PubMed:20208530, ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:25275521, ECO:0000269|PubMed:9765397, ECO:0000305}.P02511CRYABAlpha-crystallin B chainSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.aging [GO:0007568]; apoptotic process involved in morphogenesis [GO:0060561]; cellular response to gamma radiation [GO:0071480]; lens development in camera-type eye [GO:0002088]; microtubule polymerization or depolymerization [GO:0031109]; muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of gene expression [GO:0010629]; negative regulation of intracellular transport [GO:0032387]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; protein folding [GO:0006457]; protein homooligomerization [GO:0051260]; regulation of cell death [GO:0010941]; response to estradiol [GO:0032355]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; stress-activated MAPK cascade [GO:0051403]; tubulin complex assembly [GO:0007021]identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082]Uactin filament bundle [GO:0032432]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Z disc [GO:0030018]FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.Q96S19CP013UPF0585 protein C16orf13P18433PTPRA0Receptor-type tyrosine-protein phosphatase alphaaxon guidance [GO:0007411]; insulin receptor signaling pathway [GO:0008286]; peptidyl-tyrosine dephosphorylation [GO:0035335]; protein phosphorylation [GO:0006468]}protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]Q96S59RANB9Ran-binding protein 9SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note==Predominantly cytoplasmic. A phosphorylated form is associated with the plasma membrane.axon guidance [GO:0007411]; microtubule nucleation [GO:0007020]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; protein complex assembly [GO:0006461]<enzyme binding [GO:0019899]; Ran GTPase binding [GO:0008536]Wcytosol [GO:0005829]; microtubule associated complex [GO:0005875]; nucleus [GO:0005634]FUNCTION: May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity). {ECO:0000250}.Q9UQ80PA2G4$Proliferation-a< ssociated protein 2G4SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}. Nucleus, nucleolus {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}. Note=Tranlocates to the nucleus upon treatment with HRG. Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar localization. {ECO:0000269|PubMed:16832058}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.ccell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of cell differentiation [GO:0045597]; regulation of translation [GO:0006417]; rRNA processing [GO:0006364]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]"FUNCTION: May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity). Regulates cell proliferation, differentiation, and survival. Isoform 1 suppresses apoptosis whereas isoform 2 promotes cell differentiation (By similarity). {ECO:0000250|UniProtKB:P50580, ECO:0000250|UniProtKB:Q6AYD3, ECO:0000269|PubMed:11268000, ECO:0000269|PubMed:12682367, ECO:0000269|PubMed:15064750, ECO:0000269|PubMed:15583694, ECO:0000269|PubMed:16832058}.Q9Y3E1HDGR30Hepatoma-derived growth factor-related protein 3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10581169}.jFUNCTION: Enhances DNA synthesis and may play a role in cell proliferation. {ECO:0000269|PubMed:10581169}.Q8IWV8UBR2 E3 ubiquitin-protein ligase UBR2[SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with chromatin during meiosis.9cellular response to leucine [GO:0071233]; chromatin silencing [GO:0006342]; histone H2A ubiquitination [GO:0033522]; male meiosis I [GO:0007141]; negative regulation of TOR signaling [GO:0032007]; spermatogenesis [GO:0007283]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151]fFUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. {ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:20298436, ECO:0000269|PubMed:20835242}.Q8NFG4FLCN FolliculinSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly localized in the nucleus. Colocalizes with FNIP1 and FNIP2 in the cytoplasm.7cell-cell junction assembly [GO:0007043]; hemopoiesis [GO:0030097]; in utero embryonic development [GO:0001701]; negative regulation of ATP biosynthetic process [GO:2001170]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation involved in kidney development [GO:1901723]; negative regulation of energy homeostasis [GO:2000506]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of gene expression [GO:0010629]; negative regulation of mitochondrion organization [GO:0010823]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of protein localization to nucleus [GO:1900181]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of TOR signaling [GO:0032007]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell adhesion [GO:0045785]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of cytokinesis [GO:0032465]; regulation of histone acetylation [GO:0035065]; regulation of pro-B cell differentiation [GO:2000973]; regulation of protein phosphorylation [GO:0001932]; regulation of TOR signaling [GO:0032006]; TOR signaling [GO:0031929]FUNCTION: May play a role in the pathogenesis of an uncommon form of kidney cancer through its association with an inherited disorder of the hair follicle (fibrofolliculomas). May be a tumor suppressor. May be involved in colorectal tumorigenesis. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. {ECO:0000269|PubMed:12204536, ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18663353}.Q14344GNA133Guanine nucleotide-binding protein subunit alpha-13xSUBCELLULAR LOCATION: Membrane; Lipid-anchor. Melanosome. Cytoplasm. Nucleus. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Detected in the cytoplasm of Leydig cells and in the seminiferous epithelium, including differentiating cells from the spermatogonia to mature spermatozoa stages. In round spermatids, also present in the nuclei.jactivation of phospholipase D activity [GO:0031584]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; in utero embryonic development [GO:0001701]; movement of cell or subcellular component [GO:0006928]; patterning of blood vessels [GO:0001569]; platelet activation [GO:0030168]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]D5 dopamine receptor binding [GO:0031752]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]; type 1 angiotensin receptor binding [GO:0031702] brush border membrane [GO:0031526]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; heterotrimeric G-protein complex [GO:0005834]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.P52434RPAB3:DNA-directed RNA polymerases I, II, and III subunit RPABC3YSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9852112, ECO:0000269|Ref.6}.vFUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5< S rRNA and tRNAs, respectively. {ECO:0000269|PubMed:9852112}.P36959GMPR1GMP reductase 1nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide metabolic process [GO:0009117]; purine-containing compound salvage [GO:0043101]; purine nucleobase metabolic process [GO:0006144]; response to cold [GO:0009409]; small molecule metabolic process [GO:0044281]FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.Q9ULW0TPX2Targeting protein for Xklp2qSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucleus. Is released from the nucleus in apoptotic cells and is detected on apoptotic microtubules.activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; cell division [GO:0051301]; cell proliferation [GO:0008283]; mitotic nuclear division [GO:0007067]; regulation of mitotic spindle organization [GO:0060236]WATP binding [GO:0005524]; GTP binding [GO:0005525]; protein kinase binding [GO:0019901]axon hillock [GO:0043203]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle pole [GO:0000922]FUNCTION: Spindle assembly factor. Required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764}.Q13426XRCC4DNA repair protein XRCC4XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16478998, ECO:0000269|PubMed:9259561}.=cellular protein metabolic process [GO:0044267]; cellular response to lithium ion [GO:0071285]; DNA ligation involved in DNA repair [GO:0051103]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; establishment of integrated proviral latency [GO:0075713]; positive regulation of ligase activity [GO:0051351]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; response to X-ray [GO:0010165]; viral process [GO:0016032] cell junction [GO:0030054]; centrosome [GO:0005813]; cytosol [GO:0005829]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; DNA ligase IV complex [GO:0032807]; nonhomologous end joining complex [GO:0070419]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. {ECO:0000269|PubMed:10757784, ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:16412978, ECO:0000269|PubMed:8548796}.Q9H9Y2RPF1Ribosome production factor 1xmaturation of 5.8S rRNA [GO:0000460]; maturation of LSU-rRNA [GO:0000470]; ribosomal large subunit assembly [GO:0000027]hpoly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; rRNA primary transcript binding [GO:0042134]Inucleolus [GO:0005730]; preribosome, large subunit precursor [GO:0030687]QFUNCTION: May be required for ribosome biogenesis. {ECO:0000269|PubMed:11864606}.Q9BQS8FYCO10FYVE and coiled-coil domain-containing protein 1 SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome. Endosome. Lysosome. Note=Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes.Bplus-end-directed vesicle transport along microtubule [GO:0072383]autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]eFUNCTION: May mediate microtubule plus end-directed vesicle transport. {ECO:0000269|PubMed:20100911}.Q9BYB4GNB1L>Guanine nucleotide-binding protein subunit beta-like protein 1G-protein coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; social behavior [GO:0035176]Hcytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]Q9UH99SUN2SUN domain-containing protein 2SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II membrane protein. Endosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.wcentrosome localization [GO:0051642]; cytoskeletal anchoring at nuclear membrane [GO:0090286]; mitotic spindle organization [GO:0007052]; nuclear envelope organization [GO:0006998]; nuclear matrix anchoring at nuclear membrane [GO:0090292]; nuclear migration [GO:0007097]; nuclear migration along microfilament [GO:0031022]; positive regulation of cell migration [GO:0030335]identical protein binding [GO:0042802]; lamin binding [GO:0005521]; microtubule binding [GO:0008017]; protein anchor [GO:0043495]condensed nuclear chromosome [GO:0000794]; endosome membrane [GO:0010008]; integral component of nuclear inner membrane [GO:0005639]; LINC complex [GO:0034993]; nuclear chromosome, telomeric region [GO:0000784]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]FUNCTION: Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. {ECO:0000269|PubMed:18396275}.Q9H788SH24A SH2 domain-containing protein 4AvSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18641339}. Note=Located at podocyte foot processes. {ECO:0000250}.)FUNCTION: Inhibits estrogen-induced cell proliferation by competing with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG and repressing estrogen-induced proliferation. May play a role in T-cell development and function. {ECO:0000269|PubMed:18641339, ECO:0000269|PubMed:19712589}.P98171RHG04Rho GTPase-activating protein 4ESUBCELLULAR LOCATION: Cytoplasm. Note=Just below the plasma membrane.apoptotic signaling pathway [GO:0097190]; cytoskeleton organization [GO:0007010]; negative regulation of cell migration [GO:0030336]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of signal transduction [GO:0009967]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]nGTPase activator activity [GO:0005096]; Ra< c GTPase binding [GO:0048365]; SH3/SH2 adaptor activity [GO:0005070]ccytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]sFUNCTION: Inhibitory effect on stress fiber organization. May down-regulate Rho-like GTPase in hematopoietic cells.Q0ZGT2NEXNNexilinFSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Z2J4}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localizes to the cell-matrix AJ. Not found at the cell-cell AJ (By similarity). {ECO:0000250|UniProtKB:Q9Z2J4, ECO:0000269|PubMed:15823560}.cardiac muscle fiber development [GO:0048739]; protein phosphorylation [GO:0006468]; regulation of cell migration [GO:0030334]; regulation of cytoskeleton organization [GO:0051493]actin filament binding [GO:0051015]; calmodulin-dependent protein kinase activity [GO:0004683]; structural constituent of muscle [GO:0008307]Kcytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; Z disc [GO:0030018]FUNCTION: Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. {ECO:0000269|PubMed:12053183, ECO:0000269|PubMed:15823560, ECO:0000269|PubMed:19881492}.Q8TCT8SPP2A Signal peptide peptidase-like 2ASUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16829952}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9JJF9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JJF9}. Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}. Note=Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane.uextracellular exosome [GO:0070062]; Golgi-associated vesicle membrane [GO:0030660]; integral component of cytoplasmic side of endoplasmic reticulum membrane [GO:0071458]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]BFUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17557115, PubMed:17965014). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952). Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD) (PubMed:17557115). May play a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). {ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:17965014, ECO:0000269|PubMed:23132852}.Q8TCU4ALMS1Alstrom syndrome protein 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, spindle pole. Note=Associated with centrosomes and basal bodies at the base of primary cilia. Specifically locates to the proximal ends of centrioles and basal bodies. Colocalizes partially with NCAPD2 at these sites. During mitosis localizes to both spindle poles.endosomal transport [GO:0016197]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; regulation of stress fiber assembly [GO:0051492]centrosome [GO:0005813]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]ZFUNCTION: Involved in PCM1-dependent intracellular transport. Required, directly or indirectly, for the localization of NCAPD2 to the proximal ends of centrioles. Required for proper formation and/or maintenance of primary cilia (PC), microtubule-based structures that protrude from the surface of epithelial cells. {ECO:0000269|PubMed:17954613}.O94864ST65GSTAGA complex 65 subunit gammachromatin organization [GO:0006325]; histone H3 acetylation [GO:0043966]; maintenance of protein location in nucleus [GO:0051457]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]0nucleus [GO:0005634]; STAGA complex [GO:0030914]Q9HAV4XPO5 Exportin-5SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11777942}. Cytoplasm {ECO:0000269|PubMed:11777942}. Note=Shuttles between the nucleus and the cytoplasm.gene expression [GO:0010467]; positive regulation of RNA interference [GO:1900370]; pre-miRNA export from nucleus [GO:0035281]; protein export from nucleus [GO:0006611]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; pre-miRNA binding [GO:0070883]; protein transporter activity [GO:0008565]; Ran GTPase binding [GO:0008536]; RNA binding [GO:0003723]; tRNA binding [GO:0000049]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA nuclear export complex [GO:0042565]jFUNCTION: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.; FUNCTION: Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP.Q5T4B2GT2538Probable inactive glycosyltransferase 25 family member 3}cell adhesion [GO:0007155]; leukocyte cell-cell adhesion [GO:0007159]; movement of cell or subcellular component [GO:0006928]Fendoplasmic reticulum lumen [GO:0005788]; plasma membrane [GO:0005886]FUNCTION: Probable cell adhesion protein involved in leukocyte transmigration across the blood-brain barrier. Has apparently no beta-galactosyltransferase activity. {ECO:0000269|PubMed:10608765, ECO:0000269|PubMed:19075007}.O75531BAF!Barrier-to-autointegration factorSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495336}. Cytoplasm {ECO:0000269|PubMed:16495336}. Chromosome {ECO:0000269|PubMed:16495336}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase. May be included in HIV-1 virions via its interaction with viral GAG polyprotein. The phosphorylated form (by VRK1) shows a cytoplasmic localization.DNA integration [GO:0015< 074]; establishment of integrated proviral latency [GO:0075713]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; mitotic nuclear envelope reassembly [GO:0007084]; response to virus [GO:0009615]; viral process [GO:0016032]chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634].FUNCTION: Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:16680152}.Q15650TRIP4 Activating signal cointegrator 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}. Cytoplasm, cytosol {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20873783}. Note=Cytoplasmic under conditions of serum deprivation (PubMed:10454579). Colocalizes with NEK6 in the centrosome (PubMed:20873783). {ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:20873783}.intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of transcription, DNA-templated [GO:0045893]; toxin transport [GO:1901998]; transcription from RNA polymerase II promoter [GO:0006366]1estrogen receptor binding [GO:0030331]; histone acetyltransferase binding [GO:0035035]; ligand-dependent nuclear receptor binding [GO:0016922]; protease binding [GO:0002020]; transcription coactivator activity [GO:0003713]; ubiquitin-like protein ligase binding [GO:0044389]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]SFUNCTION: Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (PubMed:10454579, PubMed:25219498). Also involved in androgen receptor transactivation (By similarity). Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B (PubMed:12077347). {ECO:0000250|UniProtKB:Q9QXN3, ECO:0000269|PubMed:10454579, ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:25219498}.Q9UHG3PCYOXPrenylcysteine oxidase 1oxidation-reduction process [GO:0055114]; prenylated protein catabolic process [GO:0030327]; prenylcysteine catabolic process [GO:0030328]; prenylcysteine metabolic process [GO:0030329]`chloride-transporting ATPase activity [GO:0008555]; prenylcysteine oxidase activity [GO:0001735]extracellular exosome [GO:0070062]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774]; very-low-density lipoprotein particle [GO:0034361]FUNCTION: Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine.Q96P47AGAP3BArf-GAP with GTPase, ANK repeat and PH domain-containing protein 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16461359}. Note=In cells upon oxidative stress or in brains of Machado-Joseph disease patients, translocates to PML nuclear bodies.`GTPase activator activity [GO:0005096]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:16461359, ECO:0000305}.Q8NBR6FA63BProtein FAM63BQ8N5B7CERS5Ceramide synthase 5SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00108}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.ceramide biosynthetic process [GO:0046513]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]MDNA binding [GO:0003677]; sphingosine N-acyltransferase activity [GO:0050291]wendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; nuclear membrane [GO:0031965]FUNCTION: Dihydroceramide synthase. Catalyzes the acylation of sphingosine to form dihydroceramide, with high selectivity toward palmitoyl-CoA as acyl donor compared to stearoyl-CoA. Inhibited by fumonisin B1 (By similarity). {ECO:0000250}.Q7L5Y9MAEA Macrophage erythroblast attachertransmembranes(6)SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16510120}. Cell membrane {ECO:0000269|PubMed:16510120}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16510120}. Note=Localized as nuclear speckled-like pattern.?cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cytoskeleton organization [GO:0007010]; enucleate erythrocyte development [GO:0048822]; erythrocyte maturation [GO:0043249]; negative regulation of myeloid cell apoptotic process [GO:0033033]; regulation of mitotic cell cycle [GO:0007346]actomyosin contractile ring [GO:0005826]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; integral component of plasma membrane [GO:0005887]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]vFUNCTION: Plays a role in erythroblast enucleation and in the development of the mature macrophages. Mediates the attachment of erythroid cell to mature macrophages, in correlation with the presence of MAEA at cell surface of mature macrophages; This MAEA-mediated contact inhibits erythroid cells apoptosis. Participates to erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages. May contribute to nuclear architecture and cells division events. {ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:9763581}.Q8N2G6ZCH24-Zinc finger CCHC domain-containing protein 24Q16706MA2A1Alpha-mannosidase 2ecellular protein metabolic process [GO:0044267]; in utero embryonic development [GO:0001701]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; mannose metabolic process [GO:0006013]; mitochondrion organization [GO:0007005]; N-glycan processing [GO:0006491]; positive regulation of neurogenesis [GO:0050769]; post-translational protein modification [GO:0043687]; protein deglycosylation [GO:0006517]; protein N-linked glycosylation via asparagine [GO:0018279]; respiratory gaseous exchange [GO:0007585]; retina morphogenesis in camera-type eye [GO:0060042]; vacuole organization [GO:0007033]carbohydrate binding [GO:0030246]; hydrolase activity, hydrolyzing N-glycosyl compounds [GO:0016799]; mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity [GO:0004572]; zinc ion binding [GO:0008270]cis-Golgi network [GO:0005801]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]Q99715COCA1Collagen alpha-1(XII) chain Collagens(43)%cell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; collagen fibril orga< nization [GO:0030199]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; skeletal system development [GO:0001501]Textracellular matrix structural constituent conferring tensile strength [GO:0030020]collagen type XII trimer [GO:0005595]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]FUNCTION: Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. {ECO:0000250}.Q9NR99MXRA5&Matrix-remodeling-associated protein 5P35226BMI1Polycomb complex protein BMI-1cellular protein metabolic process [GO:0044267]; chromatin modification [GO:0016568]; hemopoiesis [GO:0030097]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of gene expression [GO:0010468]; segment specification [GO:0007379]; transcription, DNA-templated [GO:0006351]PRING-like zinc finger domain binding [GO:0071535]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]; ubiquitin ligase complex [GO:0000151]ZFUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2. {ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:16882984}.Q96D71REPS11RalBP1-associated Eps domain-containing protein 1SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000269|PubMed:20946875}. Note=Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits.*receptor-mediated endocytosis [GO:0006898]Acalcium ion binding [GO:0005509]; SH3 domain binding [GO:0017124]5coated pit [GO:0005905]; plasma membrane [GO:0005886]hFUNCTION: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases. {ECO:0000250}.P56817BACE1Beta-secretase 1SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface.beta-amyloid metabolic process [GO:0050435]; membrane protein ectodomain proteolysis [GO:0006509]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]aspartic-type endopeptidase activity [GO:0004190]; beta-amyloid binding [GO:0001540]; beta-aspartyl-peptidase activity [GO:0008798]; enzyme binding [GO:0019899]; peptidase activity [GO:0008233]axon [GO:0030424]; cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. {ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:20354142}.O95772MENTOMLN64 N-terminal domain homologintegral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]O43314VIP2JInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17690096}.inositol metabolic process [GO:0006020]; inositol phosphate metabolic process [GO:0043647]; small molecule metabolic process [GO:0044281]sacid phosphatase activity [GO:0003993]; ATP binding [GO:0005524]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832]GFUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752}.Q9UNX4WDR3WD repeat-containing protein 3nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleus [GO:0005634]; Pwp2p-containing subcomplex of 90S preribosome [GO:0034388]; small-subunit processome [GO:0032040]Q96QU8XPO6 Exportin-6^SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.(protein export from nucleus [GO:0006611]|FUNCTION: Mediates the nuclear export of actin and profilin-actin complexes in somatic cells. {ECO:0000269|PubMed:14592989}.Q9BXX0EMIL2EMILIN-2Cextracellular matrix constituent conferring elasticity [GO:0030023]collagen trimer [GO:0005581]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]Q96EC8YIPF6 Protein YIPF63intestinal epithelial cell development [GO:0060576]cis-Golgi network [GO:0005801]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle [GO:0030134]; integral component of membrane [GO:0016021]; trans-Golgi network [GO:0005802]O00505IMA4Importin subunit alpha-4cytokine-mediated signaling pathway [GO:0019221]; NLS-bearing protein import into nucleus [GO:0006607]; protein complex assembly [GO:0006461]; viral entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]]nuclear localization sequence binding [GO:0008139]; protein transporter activity [GO:0008565]FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate a< nd importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9.P35269T2FA*General transcription factor IIF subunit 1f7-methylguanosine mRNA capping [GO:0006370]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of catalytic activity [GO:0043085]; positive regulation of transcription elongation from RNA polymerase II promoter [GO:0032968]; positive regulation of viral transcription [GO:0050434]; response to virus [GO:0009615]; RNA splicing [GO:0008380]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]catalytic activity [GO:0003824]; DNA binding [GO:0003677]; phosphatase activator activity [GO:0019211]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]{cell junction [GO:0030054]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor TFIIF complex [GO:0005674]FUNCTION: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. {ECO:0000269|PubMed:10428810}.Q9Y3E7CHMP3%Charged multivesicular body protein 3SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane {ECO:0000305}. Note=Localizes to the midbody of dividing cells.apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell separation after cytokinesis [GO:0000920]; endosomal transport [GO:0016197]; membrane organization [GO:0061024]; negative regulation of viral release from host cell [GO:1902187]; positive regulation of viral release from host cell [GO:1902188]; protein heterooligomerization [GO:0051291]; protein polymerization [GO:0051258]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of viral process [GO:0050792]; vacuolar transport [GO:0007034]; viral budding via host ESCRT complex [GO:0039702]; viral life cycle [GO:0019058]; viral process [GO:0016032]phosphatidylcholine binding [GO:0031210]; protein homodimerization activity [GO:0042803]; ubiquitin-specific protease binding [GO:1990381]cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]"FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15707591, ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:17331679, ECO:0000269|PubMed:18076377}.Q9BTA9WAC5WW domain-containing adapter protein with coiled-coilSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus {ECO:0000269|PubMed:21329877}. Note=In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes (By similarity). {ECO:0000250}.cellular response to DNA damage stimulus [GO:0006974]; G1 DNA damage checkpoint [GO:0044783]; histone H2B conserved C-terminal lysine ubiquitination [GO:0071894]; histone monoubiquitination [GO:0010390]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription, DNA-templated [GO:0045893]; transcription, DNA-templated [GO:0006351]mnuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]6FUNCTION: Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. May negatively regulate the ubiquitin proteasome pathway. {ECO:0000269|PubMed:21329877, ECO:0000269|PubMed:22354037}.C9JLW8F195BProtein FAM195BO14678ABCD4*ATP-binding cassette sub-family D member 4cobalamin metabolic process [GO:0009235]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]gATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]ATP-binding cassette (ABC) transporter complex [GO:0043190]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: May be involved in intracellular processing of vitamin B12 (cobalamin). Could play a role in the lysosomal release of vitamin B12 into the cytoplasm. {ECO:0000269|PubMed:22922874}.Q8NDA2HMCN2 Hemicentin-2!response to stimulus [GO:0050896]Q13207TBX2T-box transcription factor TBX2aorta morphogenesis [GO:0035909]; atrioventricular canal development [GO:0036302]; cardiac muscle tissue development [GO:0048738]; cell aging [GO:0007569]; cellular senescence [GO:0090398]; developmental growth involved in morphogenesis [GO:0060560]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic digit morphogenesis [GO:0042733]; endocardial cushion morphogenesis [GO:0003203]; mammary placode formation [GO:0060596]; muscle cell fate determination [GO:0007521]; negative regulation of cardiac chamber formation [GO:1901211]; negative regulation of heart looping [GO:1901208]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; outflow tract morphogenesis [GO:0003151]; outflow tract septum morphogenesis [GO:0003148]; palate development [GO:0060021]; pharynx development [GO:0060465]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell proliferation [GO:0008284]; regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation [GO:0003256]; transcription, DNA-templated [GO:0006351]KDNA binding [GO:0003677]; RNA polymerase II core prom< oter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; sequence-specific DNA binding [GO:0043565]7FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm differentiation. Probably plays a role in limb pattern formation. Acts as a negative regulator of PML function in cellular senescence. May be required for cardiac atrioventricular canal formation. {ECO:0000269|PubMed:22002537}.Q9Y221NIP7460S ribosome subunit biogenesis protein NIP7 homologdSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22195017}.ribosome assembly [GO:0042255]wFUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. {ECO:0000269|PubMed:22195017}.Q9UKJ3GPTC8#G patch domain-containing protein 8Q8IZ73RUSD28RNA pseudouridylate synthase domain-containing protein 2Q8NAP3ZBT380Zinc finger and BTB domain-containing protein 38negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]metal ion binding [GO:0046872]; methyl-CpG binding [GO:0008327]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding transcription factor activity [GO:0003700]6blood microparticle [GO:0072562]; nucleus [GO:0005634]FUNCTION: Acts as a transcriptional activator. May be involved in the differentiation and/or survival of late postmitotic neurons (By similarity). {ECO:0000250|UniProtKB:Q5EXX3}.Q92685ALG3>Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase$cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; mannosylation [GO:0097502]; post-translational protein modification [GO:0043687]; protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279]alpha-1,3-mannosyltransferase activity [GO:0000033]; dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity [GO:0052925]FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. {ECO:0000269|PubMed:10581255}.Q06546GABPAGA-binding protein alpha chaincell differentiation [GO:0030154]; in utero embryonic development [GO:0001701]; mitochondrion organization [GO:0007005]; negative regulation of megakaryocyte differentiation [GO:0045653]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; organelle organization [GO:0006996]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription from RNA polymerase II promoter [GO:0006366]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription regulatory region DNA binding [GO:0044212]Nnuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Transcription factor capable of interacting with purine rich repeats (GA repeats). Necessary for the expression of the Adenovirus E4 gene.O95782AP2A1AP-2 complex subunit alpha-1antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; endocytosis [GO:0006897]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; Golgi to endosome transport [GO:0006895]; intracellular protein transport [GO:0006886]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of defense response to virus by virus [GO:0050690]; synaptic transmission [GO:0007268]; viral process [GO:0016032]Nprotein kinase binding [GO:0019901]; protein transporter activity [GO:0008565]uAP-2 adaptor complex [GO:0030122]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; filopodium tip [GO:0032433]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q6ZVM7TM1L2TOM1-like protein 2intracellular protein transport [GO:0006886]; negative regulation of mitotic nuclear division [GO:0045839]; signal transduction [GO:0007165]Bclathrin binding [GO:0030276]; protein kinase binding [GO:0019901]>extracellular exosome [GO:0070062]; intracellular [GO:0005622]FUNCTION: Probable role in protein transport. May regulate growth factor-induced mitogenic signaling. {ECO:0000269|PubMed:16412388, ECO:0000269|PubMed:16479011}.P37173TGFR2TGF-beta receptor type-2SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1310899}; Single-pass type I membrane protein {ECO:0000269|PubMed:1310899}. activation of protein kinase activity [GO:0032147]; aging [GO:0007568]; apoptotic process [GO:0006915]; blood vessel development [GO:0001568]; brain development [GO:0007420]; bronchus morphogenesis [GO:0060434]; common-partner SMAD protein phosphorylation [GO:0007182]; digestive tract development [GO:0048565]; embryo implantation [GO:0007566]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic hemopoiesis [GO:0035162]; gastrulation [GO:0007369]; growth plate cartilage chondrocyte growth [GO:0003430]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; lens development in camera-type eye [GO:0002088]; lens fiber cell apoptotic process [GO:1990086]; lung lobe morphogenesis [GO:0060463]; mammary gland morphogenesis [GO:0060443]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; organ regeneration [GO:0031100]; palate development [GO:0060021]; pathway-restricted SMAD protein phosphorylation [GO:0060389]; patterning of blood vessels [GO:0001569]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of angiogenesis [GO:0045766]; positive regulation of B cell tolerance induction [GO:0002663]; positive regulation of cell proliferation [GO:0008284]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of NK T cell differentiation [GO:0051138]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of skeletal muscle tissue regeneration [GO:0043415]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of T cell tolerance induction [GO:0002666]; positive regulation of tolerance induction to self antigen [GO:0002651]; protein phosphorylation [GO:0006468]; receptor-mediated endocytosis [GO:0006898]; regulation of cell proliferation [GO:0042127]; regulation of gene expression [GO:0010468]; response to cholesterol [GO:0070723]; response to drug [GO:0042493]; response to estrogen [GO:0043627]; response to glucose [GO:0009749]; response to mechanical stimulus [GO:0009612]; response to nutrient [GO:0007584]; smoothened signaling pathway [GO:0007224]; trachea formation [GO:0060440]; transforming growth fac< tor beta receptor signaling pathway [GO:0007179]; vasculogenesis [GO:0001570]; wound healing [GO:0042060]jATP binding [GO:0005524]; glycosaminoglycan binding [GO:0005539]; metal ion binding [GO:0046872]; receptor signaling protein serine/threonine kinase activity [GO:0004702]; SMAD binding [GO:0046332]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type II [GO:0005026]; transmembrane receptor protein serine/threonine kinase activity [GO:0004675]; type III transforming growth factor beta receptor binding [GO:0034714]; type I transforming growth factor beta receptor binding [GO:0034713]caveola [GO:0005901]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; transforming growth factor beta receptor homodimeric complex [GO:0070022]FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. {ECO:0000269|PubMed:7774578}.Q96GS4CQ059 Uncharacterized protein C17orf59Q68D10SPT2Protein SPT2 homologO43752STX6 Syntaxin-6qSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.endosome organization [GO:0007032]; Golgi ribbon formation [GO:0090161]; Golgi vesicle transport [GO:0048193]; intracellular protein transport [GO:0006886]; regulation of protein localization [GO:0032880]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion [GO:0006906]_clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; terminal bouton [GO:0043195]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]8FUNCTION: Involved in intracellular vesicle trafficking.Q5VVM6CCD30(Coiled-coil domain-containing protein 30Q9P287BCCIP$BRCA2 and CDKN1A-interacting proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10878006, ECO:0000269|PubMed:11313963, ECO:0000269|PubMed:15713648}. Note=Colocalizes with BRCA2 in discrete nuclear foci.cell cycle [GO:0007049]; DNA repair [GO:0006281]; neuroendocrine cell differentiation [GO:0061101]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]Hkinase regulator activity [GO:0019207]; poly(A) RNA binding [GO:0044822]]nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nucleus [GO:0005634]FUNCTION: May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ). {ECO:0000269|PubMed:10878006, ECO:0000269|PubMed:14726710, ECO:0000269|PubMed:15539944, ECO:0000269|PubMed:15713648, ECO:0000269|PubMed:17947333}.Q9BRX8F213A Redox-regulatory protein FAM213A>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19951071}._oxidation-reduction process [GO:0055114]; regulation of osteoclast differentiation [GO:0045670]!antioxidant activity [GO:0016209]FUNCTION: Involved in redox regulation of the cell. Acts as an antioxidant. Inhibits TNFSF11-induced NFKB1 and JUN activation and osteoclast differentiation. May affect bone resorption and help to maintain bone mass. {ECO:0000269|PubMed:19951071}.Q86WG5MTMRDMyotubularin-related protein 13SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15998640}. Membrane {ECO:0000269|PubMed:15998640}; Peripheral membrane protein {ECO:0000269|PubMed:15998640}. Note=Associated with membranes.smyelination [GO:0042552]; positive regulation of GTPase activity [GO:0043547]; protein tetramerization [GO:0051262]phosphatase regulator activity [GO:0019208]; phosphatidylinositol binding [GO:0035091]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]5membrane [GO:0016020]; vacuolar membrane [GO:0005774]FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701}.P06746DPOLBDNA polymerase betaSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.'aging [GO:0007568]; base-excision repair [GO:0006284]; base-excision repair, gap-filling [GO:0006287]; cellular response to DNA damage stimulus [GO:0006974]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; homeostasis of number of cells [GO:0048872]; immunoglobulin heavy chain V-D-J recombination [GO:0071707]; inflammatory response [GO:0006954]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lymph node development [GO:0048535]; neuron apoptotic process [GO:0051402]; pyrimidine dimer repair [GO:0006290]; response to ethanol [GO:0045471]; response to gamma radiation [GO:0010332]; response to hyperoxia [GO:0055093]; salivary gland morphogenesis [GO:0007435]; somatic hypermutation of immunoglobulin genes [GO:0016446]; spleen development [GO:0048536]damaged DNA binding [GO:0003684]; DNA-directed DNA polymerase activity [GO:0003887]; enzyme binding [GO:0019899]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; spindle microtubule [GO:0005876]FUNCTION: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. {ECO:0000269|PubMed:11805079, ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9572863}.Q9NPI6DCP1AmRNA-decapping enzyme 1ASUBCELLULAR LOCATION: Cytoplasm, P-body. Nucleus. Note=Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4. {ECO:0000250}.8exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]Ghydrolase activity [GO:0016787]; identical protein binding [GO:0042802]pcytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [< GO:0005634]uFUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1. {ECO:0000269|PubMed:11836524, ECO:0000269|PubMed:12417715}.P36954RPB9+DNA-directed RNA polymerase II subunit RPB9FSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9852112}.7-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter [GO:0001193]; mRNA splicing, via spliceosome [GO:0000398]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of viral transcription [GO:0050434]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]DNA-directed RNA polymerase II, core complex [GO:0005665]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). {ECO:0000250}.O95707RPP29"Ribonuclease P protein subunit p29GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10352175}.mRNA cleavage [GO:0006379]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033]gribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]; RNA binding [GO:0003723]ynucleolar ribonuclease P complex [GO:0005655]; ribonuclease MRP complex [GO:0000172]; ribonuclease P complex [GO:0030677]FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P.Q8WWH5TRUB1&Probable tRNA pseudouridine synthase 1ImRNA pseudouridine synthesis [GO:1990481]; tRNA modification [GO:0006400]Fpseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]hFUNCTION: May be responsible for synthesis of pseudouridine from uracil in transfer RNAs. {ECO:0000250}.Q07092COGA1Collagen alpha-1(XVI) chaingSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9022684}.cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; female pregnancy [GO:0007565]; integrin activation [GO:0033622]; integrin-mediated signaling pathway [GO:0007229]; positive regulation of focal adhesion assembly [GO:0051894]collagen type XVI trimer [GO:0005597]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology. {ECO:0000269|PubMed:16754661}.Q2M1P5KIF7Kinesin-like protein KIF7nSUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19592253}. Note=Localizes to the cilium tip.microtubule-based movement [GO:0007018]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regulation of smoothened signaling pathway [GO:0045880]; smoothened signaling pathway [GO:0007224]; ventricular system development [GO:0021591]Kciliary tip [GO:0097542]; cilium [GO:0005929]; kinesin complex [GO:0005871]FUNCTION: Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250, ECO:0000269|PubMed:21633164}.Q9H0R6GATA<Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrialcSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:19805282}.gglutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681]; mitochondrial translation [GO:0032543]>FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:19805282}.Q6UX04CWC271Peptidyl-prolyl cis-trans isomerase CWC27 homologDFUNCTION: PPIases accelerate the folding of proteins. {ECO:0000250}.Q9NXV6CARFCDKN2A-interacting proteinfSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:12154087, ECO:0000269|PubMed:12581788}.cellular response to DNA damage stimulus [GO:0006974]; negative regulation of cell growth [GO:0030308]; positive regulation of cell growth [GO:0030307]; positive regulation of signal transduction [GO:0009967]; regulation of protein stability [GO:0031647]2p53 binding [GO:0002039]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; granular component [GO:0001652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Regulates DNA damage response in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence. {ECO:0000269|PubMed:15109303, ECO:0000269|PubMed:24825908}.Q9UFF9CNOT8(CCR4-NOT transcription complex subunit 8eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12771185}. Nucleus {ECO:0000269|PubMed:12771185}.exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; gene silencing by miRNA [GO:0035195]; negative regulation of cell proliferation [GO:0008285]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cell proliferation [GO:0008284]; positive regulation of mRNA catabolic process [GO:0061014]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; transcription, DNA-templated [GO:0006351]3'-5'-exoribonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]; sequence-specific DNA binding transcription factor activity [GO:0003700]eCCR4-NOT complex [GO:0030014];< cytosol [GO:0005829]; intracellular [GO:0005622]; nucleus [GO:0005634]NFUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity. {ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:19605561, ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:23236473}.Q9H501ESF1 ESF1 homolog[SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}.FUNCTION: May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity). {ECO:0000250}.Q03135CAV1 Caveolin-15SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Membrane raft. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae.)angiogenesis [GO:0001525]; angiotensin-activated signaling pathway involved in heart process [GO:0086098]; apoptotic signaling pathway [GO:0097190]; blood coagulation [GO:0007596]; calcium ion homeostasis [GO:0055074]; calcium ion transport [GO:0006816]; caveola assembly [GO:0070836]; caveolin-mediated endocytosis [GO:0072584]; cellular calcium ion homeostasis [GO:0006874]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to hyperoxia [GO:0071455]; cellular response to mechanical stimulus [GO:0071260]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to starvation [GO:0009267]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular senescence [GO:0090398]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol transport [GO:0030301]; cytosolic calcium ion homeostasis [GO:0051480]; inactivation of MAPK activity [GO:0000188]; lactation [GO:0007595]; leukocyte migration [GO:0050900]; lipid storage [GO:0019915]; maintenance of protein location in cell [GO:0032507]; mammary gland development [GO:0030879]; mammary gland involution [GO:0060056]; MAPK cascade [GO:0000165]; membrane depolarization [GO:0051899]; microtubule polymerization [GO:0046785]; negative regulation of anoikis [GO:2000811]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cation channel activity [GO:2001258]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of JAK-STAT cascade [GO:0046426]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of necroptotic process [GO:0060546]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; negative regulation of nitric-oxide synthase activity [GO:0051001]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-tyrosine autophosphorylation [GO:1900085]; negative regulation of pinocytosis [GO:0048550]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of protein binding [GO:0032091]; negative regulation of protein tyrosine kinase activity [GO:0061099]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of tyrosine phosphorylation of Stat5 protein [GO:0042524]; nitric oxide homeostasis [GO:0033484]; nitric oxide metabolic process [GO:0046209]; organ regeneration [GO:0031100]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell adhesion molecule production [GO:0060355]; positive regulation of endocytosis [GO:0045807]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903071]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of gap junction assembly [GO:1903598]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of metalloenzyme activity [GO:0048554]; positive regulation of microtubule polymerization [GO:0031116]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein binding [GO:0032092]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; positive regulation of vasoconstriction [GO:0045907]; posttranscriptional regulation of gene expression [GO:0010608]; protein homooligomerization [GO:0051260]; protein localization [GO:0008104]; protein localization to basolateral plasma membrane [GO:1903361]; protein localization to plasma membrane raft [GO:0044860]; receptor internalization involved in canonical Wnt signaling pathway [GO:2000286]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; regulation of blood coagulation [GO:0030193]; regulation of cardiac muscle cell action potential involved in regulation of contraction [GO:0098909]; regulation of cell communication by electrical coupling involved in cardiac conduction [GO:1901844]; regulation of entry of bacterium into host cell [GO:2000535]; regulation of fatty acid metabolic process [GO:0019217]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of inward rectifier potassium channel activity [GO:1901979]; regulation of membrane repolarization during action potential [GO:0098903]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of peptidase activity [GO:0052547]; regulation of ruffle assembly [GO:1900027]; regulation of smooth muscle contraction [GO:0006940]; regulation of the force of heart contraction by chemical signal [GO:0003057]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; response to bacterium [GO:0009617]; response to calcium ion [GO:0051592]; response to drug [GO:0042493]; response to estrogen [GO:0043627]; response to gamma radiation [GO:0010332]; response to glucocorticoid [GO:0051384]; response to hypoxia [GO:0001666]; response to ischemia [GO:0002931]; response to nutrient [GO:0007584]; response to progesterone [GO:0032570]; skeletal muscle tissue development [GO:0007519]; small molecule metabolic process [GO:0044281]; T cell costimulation [GO:0031295]; triglyceride metabolic process [GO:0006641]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vasculogenesis [GO:0001570]; vasoconstriction [GO:0042310]; vesicle organization [GO:0016050]ATPase binding [GO:0051117]; cholesterol binding [GO:0015485]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; inward rectifier potassium channel inhibitor activity [GO:0070320]; ion channel binding [GO:0044325]; nitric-oxide synthase binding [GO:0050998]; patched binding [GO:0005113]; peptidase activator activity [GO:0016504]; protein complex scaffold [GO:0032947]; protein kinase binding [GO:0019901]; Rac GTPase binding [GO:0048365]; receptor binding [GO:0005102]; structural molecule< activity [GO:0005198]dacrosomal membrane [GO:0002080]; apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell cortex [GO:0005938]; cell surface [GO:0009986]; cilium [GO:0005929]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; lipid particle [GO:0005811]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886]; protein complex [GO:0043234]BFUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. {ECO:0000250, ECO:0000269|PubMed:11751885, ECO:0000269|PubMed:17287217}.Q13043STK4!Serine/threonine-protein kinase 4qSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm.activation of MAPKK activity [GO:0000186]; apoptotic process [GO:0006915]; cell differentiation involved in embryonic placenta development [GO:0060706]; cell morphogenesis [GO:0000902]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; hepatocyte apoptotic process [GO:0097284]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; keratinocyte differentiation [GO:0030216]; MAPK cascade [GO:0000165]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell proliferation [GO:0008285]; negative regulation of organ growth [GO:0046621]; neural tube formation [GO:0001841]; patterning of blood vessels [GO:0001569]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of apoptotic process [GO:0043065]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of protein binding [GO:0032092]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; primitive hemopoiesis [GO:0060215]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell differentiation involved in embryonic placenta development [GO:0060800]; regulation of mitotic cell cycle [GO:0007346]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]; transcription factor binding [GO:0008134] FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250, ECO:0000269|PubMed:11278283, ECO:0000269|PubMed:11517310, ECO:0000269|PubMed:12757711, ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:16510573, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:17932490, ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:19525978, ECO:0000269|PubMed:21212262, ECO:0000269|PubMed:21245099, ECO:0000269|PubMed:21512132, ECO:0000269|PubMed:8702870, ECO:0000269|PubMed:8816758}.P13726TF Tissue factoractivation of blood coagulation via clotting cascade [GO:0002543]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; activation of plasma proteins involved in acute inflammatory response [GO:0002541]; aging [GO:0007568]; blood coagulation [GO:0007596]; blood coagulation, extrinsic pathway [GO:0007598]; cellular response to hydrogen peroxide [GO:0070301]; cytokine-mediated signaling pathway [GO:0019221]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of platelet-derived growth factor receptor signaling pathway [GO:0010641]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of smooth muscle cell migration [GO:0014911]; response to estradiol [GO:0032355]; response to fluid shear stress [GO:0034405]; response to lipopolysaccharide [GO:0032496]; response to low-density lipoprotein particle [GO:0055098]; response to mechanical stimulus [GO:0009612]; response to temperature stimulus [GO:0009266]icytokine receptor activity [GO:0004896]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]+cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; intrinsic component of external side of plasma membrane [GO:0031233]; plasma membrane [GO:0005886]PFUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. {ECO:0000269|PubMed:12652293}.Q86TV6TTC7B#Tetratricopeptide repeat protein 7BQ6P6C2ALKB5RNA demethylase ALKBH5aSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:21264265, ECO:0000269|PubMed:23177736}.'cell differentiation [GO:0030154]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; oxidative single-stranded RNA demethylation [GO:0035553]; < positive regulation of defense response to virus by host [GO:0002230]; response to hypoxia [GO:0001666]; spermatogenesis [GO:0007283]Ametal ion binding [GO:0046872]; oxidative RNA demethylase activity [GO:0035515]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [GO:0016706]; poly(A) RNA binding [GO:0044822]:FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Demethylation of m6A mRNA affects mRNA processing and export (PubMed:23177736). Required for spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q3TSG4, ECO:0000269|PubMed:21264265, ECO:0000269|PubMed:23177736, ECO:0000269|PubMed:24489119, ECO:0000269|PubMed:24616105, ECO:0000269|PubMed:24778178}.P41208CETN2 Centrin-2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus {ECO:0000305}. Note=Centrosome of S-phase, interphase and mitotic cells.cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; centriole replication [GO:0007099]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; nucleotide-excision repair [GO:0006289]; organelle organization [GO:0006996]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of cytokinesis [GO:0032465]; spermatogenesis [GO:0007283]centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; intracellular [GO:0005622]; nucleoplasm [GO:0005654]; photoreceptor connecting cilium [GO:0032391]; XPC complex [GO:0071942]%FUNCTION: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; FUNCTION: Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (PubMed:22307388). {ECO:0000269|PubMed:22307388}.Q15054DPOD3DNA polymerase delta subunit 3base-excision repair [GO:0006284]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA synthesis involved in DNA repair [GO:0000731]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]1DNA-directed DNA polymerase activity [GO:0003887]udelta DNA polymerase complex [GO:0043625]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Required for optimal DNA polymerase delta activity. {ECO:0000269|PubMed:10219083, ECO:0000269|PubMed:10852724, ECO:0000269|PubMed:16510448}.O00566MPP102U3 small nucleolar ribonucleoprotein protein MPP10SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Note=Fibrillar region of the nucleolus. After dissolution of the nucleolus in early M phase becomes associated with chromosomes through metaphase and anaphase. In telophase localized to small cellular prenucleolar bodies that not always contain fibrillarin. The reassociation with nucleolus is preceeded by the arrival of fibrillarin.negative regulation of phosphatase activity [GO:0010923]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; rRNA processing [GO:0006364]chromosome [GO:0005694]; Mpp10 complex [GO:0034457]; nucleolus [GO:0005730]; small nucleolar ribonucleoprotein complex [GO:0005732]; small-subunit processome [GO:0032040]FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.Q9H204MED286Mediator of RNA polymerase II transcription subunit 28SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15467741}. Cytoplasm {ECO:0000269|PubMed:15467741}. Membrane {ECO:0000269|PubMed:15467741}; Peripheral membrane protein {ECO:0000269|PubMed:15467741}. Note=According to PubMed:15467741, it is cytoplasmic and mainly membrane-associated.negative regulation of smooth muscle cell differentiation [GO:0051151]; regulation of transcription, DNA-templated [GO:0006355]; stem cell maintenance [GO:0019827]; transcription, DNA-templated [GO:0006351]^cortical actin cytoskeleton [GO:0030864]; mediator complex [GO:0016592]; membrane [GO:0016020]FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May be part of a complex containing NF2/merlin that participates in cellular signaling to the actin cytoskeleton downstream of tyrosine kinase signaling pathways. {ECO:0000269|PubMed:15467741}.Q9BZH6WDR11WD repeat-containing protein 11SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:20887964}. Nucleus {ECO:0000269|PubMed:20887964}. Note=Might be shuttling between the nucleus and the cytoplasm.cilium [GO:0005929]; cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]Q6P3R8NEK5< $Serine/threonine-protein kinase Nek5positive regulation of cysteine-type endopeptidase activity [GO:2001056]; positive regulation of striated muscle cell differentiation [GO:0051155]; protein phosphorylation [GO:0006468]O95757HS74LHeat shock 70 kDa protein 4LSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=May translocate to the nucleus after heat shock. {ECO:0000250}.Gprotein folding [GO:0006457]; response to unfolded protein [GO:0006986]qFUNCTION: Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. {ECO:0000250}.Q9UDY4DNJB4!DnaJ homolog subfamily B member 4SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Cytoplasmic according to PubMed:18837411 and membrane-associated according to PubMed:16542645.fprotein folding [GO:0006457]; response to heat [GO:0009408]; response to unfolded protein [GO:0006986]FUNCTION: Probable chaperone.Q6UW78CK083UPF0723 protein C11orf83SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}; Single-pass membrane protein {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}.cristae formation [GO:0042407]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrial respiratory chain complex III assembly [GO:0034551]; mitochondrial respiratory chain complex III biogenesis [GO:0097033]Hcardiolipin binding [GO:1901612]; phosphatidic acid binding [GO:0070300]FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. {ECO:0000269|PubMed:25008109, ECO:0000269|PubMed:25605331}.Q8WVN6SCTM1$Secreted and transmembrane protein 1oSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted.immune response [GO:0006955]; mesoderm development [GO:0007498]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]Gcytokine activity [GO:0005125]; signal transducer activity [GO:0004871]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]PFUNCTION: May be involved in thymocyte signaling. {ECO:0000269|PubMed:15742156}.P23193TCEA1+Transcription elongation factor A protein 1tDNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; gene expression [GO:0010467]; nucleotide-excision repair [GO:0006289]; positive regulation of exoribonuclease activity [GO:1901919]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; regulation of DNA-templated transcription, elongation [GO:0032784]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.Q9NVA1UQCC1:Ubiquinol-cytochrome-c reductase complex assembly factor 1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:24385928}. Cytoplasmic vesicle {ECO:0000250}. Note=Cytoplasmic vesicular structures. {ECO:0000250}.mitochondrial respiratory chain complex III assembly [GO:0034551]; positive regulation of mitochondrial translation [GO:0070131]\cytoplasmic membrane-bounded vesicle [GO:0016023]; mitochondrial inner membrane [GO:0005743]FUNCTION: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Involved in cytochrome b translation and/or stability. {ECO:0000269|PubMed:24385928}.A8MSI8LYRM9LYR motif-containing protein 9P10619PPGBLysosomal protective proteincellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; glycosphingolipid metabolic process [GO:0006687]; intracellular protein transport [GO:0006886]; positive regulation of catalytic activity [GO:0043085]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]carboxypeptidase activity [GO:0004180]; enzyme activator activity [GO:0008047]; serine-type carboxypeptidase activity [GO:0004185]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FFUNCTION: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. {ECO:0000269|PubMed:1907282}.Q06481APLP2Amyloid-like protein 2|SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000305}.cellular copper ion homeostasis [GO:0006878]; cholesterol metabolic process [GO:0008203]; extracellular matrix organization [GO:0030198]; forebrain development [GO:0030900]; G-protein coupled receptor signaling pathway [GO:0007186]; locomotory behavior [GO:0007626]; mating behavior [GO:0007617]; midbrain development [GO:0030901]; neuromuscular process controlling balance [GO:0050885]; regulation of epidermal growth factor-activated receptor activity [GO:0007176]; regulation of protein binding [GO:0043393]; suckling behavior [GO:0001967]DNA binding [GO:0003677]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; serine-type endopeptidase inhibitor activity [GO:0004867]; transition metal ion binding [GO:0046914]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity). {ECO:0000250}.Q96B97SH3K1.SH3 domain-containing kinase-binding protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junction, synapse, synaptosome. Cell junction, focal adhesion {ECO:0000250}. Note=Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions (By similarity). Colocalized with MAGI2 in synaptosomes (By similarity). {ECO:0000250}._apoptotic process [GO:0006915]; cell-cell signaling [GO:0007267]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; regulation of cell shape [GO:0008360]cell-cell junction [GO:0005911]; cytoplasmic vesicle membr< ane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]BFUNCTION: Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. {ECO:0000250, ECO:0000269|PubMed:11894095, ECO:0000269|PubMed:11894096, ECO:0000269|PubMed:12177062, ECO:0000269|PubMed:12734385, ECO:0000269|PubMed:12771190, ECO:0000269|PubMed:15090612, ECO:0000269|PubMed:15707590, ECO:0000269|PubMed:16177060, ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:21834987}.Q9NRX1PNO1RNA-binding protein PNO1GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15497447}.P24557THASThromboxane-A synthaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8366093}; Multi-pass membrane protein {ECO:0000269|PubMed:8366093}.arachidonic acid metabolic process [GO:0019369]; cyclooxygenase pathway [GO:0019371]; icosanoid metabolic process [GO:0006690]; small molecule metabolic process [GO:0044281]; xenobiotic metabolic process [GO:0006805]heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; thromboxane-A synthase activity [GO:0004796]P14136GFAPGlial fibrillary acidic proteinkSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12058025}. Note=Associated with intermediate filaments.astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; extracellular matrix organization [GO:0030198]; intermediate filament organization [GO:0045109]; long-term synaptic potentiation [GO:0060291]; negative regulation of neuron projection development [GO:0010977]; neuron projection regeneration [GO:0031102]; positive regulation of Schwann cell proliferation [GO:0010625]; regulation of neurotransmitter uptake [GO:0051580]; response to wounding [GO:0009611]astrocyte end-foot [GO:0097450]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intermediate filament [GO:0005882]; membrane [GO:0016020]; myelin sheath [GO:0043209]FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.Q12873CHD3+Chromodomain-helicase-DNA-binding protein 3SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17626165}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in interphase and mitosis.centrosome organization [GO:0051297]; chromatin assembly or disassembly [GO:0006333]; chromatin modification [GO:0016568]; chromatin organization [GO:0006325]; DNA duplex unwinding [GO:0032508]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spindle organization [GO:0007051]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]centrosome [GO:0005813]; cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]EFUNCTION: Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:9804427}.Q9H8H3MET7A!Methyltransferase-like protein 7AESUBCELLULAR LOCATION: Lipid droplet. Endoplasmic reticulum. Membrane.methylation [GO:0032259]zendoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; lipid particle [GO:0005811]; membrane [GO:0016020]P35527K1C9Keratin, type I cytoskeletal 9epidermis development [GO:0008544]; intermediate filament organization [GO:0045109]; skin development [GO:0043588]; spermatogenesis [GO:0007283]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly. {ECO:0000269|PubMed:10218578, ECO:0000269|PubMed:7507869}.Q9Y243AKT3)RAC-gamma serine/threonine-protein kinaseSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20018949}. Cytoplasm {ECO:0000269|PubMed:20018949}. Membrane {ECO:0000269|PubMed:20018949}; Peripheral membrane protein {ECO:0000269|PubMed:20018949}. Note=Membrane-associated after cell stimulation leading to its translocation.umitochondrial genome maintenance [GO:0000002]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]lcytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] FUNCTION: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. {ECO:0000269|PubMed:18524868, ECO:0000269|PubMed:21191416}.Q9Y6R0NUMBLNumb-like proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS. {ECO:0000250}.`adherens junction organization [GO:0034332]; axonogenesis [GO:0007409]; cytokine-mediated signaling pathway [GO:0019221]; lateral ventricle development [GO:0021670]; nervous system development [GO:0007399]; neuroblast division in subventricular zone [GO:0021849]; positive regulation of neurogenesis [GO:0050769]; protein metabolic process [GO:0019538]bFUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zo< ne (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons. {ECO:0000269|PubMed:18299187, ECO:0000269|PubMed:20079715}.Q6P1K2PMF1Polyamine-modulated factor 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585270}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16585270}. Note=Associated with the kinetochore.4cell division [GO:0051301]; chromosome segregation [GO:0007059]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; regulation of transcription, DNA-templated [GO:0006355]; small GTPase mediated signal transduction [GO:0007264]; transcription from RNA polymerase II promoter [GO:0006366][leucine zipper domain binding [GO:0043522]; transcription coactivator activity [GO:0003713]{cytosol [GO:0005829]; MIS12/MIND type complex [GO:0000444]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]wFUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947, ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.Q9ULR0ISY1%Pre-mRNA-splicing factor ISY1 homolog>FUNCTION: May play a role in pre-mRNA splicing. {ECO:0000305}.O75165DJC13"DnaJ homolog subfamily C member 13SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:18256511}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000269|PubMed:18256511}. Endosome membrane {ECO:0000269|PubMed:24643499}.endosome organization [GO:0007032]; osteoblast differentiation [GO:0001649]; protein transport [GO:0015031]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of early endosome to recycling endosome transport [GO:1902954]early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]fFUNCTION: Involved in membrane trafficking through early endosomes, such as the early endosome to recycling endosome transport implicated in the recycling of transferrin and the early endosome to late endosome transport implicated in degradation of EGF and EGFR (PubMed:18256511, PubMed:18307993). Involved in the regulation of endosomal membrane tubulation and regulates th dynamics of SNX1 on the endosomal membrane; via association with FAM21 may link the WASH complex to the retromer SNX-BAR subcomplex (PubMed:24643499). {ECO:0000269|PubMed:18256511, ECO:0000269|PubMed:18307993, ECO:0000269|PubMed:24643499}.Q9UBV8PEF1PeflinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278427}. Membrane {ECO:0000269|PubMed:11278427}; Peripheral membrane protein {ECO:0000269|PubMed:11278427}. Note=Membrane-associated in the presence of Ca(2+).>proteolysis [GO:0006508]; response to calcium ion [GO:0051592]calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; calcium ion binding [GO:0005509]; poly(A) RNA binding [GO:0044822]; protein dimerization activity [GO:0046983]; protein heterodimerization activity [GO:0046982]Qcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]Q7Z5L9I2BP20Interferon regulatory factor 2-binding protein 2}FUNCTION: Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle. {ECO:0000269|PubMed:12799427, ECO:0000269|PubMed:20702774, ECO:0000269|PubMed:21576369}.Q9P265DIP2B%Disco-interacting protein 2 homolog Bgcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]Q13838DX39BSpliceosome RNA helicase DDX39BSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm. Note=Can translocate to the cytoplasm in the presence of MX1. TREX complex assembly seems to occur in regions surrounding nuclear speckles known as perispeckles.cellular response to DNA damage stimulus [GO:0006974]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of DNA damage checkpoint [GO:2000002]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; RNA secondary structure unwinding [GO:0010501]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]; viral mRNA export from host cell nucleus [GO:0046784]ATP binding [GO:0005524]; ATP-dependent protein binding [GO:0043008]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]; RNA-dependent ATPase activity [GO:0008186]; U4 snRNA binding [GO:0030621]; U6 snRNA binding [GO:0017070]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; transcription export complex [GO:0000346]fFUNCTION: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability.; FUNCTION: Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect.Q9Y3B9RRP15RRP15-like proteinHmitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]P05120PAI2!Plasminogen activator inhibitor 2?SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space.blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endopeptidase activity [GO:0010951]ycytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derive< d PAI-1.Q32P28P3H1Prolyl 3-hydroxylase 1 SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum.; SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). {ECO:0000269|PubMed:19088120}.[bone development [GO:0060348]; cell growth [GO:0016049]; chaperone-mediated protein folding [GO:0061077]; collagen fibril organization [GO:0030199]; collagen metabolic process [GO:0032963]; extracellular matrix organization [GO:0030198]; negative regulation of cell proliferation [GO:0008285]; negative regulation of post-translational protein modification [GO:1901874]; peptidyl-proline hydroxylation [GO:0019511]; protein folding [GO:0006457]; protein hydroxylation [GO:0018126]; protein stabilization [GO:0050821]; regulation of ossification [GO:0030278]; regulation of protein secretion [GO:0050708]iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-proline 3-dioxygenase activity [GO:0019797]; protein complex binding [GO:0032403]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; macromolecular complex [GO:0032991]; membrane [GO:0016020]; nucleus [GO:0005634]; proteinaceous extracellular matrix [GO:0005578]wFUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. {ECO:0000269|PubMed:10951563}.Q9Y4G2PKHM17Pleckstrin homology domain-containing family M member 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:20943950}. Lysosome {ECO:0000269|PubMed:25500191}. Lysosome membrane {ECO:0000269|PubMed:25498145}. Note=Localizes to the external membrane of autolysosomes (PubMed:25498145). In case of infection colocalizes with Salmonella typhimurium sifA in proximity of Salmonella-containing vacuole (SCV) (PubMed:25500191). {ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:25500191}.fautophagy [GO:0006914]; intracellular signal transduction [GO:0035556]; protein transport [GO:0015031]?endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]FUNCTION: Proposed to act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. Required for late stages of endolysosomal maturation, facilitating both endocytosis-mediated degradation of growth factor receptors and autophagosome clearance. Seems to be involved in the terminal maturation of autophagosomes and to mediate autophagosome-lysosome fusion (PubMed:25498145). Involved in vesicular transport in the osteoclast (By similarity). May be involved in negative regulation of endocytic transport from early endosome to late endosome/lysosome implicating its association with Rab7 (PubMed:20943950). May have a role in sialyl-lex-mediated transduction of apoptotic signals (PubMed:12820725). In case of infection contributes to Salmonella typhimurium pathogenesis by supporting the integrity of the Salmonella-containing vacuole (SCV) probably in concert with the HOPS complex and Rab7 (PubMed:25500191). {ECO:0000250|UniProtKB:Q5PQS0, ECO:0000269|PubMed:12820725, ECO:0000269|PubMed:20943950, ECO:0000269|PubMed:25498145, ECO:0000269|PubMed:25500191, ECO:0000305}.Q96J84KIRR1Kin of IRRE-like protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly located at podocyte slit diaphragm.excretion [GO:0007588]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of actin filament polymerization [GO:0030838]; single organismal cell-cell adhesion [GO:0016337]myosin binding [GO:0017022]cell-cell junction [GO:0005911]; cell projection membrane [GO:0031253]; dendritic shaft [GO:0043198]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Plays a significant role in the normal development and function of the glomerular permeability. Signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity). {ECO:0000250}.Q2LD37K1109 Uncharacterized protein KIAA1109bregulation of cell growth [GO:0001558]; regulation of epithelial cell differentiation [GO:0030856]Q69YU3AN34A,Ankyrin repeat domain-containing protein 34AP19320VCAM1 Vascular cell adhesion protein 1 inflammationamine metabolic process [GO:0009308]; B cell differentiation [GO:0030183]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; cytokine-mediated signaling pathway [GO:0019221]; extracellular matrix organization [GO:0030198]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; interferon-gamma-mediated signaling pathway [GO:0060333]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte tethering or rolling [GO:0050901]; membrane to membrane docking [GO:0022614]; oxidation-reduction process [GO:0055114]; positive regulation of T cell proliferation [GO:0042102]; regulation of immune response [GO:0050776]; viral process [GO:0016032]wcell adhesion molecule binding [GO:0050839]; integrin binding [GO:0005178]; primary amine oxidase activity [GO:0008131]alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex [GO:0071065]; apical part of cell [GO:0045177]; cell surface [GO:0009986]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; podosome [GO:0002102]sFUNCTION: Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.Q08357S20A2(Sodium-dependent phosphate transporter 2{SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9151850}; Multi-pass membrane protein {ECO:0000269|PubMed:9151850}.ion transport [GO:0006811]; phosphate ion transmembrane transport [GO:0035435]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]; transport [GO:0006810]inorganic phosphate transmembrane transporter activity [GO:0005315]; receptor activity [GO:0004872]; sodium:inorganic phosphate symporter activity [GO:0015319]; sodium:phosphate symporter activity [GO:0005436]; virus receptor activity [GO:0001618]FUNCTION: Sodium-phosphate symporter which seems to play a fundamental housekeeping role in phosphate transport by absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. In vitro, sodium-dependent phosphate uptake is not siginificantly affected by acidic and alkaline conditions, however sodium-independent phosphate uptake occurs at acidic conditions. May play a role in extracellular matrix, cartilage and vascular calcification. Functions as a retroviral receptor and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. {ECO:0000269|PubMed:11435563, ECO:0000269|PubMed:12205090, ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:8302848}.Q7Z4W1DCXRL-xylulose reductaseSUBCELLULAR LOCATION: Membrane {ECO:0000250}; Periphera< l membrane protein {ECO:0000250}. Note=Probably recruited to membranes via an interaction with phosphatidylinositol. {ECO:0000250}.D-xylose metabolic process [GO:0042732]; glucose metabolic process [GO:0006006]; NADP metabolic process [GO:0006739]; oxidation-reduction process [GO:0055114]; protein homotetramerization [GO:0051289]; xylulose metabolic process [GO:0005997]L-xylulose reductase (NADP+) activity [GO:0050038]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]brush border [GO:0005903]; cytoplasmic microtubule [GO:0005881]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microvillus [GO:0005902]; nucleus [GO:0005634]FUNCTION: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.P48730KC1DCasein kinase I isoform deltaSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity.circadian regulation of gene expression [GO:0032922]; DNA repair [GO:0006281]; endocytosis [GO:0006897]; G2/M transition of mitotic cell cycle [GO:0000086]; Golgi organization [GO:0007030]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; nonmotile primary cilium assembly [GO:0035058]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; protein localization to centrosome [GO:0071539]; protein localization to cilium [GO:0061512]; protein localization to Golgi apparatus [GO:0034067]; protein phosphorylation [GO:0006468]; regulation of cell shape [GO:0008360]; regulation of circadian rhythm [GO:0042752]; signal transduction [GO:0007165]; spindle assembly [GO:0051225]; Wnt signaling pathway [GO:0016055]ATP binding [GO:0005524]; peptide binding [GO:0042277]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle [GO:0005819]; spindle microtubule [GO:0005876]'FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phospohorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate. {ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:16027726, ECO:0000269|PubMed:17562708, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:19043076, ECO:0000269|PubMed:19339517, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20048001, ECO:0000269|PubMed:20407760, ECO:0000269|PubMed:20637175, ECO:0000269|PubMed:20696890, ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:21084295, ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:23636092}.P39687AN32A=Acidic leucine-rich nuclear phosphoprotein 32 family member ASUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm. {ECO:0000250}.gene expression [GO:0010467]; intracellular signal transduction [GO:0035556]; nucleocytoplasmic transport [GO:0006913]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]TFUNCTION: Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression. {ECO:0000269|PubMed:10400610, ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:15642345, ECO:0000269|PubMed:17557114}.Q9BU76MMTA2+Multiple myeloma tumor-associated protein 2Q9Y4L1HYOU1Hypoxia up-regulated protein 1&cellular protein metabolic process [GO:0044267]; cellular response to hypoxia [GO:0071456]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903382]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; receptor-mediated endocytosis [GO:0006898]; response to endoplasmic reticulum stress [GO:0034976]; response to ischemia [GO:0002931]8ATP binding [GO:0005524]; chaperone binding [GO:0051087]Nendocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; membrane [GO:0016020]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding. {ECO:0000269|PubMed:10037731}.Q9BTE3MCMBP3Mini-chromosome maintenance complex-binding protein`SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17296731}. Note=Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chromatin later than component of the MCM complex.cell division [GO:0051301]; DNA-dependent DNA replication [GO:0006261]; mitotic nuclear division [GO:0007067]; sister chromatid< cohesion [GO:0007062](FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion. {ECO:0000269|PubMed:20090939, ECO:0000269|PubMed:21196493}.Q04828AK1C1&Aldo-keto reductase family 1 member C1bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; cellular response to jasmonic acid stimulus [GO:0071395]; cholesterol homeostasis [GO:0042632]; daunorubicin metabolic process [GO:0044597]; digestion [GO:0007586]; doxorubicin metabolic process [GO:0044598]; epithelial cell differentiation [GO:0030855]; intestinal cholesterol absorption [GO:0030299]; oxidation-reduction process [GO:0055114]; phototransduction, visible light [GO:0007603]; progesterone metabolic process [GO:0042448]; protein homooligomerization [GO:0051260]; response to organophosphorus [GO:0046683]; retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; xenobiotic metabolic process [GO:0006805]z17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity [GO:0047006]; alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; androsterone dehydrogenase (B-specific) activity [GO:0047042]; bile acid binding [GO:0032052]; carboxylic acid binding [GO:0031406]; indanol dehydrogenase activity [GO:0047718]; ketosteroid monooxygenase activity [GO:0047086]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; phenanthrene 9,10-monooxygenase activity [GO:0018636]; trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity [GO:0047115]rFUNCTION: Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation. {ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067}.O75937DNJC8!DnaJ homolog subfamily C member 8Q96G23CERS2Ceramide synthase 2endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear membrane [GO:0031965][FUNCTION: Suppresses the growth of cancer cells. May be involved in sphingolipid synthesis.P78347GTF2I!General transcription factor II-ISUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10373551}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00484, ECO:0000269|PubMed:10373551}. Note=Colocalizes with BTK in the cytoplasm. negative regulation of angiogenesis [GO:0016525]; signal transduction [GO:0007165]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transition between slow and fast fiber [GO:0014886]cell projection [GO:0042995]; cytoplasm [GO:0005737]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]&FUNCTION: Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, ECO:0000269|PubMed:16738337}.Q6FIF0ZFAN6AN1-type zinc finger protein 6apoptotic process [GO:0006915]; cellular response to tumor necrosis factor [GO:0071356]; negative regulation of apoptotic process [GO:0043066]; protein targeting to peroxisome [GO:0006625]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122][DNA binding [GO:0003677]; polyubiquitin binding [GO:0031593]; zinc ion binding [GO:0008270]FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B activation and apoptosis. Involved in modulation of 'Lys-48'-linked polyubiquitination status of TRAF2 and decreases association of TRAF2 with RIPK1. Required for PTS1 target sequence-dependent protein import into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes (By similarity). {ECO:0000250}.Q96JC1VPS39Vam6/Vps39-like proteinQSUBCELLULAR LOCATION: Cytoplasm. Lysosome membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein. Late endosome {ECO:0000269|PubMed:23167963}. Lysosome {ECO:0000269|PubMed:23167963}. Note=Colocalizes with TGFBR1 and TGFBR2 in cytoplasmic vesicular structures and most prominently in cortical vesicles.3autophagy [GO:0006914]; endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; late endosome to lysosome transport [GO:1902774]; retrograde transport, endosome to plasma membrane [GO:1990126]; vesicle-mediated transport [GO:0016192]_HOPS complex [GO:0030897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]FUNCTION: Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2-dependent transcription. Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation. {ECO:0000269|PubMed:12941698}.; FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (PubMed:23351085). Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes (PubMed:11448994, PubMed:23351085, PubMed:23167963). Required for fusion of endosomes and autophagosomes with lysosomes (PubMed:25783203). {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:25783203, ECO:0000305|PubMed:23351085}.Q9UI42CBPA4Carboxypeptidase A4:histone acetylation [GO:0016573]; proteolysis [GO:0006508]Lmetallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]xFUNCTION: Metalloprotease that could be involved in the histone hyperacetylation pathway. {ECO:0000269|PubMed:10383164}.P20700LMNB1Lamin-B1apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; programmed cell death [GO:0012501]lamin filament [GO:0005638]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]O15234CASC3 Protein CASC3.SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Nucleus speckle. Note=Predominantly found in the perinuclear region (B< y similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Shuttles between the cytoplasm and the stress granules. More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. Colocalizes in nuclear speckles with MAGOH. Under stress condition, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules, which contain stored mRNAs whose translation is stopped in response to stress. {ECO:0000250}.gene expression [GO:0010467]; intracellular mRNA localization [GO:0008298]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translation [GO:0006417]; RNA splicing [GO:0008380]enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; ubiquitin protein ligase binding [GO:0031625]cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; nuclear speck [GO:0016607]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:0030529]FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer. {ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:17652158}.Q460N5PAR14Poly [ADP-ribose] polymerase 14SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In steady state cells the protein is mostly nuclear. A minor proportion is detected in the cytoplasm (By similarity). {ECO:0000250}.acytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. {ECO:0000250, ECO:0000269|PubMed:16061477}.Q9NWK9BCD1Box C/D snoRNA protein 1Fbox C/D snoRNP assembly [GO:0000492]; ribosome biogenesis [GO:0042254]cenzyme binding [GO:0019899]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]Cextracellular exosome [GO:0070062]; pre-snoRNP complex [GO:0070761]FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. {ECO:0000269|PubMed:17636026}.Q9HCD5NCOA5Nuclear receptor coactivator 5glucose homeostasis [GO:0042593]; negative regulation of insulin receptor signaling pathway [GO:0046627]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]qactin cytoskeleton [GO:0015629]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2). {ECO:0000269|PubMed:15073177}.A6NGZ7U93BL/Putative protein unc-93 homolog B1-like proteinO14795UN13BProtein unc-13 homolog B9SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Localized to synapses. Translocated to the plasma membrane in response to phorbol ester binding (By similarity). {ECO:0000250}.apoptotic process [GO:0006915]; excretion [GO:0007588]; glutamate secretion [GO:0014047]; innervation [GO:0060384]; intracellular signal transduction [GO:0035556]; neuromuscular junction development [GO:0007528]; neurotransmitter secretion [GO:0007269]; positive regulation of inhibitory postsynaptic membrane potential [GO:0097151]; positive regulation of synaptic vesicle priming [GO:0010808]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; signal transduction [GO:0007165]; synaptic transmission [GO:0007268]; synaptic transmission, glutamatergic [GO:0035249]; synaptic vesicle docking [GO:0016081]; synaptic vesicle priming [GO:0016082]diacylglycerol binding [GO:0019992]; metal ion binding [GO:0046872]; receptor activity [GO:0004872]; signal transducer activity [GO:0004871]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; terminal bouton [GO:0043195]FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). {ECO:0000250}.Q9HCE5MET14.N6-adenosine-methyltransferase subunit METTL14YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421}.mRNA destabilization [GO:0061157]; mRNA methylation [GO:0080009]; mRNA splicing, via spliceosome [GO:0000398]; stem cell maintenance [GO:0019827]amRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA binding [GO:0003723]HMIS complex [GO:0036396]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]@FUNCTION: N6-methyltransferase that methylates adenosine residues of some mRNAs and acts as a regulator of the circadian clock and differentiation of embryonic stem cells. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing, processing and mRNA stability (PubMed:24316715, PubMed:24407421, PubMed:25719671). M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop. M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity). {ECO:0000250|UniProtKB:Q3UIK4, ECO:0000269|PubMed:24316715, ECO:0000269|PubMed:24407421, ECO:0000269|PubMed:25719671}.O00534VMA5A4von Willebrand factor A domain-containing protein 5AFUNCTION: May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in, may contribute directly to or modify tumorigenesis.O15126SCAM1/Secretory carrier-associated membrane protein 1kexocytosis [GO:0006887]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]clathrin-coated vesicle [GO:0030136]; integral component of membrane [GO:0016021]; recycling endosome membrane [GO:0055038]; synaptic vesicle membrane [GO:0030672]; t< rans-Golgi network [GO:0005802]; zymogen granule membrane [GO:0042589]Q9NVJ2ARL8B'ADP-ribosylation factor-like protein 8BSUBCELLULAR LOCATION: Late endosome membrane. Lysosome membrane. Cytoplasm, cytoskeleton, spindle. Note=According to PubMed:15331635, it localizes with microtubules at the spindle mid-zone during mitosis.cell cycle [GO:0007049]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; small GTPase mediated signal transduction [GO:0007264]alpha-tubulin binding [GO:0043014]; beta-tubulin binding [GO:0048487]; GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; midbody [GO:0030496]; spindle midzone [GO:0051233]FUNCTION: May play a role in lysosome motility (PubMed:16537643). May play a role in chromosome segregation (PubMed:15331635). {ECO:0000269|PubMed:15331635, ECO:0000269|PubMed:16537643}.P28289TMOD1Tropomodulin-1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574). {ECO:0000269|PubMed:25250574}.actin filament organization [GO:0007015]; adult locomotory behavior [GO:0008344]; lens fiber cell development [GO:0070307]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]cortical cytoskeleton [GO:0030863]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; myofibril [GO:0030016]; nucleus [GO:0005634]; striated muscle thin filament [GO:0005865]FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus. {ECO:0000269|PubMed:8002995}.P43121MUC18Cell surface glycoprotein MUC18anatomical structure morphogenesis [GO:0009653]; angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; glomerular filtration [GO:0003094]; positive regulation of cell migration [GO:0030335]; vascular wound healing [GO:0061042]external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; plasma membrane [GO:0005886]DFUNCTION: Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration. {ECO:0000269|PubMed:11036077, ECO:0000269|PubMed:8292890}.O75487GPC4 Glypican-4SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted glypican-4: Secreted, extracellular space {ECO:0000250}.anatomical structure morphogenesis [GO:0009653]; carbohydrate metabolic process [GO:0005975]; cell proliferation [GO:0008283]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; phototransduction, visible light [GO:0007603]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]qanchored component of membrane [GO:0031225]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system (By similarity). {ECO:0000250}.Q8NEF9SRFB1'Serum response factor-binding protein 1SSUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9CZ91}.`90S preribosome [GO:0030686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells (By similarity). {ECO:0000250|UniProtKB:Q9CZ91}.Q96SQ7ATOH8Protein atonal homolog 8SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24463812}. Nucleus speckle {ECO:0000269|PubMed:24463812}. Cytoplasm {ECO:0000250|UniProtKB:Q99NA2}.bcell differentiation [GO:0030154]; formation of primary germ layer [GO:0001704]; myoblast proliferation [GO:0051450]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of transcription, DNA-templated [GO:0045892]; nervous system development [GO:0007399]; positive regulation of endothelial cell differentiation [GO:0045603]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of transcription, DNA-templated [GO:0045893]; SMAD protein signal transduction [GO:0060395]; transcription, DNA-templated [GO:0006351]; tube formation [GO:0035148]dE-box binding [GO:0070888]; sequence-specific DNA binding transcription factor activity [GO:0003700]Hcytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]4FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (PubMed:24236640). Regulates endothelial cell proliferation, migration and tube-like structures formation (PubMed:24463812). Modulates endothelial cell differentiation through NOS3 (PubMed:24463812). May be implicated in specification and differentiation of neuronal cell lineages in the brain (By similarity). May participate in kidney development and may be involved in podocyte differentiation (By similarity). During early embryonic development is involved in tissue-specific differentiation processes that are dependent on class II bHLH factors and namely modulates the differentiation program initiated by the pro-endocrine factor NEUROG3 (By similarity). During myogenesis, may play a role during the transition of myoblasts from the proliferative phase to the differentiation phase (By similarity). Positively regulates HAMP transcription in two ways, firstly by acting directly on the HAMP promoter via E-boxes binding and indirectly through increased phosphorylation of SMAD protein complex (PubMed:24236640). Repress NEUROG3-dependent gene activation in a gene-specific manner through at least two mechanisms; requires only either the sequestering of a general partner such as TCF3 through heterodimerization, either also requires binding of the bHLH domain to DNA via a basic motif (By similarity). {ECO:0000250|UniProtKB:Q99NA2, ECO:0000269|PubMed:24236640, ECO:0000269|PubMed:24463812}.Q9BVC4LST8(Target of rapamycin complex subunit LST8cell cycle arrest [GO:0007050]; cellular response to heat [GO:0034605]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of peptidyl-tyrosine< phosphorylation [GO:0050731]; positive regulation of TOR signaling [GO:0032008]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cellular response to heat [GO:1900034]; regulation of GTPase activity [GO:0043087]; T cell costimulation [GO:0031295]; transcription initiation from RNA polymerase II promoter [GO:0006367]; vascular endothelial growth factor receptor signaling pathway [GO:0048010],FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. {ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15467718}.Q9NP84TNR125Tumor necrosis factor receptor superfamily member 12Aangiogenesis [GO:0001525]; extrinsic apoptotic signaling pathway [GO:0097191]; positive regulation of apoptotic process [GO:0043065]; positive regulation of axon extension [GO:0045773]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; regulation of angiogenesis [GO:0045765]; regulation of wound healing [GO:0061041]; substrate-dependent cell migration, cell attachment to substrate [GO:0006931]ycell surface [GO:0009986]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; ruffle [GO:0001726]FUNCTION: Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins. {ECO:0000269|PubMed:11728344}.Q9H4I2ZHX3%Zinc fingers and homeoboxes protein 3bSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12659632}.!cell differentiation [GO:0030154]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of osteoblast differentiation [GO:0045669]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]&FUNCTION: Acts as a transcriptional repressor. Involved in the early stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a regulator of podocyte gene expression during primary glomerula disease. Binds to promoter DNA. {ECO:0000269|PubMed:12659632, ECO:0000269|PubMed:21174497}.Q8NI08NCOA7Nuclear receptor coactivator 7|positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; nuclear hormone receptor binding [GO:0035257]FUNCTION: Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA. {ECO:0000269|PubMed:11971969}.Q03113GNA123Guanine nucleotide-binding protein subunit alpha-12tadenylate cyclase-modulating G-protein coupled receptor signaling pathway [GO:0007188]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; embryonic digit morphogenesis [GO:0042733]; G-protein coupled receptor signaling pathway [GO:0007186]; in utero embryonic development [GO:0001701]; platelet activation [GO:0030168]; regulation of cell shape [GO:0008360]; regulation of fibroblast migration [GO:0010762]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of TOR signaling [GO:0032006]; response to drug [GO:0042493]; Rho protein signal transduction [GO:0007266]D5 dopamine receptor binding [GO:0031752]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; signal transducer activity [GO:0004871]brush border membrane [GO:0031526]; focal adhesion [GO:0005925]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886]FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade. {ECO:0000269|PubMed:22609986}.O95793STAU15Double-stranded RNA-binding protein Staufen homolog 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19029303}. Rough endoplasmic reticulum {ECO:0000269|PubMed:19029303}. Note=Localizes exclusively with the rough reticulum endoplasmic (RER).intracellular mRNA localization [GO:0008298]; positive regulation by virus of viral protein levels in host cell [GO:0046726]; positive regulation of viral genome replication [GO:0045070]cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; microtubule associated complex [GO:0005875]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.O60503ADCY9Adenylate cyclase type 9nactivation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; adenylate cyclase-activating G-protein coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; neurotrophin TRK receptor signaling pathway [GO:0048011]; renal water homeostasis [GO:0003091]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; transmembrane transport [GO:0055085]; water transport [GO:0006833]aadenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]lintegral component of plasma membrane [GO:0005887]; intracellular [GO:00056< 22]; plasma membrane [GO:0005886]FUNCTION: May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin (By similarity). {ECO:0000250}.Q86TB9PATL1Protein PAT1 homolog 1ESUBCELLULAR LOCATION: Cytoplasm, P-body. Nucleus. Nucleus, PML body. Nucleus speckle. Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Enriched in splicing speckles. Localization to nuclear foci and speckles requires active transcription. Excluded from the nucleolus.jcytoplasmic mRNA processing body assembly [GO:0033962]; deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]zpoly(A) RNA binding [GO:0044822]; poly(G) binding [GO:0034046]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; PML body [GO:0016605]FUNCTION: RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV). {ECO:0000269|PubMed:17936923, ECO:0000269|PubMed:19628699, ECO:0000269|PubMed:20543818, ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:20852261}.O75326SEM7A Semaphorin-7ASUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Extracellular side {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}. Note=Detected in a punctate pattern on the cell membrane of basal and supra-basal skin keratinocytes.axon extension [GO:0048675]; axon guidance [GO:0007411]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; olfactory lobe development [GO:0021988]; osteoblast differentiation [GO:0001649]; positive regulation of axon extension [GO:0045773]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage cytokine production [GO:0060907]; regulation of inflammatory response [GO:0050727]anchored component of membrane [GO:0031225]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Plays an important role in integrin-mediated signaling and functions both in regulating cell migration and immune responses. Promotes formation of focal adhesion complexes, activation of the protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and MAPK3. Promotes production of proinflammatory cytokines by monocytes and macrophages. Plays an important role in modulating inflammation and T-cell-mediated immune responses. Promotes axon growth in the embryonic olfactory bulb. Promotes attachment, spreading and dendrite outgrowth in melanocytes. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:17377534, ECO:0000269|PubMed:17671519}.Q8N6M0OTU6B OTU domain-containing protein 6B-cysteine-type peptidase activity [GO:0008234]P04183KITHThymidine kinase, cytosolicLdeoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; digestive tract development [GO:0048565]; DNA biosynthetic process [GO:0071897]; fetal process involved in parturition [GO:0060138]; liver development [GO:0001889]; nucleobase-containing compound metabolic process [GO:0006139]; nucleobase-containing small molecule metabolic process [GO:0055086]; nucleotide biosynthetic process [GO:0009165]; protein homotetramerization [GO:0051289]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside salvage [GO:0043097]; response to copper ion [GO:0046688]; response to cortisol [GO:0051414]; response to nutrient levels [GO:0031667]; response to toxic substance [GO:0009636]; skeletal muscle cell proliferation [GO:0014856]; small molecule metabolic process [GO:0044281]; thymidine metabolic process [GO:0046104]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; nucleoside kinase activity [GO:0019206]; thymidine kinase activity [GO:0004797]; zinc ion binding [GO:0008270]Q9H2U1DHX36 ATP-dependent RNA helicase DHX36SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome, telomere {ECO:0000305}. Note=Isoform 1 preferentially localized to the nucleus and isoform 2 localized to the cytoplasm. However, partitioning of cellular localization between the nucleus and cytoplasm is not exclusive, as isoform 1 was also detected in the cytoplasm. Both isoforms were excluded from nucleoli. Localizes to cytoplasmic stress granules.innate immune response [GO:0045087]; ossification [GO:0001503]; positive regulation of telomere maintenance [GO:0032206]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RNA processing [GO:0006396]; RNA secondary structure unwinding [GO:0010501]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; core promoter binding [GO:0001047]; DNA-dependent ATPase activity [GO:0008094]; double-stranded RNA binding [GO:0003725]; G-quadruplex DNA binding [GO:0051880]; G-quadruplex RNA binding [GO:0002151]; histone deacetylase binding [GO:0042826]; poly(A) RNA binding [GO:0044822]; transcription regulatory region DNA binding [GO:0044212]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]FUNCTION: Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification. {ECO:0000269|PubMed:12198572, ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:16150737, ECO:0000269|PubMed:18842585, ECO:0000269|PubMed:20472641, ECO:0000269|PubMed:21149580, ECO:0000269|PubMed:21586581, ECO:0000269|PubMed:21993297, ECO:0000269|PubMed:22238380}.Q03519TAP2Antigen peptide transporter 2antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent [GO:0002489]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent [GO:0002481]; antigen processing and presentation of peptid< e antigen via MHC class I [GO:0002474]; cytosol to ER transport [GO:0046967]; intracellular transport of viral protein in host cell [GO:0019060]; peptide antigen transport [GO:0046968]; positive regulation of antigen processing and presentation of peptide antigen via MHC class I [GO:0002591]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; MHC class Ib protein binding [GO:0023029]; peptide antigen-transporting ATPase activity [GO:0015433]; TAP1 binding [GO:0046978]; tapasin binding [GO:0046980]; transporter activity [GO:0005215]endoplasmic reticulum membrane [GO:0005789]; host cell [GO:0043657]; integral component of endoplasmic reticulum membrane [GO:0030176]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; TAP complex [GO:0042825]QFUNCTION: Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association.Q6P158DHX57)Putative ATP-dependent RNA helicase DHX57ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]Q14315FLNC Filamin-C SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11038172}. Membrane {ECO:0000269|PubMed:11038172}; Peripheral membrane protein {ECO:0000269|PubMed:11038172}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11038172}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11038172}. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fraction localizes with subsarcolemme. Targeting to developing and mature Z lines is mediated by the intradomain insert.Jcell junction assembly [GO:0034329]; muscle fiber development [GO:0048747]Gankyrin binding [GO:0030506]; cytoskeletal protein binding [GO:0008092]costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; Z disc [GO:0030018]FUNCTION: Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.Q9H2D1MFTC(Mitochondrial folate transporter/carrierfolic acid metabolic process [GO:0046655]; folic acid transport [GO:0015884]; mitochondrial transport [GO:0006839]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767],folic acid transporter activity [GO:0008517]GFUNCTION: Transports folate across the inner membranes of mitochondria.Q8NDA8MROH1;Maestro heat-like repeat-containing protein family member 1P08473NEP Neprilysinangiotensin maturation [GO:0002003]; beta-amyloid metabolic process [GO:0050435]; cellular protein metabolic process [GO:0044267]; cellular response to cytokine stimulus [GO:0071345]; cellular response to UV-A [GO:0071492]; cellular response to UV-B [GO:0071493]; creatinine metabolic process [GO:0046449]; kidney development [GO:0001822]; peptide metabolic process [GO:0006518]; proteolysis [GO:0006508]; replicative senescence [GO:0090399]; sensory perception of pain [GO:0019233]endopeptidase activity [GO:0004175]; exopeptidase activity [GO:0008238]; metalloendopeptidase activity [GO:0004222]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]yaxon [GO:0030424]; brush border [GO:0005903]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; neuron projection terminus [GO:0044306]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573, ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:2972276}.Q86V87F16B2Protein FAM160B2Q96CC6RHDF1Inactive rhomboid protein 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Predominantly localized in the endoplasmic reticulum membrane.lcell migration [GO:0016477]; cell proliferation [GO:0008283]; negative regulation of protein secretion [GO:0050709]; protein transport [GO:0015031]; proteolysis [GO:0006508]; regulation of epidermal growth factor receptor signaling pathway [GO:0042058]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein secretion [GO:0050708]FUNCTION: Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration. {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:18524845, ECO:0000269|PubMed:18832597, ECO:0000269|PubMed:21439629}.O14787TNPO2 Transportin-22nuclear localization sequence binding [GO:0008139](FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}.Q9NWY4CD027UPF0609 protein C4orf27Q12816TROP Trophininembryo implantation [GO:0007566]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell growth [GO:0030308]~cytoplasm [GO:0005737]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Could be involved with bystin and tastin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation. Directly responsible for homophilic cell adhesion.Q86VI3IQGA3)Ras GTPase-activating-like protein IQGAP3activation of MAPK activity [GO:0000187]; cellular response to organ< ic substance [GO:0071310]; ERK1 and ERK2 cascade [GO:0070371]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of mammary gland epithelial cell proliferation [GO:0033601]; Ras protein signal transduction [GO:0007265]; regulation of cell size [GO:0008361]; small GTPase mediated signal transduction [GO:0007264]scalmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; myosin VI light chain binding [GO:0070856][cell-cell junction [GO:0005911]; cytosol [GO:0005829]; lateral plasma membrane [GO:0016328]P35790CHKACholine kinase alphaCDP-choline pathway [GO:0006657]; choline metabolic process [GO:0019695]; glycerophospholipid biosynthetic process [GO:0046474]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; choline binding [GO:0033265]; choline kinase activity [GO:0004103]; cholinesterase activity [GO:0004104]; drug binding [GO:0008144]; ethanolamine kinase activity [GO:0004305]; signal transducer activity [GO:0004871]<FUNCTION: Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline. {ECO:0000269|PubMed:19915674}.A6NL28TPM3L/Putative tropomyosin alpha-3 chain-like proteinQ96S06LMF1Lipase maturation factor 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19783858, ECO:0000269|PubMed:24909692}; Multi-pass membrane protein {ECO:0000269|PubMed:19783858, ECO:0000269|PubMed:24909692}.chylomicron remnant clearance [GO:0034382]; ER to Golgi vesicle-mediated transport [GO:0006888]; positive regulation of lipoprotein lipase activity [GO:0051006]; protein glycosylation in Golgi [GO:0033578]; protein maturation [GO:0051604]; protein secretion [GO:0009306]; regulation of cholesterol metabolic process [GO:0090181]; regulation of triglyceride metabolic process [GO:0090207]vendoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]&FUNCTION: Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL. {ECO:0000250, ECO:0000269|PubMed:24909692}.Q9UJJ9GNPTG6N-acetylglucosamine-1-phosphotransferase subunit gammalSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15532026}. Golgi apparatus {ECO:0000269|PubMed:15532026}.Wcarbohydrate phosphorylation [GO:0046835]; N-glycan processing to lysosome [GO:0016256]protein homodimerization activity [GO:0042803]; UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity [GO:0003976]]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]FUNCTION: Non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors. {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:19955174}.P07738PMGEBisphosphoglycerate mutasecarbohydrate metabolic process [GO:0005975]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; regulation of pentose-phosphate shunt [GO:0043456]; respiratory gaseous exchange [GO:0007585]2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate 2-phosphatase activity [GO:0004083]; bisphosphoglycerate mutase activity [GO:0004082]FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.Q15124PGM5!Phosphoglucomutase-like protein 5SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:8175905}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8175905}. Note=Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments.Gcarbohydrate metabolic process [GO:0005975]; cell adhesion [GO:0007155]intramolecular transferase activity, phosphotransferases [GO:0016868]; magnesium ion binding [GO:0000287]; structural molecule activity [GO:0005198]Vcell-cell adherens junction [GO:0005913]; costamere [GO:0043034]; cytoplasmic side of plasma membrane [GO:0009898]; dystrophin-associated glycoprotein complex [GO:0016010]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; sarcolemma [GO:0042383]; spot adherens junction [GO:0005914]; stress fiber [GO:0001725]; Z disc [GO:0030018]lFUNCTION: Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity.P21926CD9 CD9 antigenSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19640571}; Multi-pass membrane protein {ECO:0000269|PubMed:19640571}. Cell membrane {ECO:0000269|PubMed:19640571}; Multi-pass membrane protein {ECO:0000269|PubMed:19640571}.blood coagulation [GO:0007596]; brain development [GO:0007420]; cell adhesion [GO:0007155]; fusion of sperm to egg plasma membrane [GO:0007342]; movement of cell or subcellular component [GO:0006928]; multicellular organism reproduction [GO:0032504]; negative regulation of cell proliferation [GO:0008285]; oligodendrocyte development [GO:0014003]; paranodal junction assembly [GO:0030913]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; response to water deprivation [GO:0009414]; single fertilization [GO:0007338]apical plasma membrane [GO:0016324]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]FUNCTION: Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion. {ECO:0000269|PubMed:14575715, ECO:0000269|PubMed:7511626, ECO:0000269|PubMed:8478605}.O95218ZRAB23Zinc finger Ran-binding domain-containing protein 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11448987}.pmRNA processing [GO:0006397]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]FUNCTION: Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection. {ECO:0000269|PubMed:11448987}.Q96PK6RBM14RNA-binding protein 14SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; glucocorticoid receptor signaling pathway [GO:0042921]; histone deacetylation [GO:0016575]; intracellular estrogen receptor signaling pathway [GO:0030520]; negative regulation of centriole replication [GO:0046600]; positive regulation of transcription from RNA polymerase II p< romoter [GO:0045944]; response to hormone [GO:0009725]; transcription, DNA-templated [GO:0006351]ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein binding, bridging [GO:0030674]; RNA binding [GO:0003723]; RNA polymerase II transcription cofactor activity [GO:0001104]mediator complex [GO:0016592]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]; transcription factor complex [GO:0005667]"FUNCTION: Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1.P46976GLYG Glycogenin-1Tglycogenin glucosyltransferase activity [GO:0008466]; metal ion binding [GO:0046872]mcytosol [GO:0005829]; extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]P60604UB2G2"Ubiquitin-conjugating enzyme E2 G2rcellular protein catabolic process [GO:0044257]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; protein K48-linked ubiquitination [GO:0070936]; protein N-linked glycosylation via asparagine [GO:0018279]; ubiquitin-dependent protein catabolic process [GO:0006511]Pcytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22607976}.P05787K2C8Keratin, type II cytoskeletal 8SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250}.cell differentiation involved in embryonic placenta development [GO:0060706]; extrinsic apoptotic signaling pathway [GO:0097191]; hepatocyte apoptotic process [GO:0097284]; response to hydrostatic pressure [GO:0051599]; response to other organism [GO:0051707]; sarcomere organization [GO:0045214]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; viral process [GO:0016032]Pscaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]cell-cell junction [GO:0005911]; costamere [GO:0043034]; cytoplasm [GO:0005737]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}.P35580MYH10 Myosin-10SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:22480440}. Note=Colocalizes with MCC at the leading edge of migrating cells.actin filament-based movement [GO:0030048]; actomyosin structure organization [GO:0031032]; adult heart development [GO:0007512]; axon guidance [GO:0007411]; cardiac myofibril assembly [GO:0055003]; cell adhesion [GO:0007155]; cell proliferation [GO:0008283]; cerebellar Purkinje cell layer development [GO:0021680]; ephrin receptor signaling pathway [GO:0048013]; exocytosis [GO:0006887]; fourth ventricle development [GO:0021592]; in utero embryonic development [GO:0001701]; lateral ventricle development [GO:0021670]; mitotic cytokinesis [GO:0000281]; neuromuscular process controlling balance [GO:0050885]; neuron migration [GO:0001764]; nuclear migration [GO:0007097]; plasma membrane repair [GO:0001778]; regulation of cell shape [GO:0008360]; retina development in camera-type eye [GO:0060041]; small GTPase mediated signal transduction [GO:0007264]; substrate-dependent cell migration, cell extension [GO:0006930]; third ventricle development [GO:0021678]; ventricular cardiac muscle cell development [GO:0055015]actin binding [GO:0003779]; actin-dependent ATPase activity [GO:0030898]; actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]actin cytoskeleton [GO:0015629]; actomyosin [GO:0042641]; axon [GO:0030424]; brush border [GO:0005903]; cell cortex [GO:0005938]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; midbody [GO:0030496]; mitochondrion [GO:0005739]; myosin complex [GO:0016459]; myosin II complex [GO:0016460]; myosin II filament [GO:0097513]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle [GO:0005819]; stress fiber [GO:0001725]FUNCTION: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9. {ECO:0000269|PubMed:20052411, ECO:0000269|PubMed:20603131}.O43909EXTL3Exostosin-like 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000269|PubMed:10639137}.Icellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; IRE1-mediated unfolded protein response [GO:0036498]; positive regulation of cell growth [GO:0030307]glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0001888]; metal ion binding [GO:0046872]; receptor activity [GO:0004872]FUNCTION: Probable glycosyltransferase (By similarity). Required for the function of REG3A in regulating keratinocyte proliferation and differentiation. {ECO:0000250, ECO:0000269|PubMed:22727489}.Q6ZP29LAAT1*Lysosomal amino acid transporter 1 homologSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:22822152}; Multi-pass membrane protein {ECO:0000269|PubMed:22822152}.amino acid homeostasis [GO:0080144]; arginine transmembrane transport [GO:1903826]; arginine transport [GO:0015809]; L-lysine transmembrane transport [GO:1903401]; lysine transport [GO:0015819]arginine transmembrane transporter activity [GO:0015181]; basic amino acid transmembrane transporter activity [GO:0015174]; L-lysine transmembrane transporter activity [GO:0015189]integral component of organelle membrane [GO:0031301]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]FUNCTION: Amino acid transporter that specifically mediates the pH-dependent export of the cationic amino acids arginine, histidine and lysine from lysosomes. {ECO:0000269|PubMed:22822152, ECO:0000269|PubMed:23169667}.Q5BJH2TM128Transmembrane protein 128Q9Y296TPPC4.Trafficking protein particle complex subunit 4dendrite development [GO:0016358]; ER to Golgi vesicle-mediated transport [GO:0006888]; extracellular matrix organization [GO:0030198]; positive regulation of GTPase activity [GO:0043547]cis-Golgi network [GO:0005801]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi stack [GO:0005795]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; TRAPP complex [GO:0030008]Q96K83ZN521Zinc finger protein 521cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; regulation of transcription, DNA-te< mplated [GO:0006355]; transcription, DNA-templated [GO:0006351]fDNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Involved in BMP signaling and in the regulation of the immature compartment of the hematopoietic system. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved specification of B-cell lineage; this interaction preventing EBF1 to bind DNA and activate target genes. {ECO:0000269|PubMed:14630787}.O75427LRCH4ELeucine-rich repeat and calponin homology domain-containing protein 4PML body [GO:0016605]Q9NQG1MANBLProtein MANBALQ96PU8QKIProtein quakingz3'-UTR-mediated mRNA destabilization [GO:0061158]; long-chain fatty acid biosynthetic process [GO:0042759]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; muscle cell differentiation [GO:0042692]; myelination [GO:0042552]; positive regulation of gene expression [GO:0010628]; RNA splicing [GO:0008380]; spermatid development [GO:0007286]; vasculogenesis [GO:0001570];mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]0FUNCTION: RNA-binding protein that plays a central role in myelinization (PubMed:16641098). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Regulates target mRNA stability (PubMed:23630077). In addition, acts by regulating pre-mRNA splicing, mRNA export and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B. Regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia (PubMed:16641098). Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:16641098, ECO:0000269|PubMed:23630077}.Q7RTV2GSTA5Glutathione S-transferase A5*glutathione metabolic process [GO:0006749]-glutathione transferase activity [GO:0004364]Q9UDR5AASS6Alpha-aminoadipic semialdehyde synthase, mitochondrialcellular nitrogen compound metabolic process [GO:0034641]; L-lysine catabolic process to acetyl-CoA via saccharopine [GO:0033512]; lysine catabolic process [GO:0006554]; protein tetramerization [GO:0051262]; small molecule metabolic process [GO:0044281]saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity [GO:0047131]; saccharopine dehydrogenase (NADP+, L-lysine-forming) activity [GO:0047130]FUNCTION: Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively.Q9UM54MYO6Unconventional myosin-VISUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Golgi apparatus {ECO:0000250}. Nucleus. Cytoplasm, perinuclear region. Membrane, clathrin-coated pit. Cell projection, ruffle membrane; Peripheral membrane protein. Note=Also present in endocyctic vesicles, and membrane ruffles. Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles. Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasmic vesicle, clathrin-coated vesicle membrane.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasmic vesicle, clathrin-coated vesicle membrane. Cell projection, ruffle membrane.1actin filament-based movement [GO:0030048]; auditory receptor cell differentiation [GO:0042491]; cellular response to electrical stimulus [GO:0071257]; dendrite development [GO:0016358]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocytosis [GO:0006897]; glutamate secretion [GO:0014047]; inner ear morphogenesis [GO:0042472]; intracellular protein transport [GO:0006886]; locomotory behavior [GO:0007626]; membrane organization [GO:0061024]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein targeting [GO:0006605]; regulation of secretion [GO:0051046]; regulation of synaptic plasticity [GO:0048167]; response to drug [GO:0042493]; sensory perception of sound [GO:0007605]; synapse assembly [GO:0007416]; synaptic transmission [GO:0007268]actin binding [GO:0003779]; actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; minus-end directed microfilament motor activity [GO:0060001]; motor activity [GO:0003774]apical part of cell [GO:0045177]; axon [GO:0030424]; cell cortex [GO:0005938]; clathrin-coated vesicle membrane [GO:0030665]; coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; DNA-directed RNA polymerase II, holoenzyme [GO:0016591]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microvillus [GO:0005902]; neuronal cell body [GO:0043025]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; unconventional myosin complex [GO:0016461]MFUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity). {ECO:0000250}.Q9UKG9OCTC+Peroxisomal carnitine O-octanoyltransferasecarnitine metabolic process [GO:0009437]; cellular lipid metabolic process [GO:0044255]; coenzyme A metabolic process [GO:0015936]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; generation of precursor metabolites and energy [GO:0006091]; medium-chain fatty acid metabolic process [GO:0051791]; small molecule metabolic process [GO:0044281]Tcarnitine O-octanoyltransferase activity [GO:0008458]; receptor binding [GO:0005102]intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. {ECO:0000269|PubMed:10486279}.Q6NZI2PTRF*Polymerase I and transcript release factorSUBCELLULAR LOCATION: Membrane, caveola. Cell membrane {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Microsome {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Endoplasmic reticulum. Cytoplasm, cytosol. Mitochondrion {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Nucleus {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Note=Found at the surface of < the caveolae. Also found in the plasma membrane, microsomal and cytosolic fractions and at a low level in the mitochondrial and nuclear fractions. Translocates to the cytoplasm from the caveolae upon insulin stimulation. CAV1 is necessary to recruit it to the cell membrane (By similarity). Co-localizes with CAV1 in lipid rafts in adipocytes. {ECO:0000250}.gene expression [GO:0010467]; regulation of transcription, DNA-templated [GO:0006355]; termination of RNA polymerase I transcription [GO:0006363]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]Npoly(A) RNA binding [GO:0044822]; rRNA primary transcript binding [GO:0042134]Acaveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex. {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19726876}.P61925IPKA-cAMP-dependent protein kinase inhibitor alpha negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]vcAMP-dependent protein kinase inhibitor activity [GO:0004862]; protein kinase A catalytic subunit binding [GO:0034236]FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.Q96HH9GRAM3 GRAM domain-containing protein 3$cytoplasmic microtubule [GO:0005881]Q96RD7PANX1 Pannexin-1@SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:17715132}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.calcium ion transport [GO:0006816]; cation transport [GO:0006812]; cell-cell signaling [GO:0007267]; innate immune response [GO:0045087]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; positive regulation of interleukin-1 alpha secretion [GO:0050717]; positive regulation of interleukin-1 beta secretion [GO:0050718]; protein hexamerization [GO:0034214]; response to ATP [GO:0033198]; response to ischemia [GO:0002931]; synaptic transmission [GO:0007268]calcium channel activity [GO:0005262]; gap junction hemi-channel activity [GO:0055077]; leak channel activity [GO:0022840]; receptor binding [GO:0005102]bleb [GO:0032059]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; gap junction [GO:0005921]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein complex [GO:0043234]FUNCTION: Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis. {ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:20829356}.Q14692BMS1(Ribosome biogenesis protein BMS1 homologFUNCTION: May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. {ECO:0000250|UniProtKB:Q08965}.P13497BMP1Bone morphogenetic protein 1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12637569}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12637569}. Note=Co-localizes with POSTN in the Golgi. {ECO:0000250}.cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; lipoprotein metabolic process [GO:0042157]; multicellular organismal development [GO:0007275]; ossification [GO:0001503]; positive regulation of cartilage development [GO:0061036]; proteolysis [GO:0006508]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane-bounded vesicle [GO:0031988]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD). Responsible for the proteolytic activation of lysyl oxidase LOX.Q9BVC3DCC1&Sister chromatid cohesion protein DCC1DNA replication [GO:0006260]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; post-translational protein acetylation [GO:0034421]; regulation of DNA replication [GO:0006275]chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; Ctf18 RFC-like complex [GO:0031390]; nucleoplasm [GO:0005654])FUNCTION: Loads PCNA onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion through regulation of the acetylation of the cohesin subunit SMC3. {ECO:0000269|PubMed:12766176, ECO:0000269|PubMed:19907496}.Q13449LSAMP)Limbic system-associated membrane proteinlocomotory exploration behavior [GO:0035641]; nervous system development [GO:0007399]; regulation of neurogenesis [GO:0050767]; single organismal cell-cell adhesion [GO:0016337]FUNCTION: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hyppocampal mossy fiber projection (By similarity). {ECO:0000250}.P08572CO4A2Collagen alpha-2(IV) chainangiogenesis [GO:0001525]; axon guidance [GO:0007411]; cellular response to transforming growth factor beta stimulus [GO:0071560]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; negative regulation of angiogenesis [GO:0016525]; receptor-mediated endocytosis [GO:0006898]; transcription, DNA-templated [GO:0006351]collagen type IV trimer [GO:0005587]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]hFUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; FUNCTION: Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.Q9UPT9UBP22(Ubiquitin carboxyl-terminal hydrolase 22,cell cycle [GO:0007049]; chromatin organization [GO:0006325]; embryo development [GO:0009790]; histone deubiquitination [GO:0016578]; histone H4 acetylation [GO:0043967]; histone ubiquitinatio< n [GO:0016574]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of transcription, DNA-templated [GO:0045893]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]; transcription, DNA-templated [GO:0006351]$cysteine-type endopeptidase activity [GO:0004197]; enzyme binding [GO:0019899]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; transcription coactivator activity [GO:0003713]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]SAGA complex [GO:0000124]FUNCTION: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression. {ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:18206973, ECO:0000269|PubMed:18469533}.Q86VP1TAXB1Tax1-binding protein 1 apoptotic process [GO:0006915]; innate immune response [GO:0045087]; negative regulation of apoptotic process [GO:0043066]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of type I interferon production [GO:0032480];kinase binding [GO:0019900]; metal ion binding [GO:0046872]+FUNCTION: Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. {ECO:0000269|PubMed:10435631, ECO:0000269|PubMed:10920205}.Q16881TRXR1$Thioredoxin reductase 1, cytoplasmicSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.cell proliferation [GO:0008283]; cell redox homeostasis [GO:0045454]; cellular lipid metabolic process [GO:0044255]; gene expression [GO:0010467]; mesoderm formation [GO:0001707]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; response to reactive oxygen species [GO:0000302]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transcription initiation from RNA polymerase II promoter [GO:0006367]electron carrier activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; protein disulfide oxidoreductase activity [GO:0015035]; thioredoxin-disulfide reductase activity [GO:0004791]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]<FUNCTION: Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. {ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704, ECO:0000269|PubMed:9774665}.P49321NASP#Nuclear autoantigenic sperm protein7SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus.blastocyst development [GO:0001824]; cell cycle [GO:0007049]; cell proliferation [GO:0008283]; DNA replication [GO:0006260]; DNA replication-dependent nucleosome assembly [GO:0006335]; DNA replication-independent nucleosome assembly [GO:0006336]; histone exchange [GO:0043486]; male gonad development [GO:0008584]; nucleosome assembly [GO:0006334]; protein transport [GO:0015031]; response to testosterone [GO:0033574]HHsp90 protein binding [GO:0051879]; protein complex binding [GO:0032403]cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]pFUNCTION: Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA (By similarity). {ECO:0000250}.P11802CDK4Cyclin-dependent kinase 4SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus.cell division [GO:0051301]; chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; G1/S transition of mitotic cell cycle [GO:0000082]; lens development in camera-type eye [GO:0002088]; mitotic cell cycle [GO:0000278]; negative regulation of cell cycle arrest [GO:0071157]; organ regeneration [GO:0031100]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cell size [GO:0045793]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of translation [GO:0045727]; protein phosphorylation [GO:0006468]; regulation of gene expression [GO:0010468]; regulation of protein kinase activity [GO:0045859]; response to drug [GO:0042493]; response to hyperoxia [GO:0055093]; response to lead ion [GO:0010288]; response to testosterone [GO:0033574]; response to toxic substance [GO:0009636]; signal transduction [GO:0007165]ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]Ubicellular tight junction [GO:0005923]; chromatin [GO:0000785]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; transcription factor complex [GO:0005667]FUNCTION: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:15241418, ECO:0000269|PubMed:18827403, ECO:0000269|PubMed:9003781}.O602393BP5SH3 domain-binding protein 5BSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12167088}.intracellular signal transduction [GO:0035556]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]; negative regulation of protein tyrosine kinase activity [GO:0061099]; signal transduction [GO:0007165]FUNCTION: Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death. {ECO:0000269|PubMed:10339589, ECO:0000269|PubMed:9571151}.Q5XKK7F219BProtein FAM219BP22692IBP4,Insulin-like growth factor-binding protein 4< Tcell proliferation [GO:0008283]; cellular protein metabolic process [GO:0044267]; DNA metabolic process [GO:0006259]; inflammatory response [GO:0006954]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of MAPK cascade [GO:0043410]; regulation of cell growth [GO:0001558]; regulation of glucose metabolic process [GO:0010906]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; type B pancreatic cell proliferation [GO:0044342]einsulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]P09493TPM1Tropomyosin alpha-1 chainJcardiac muscle contraction [GO:0060048]; cellular response to reactive oxygen species [GO:0034614]; cytoskeleton organization [GO:0007010]; in utero embryonic development [GO:0001701]; movement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; negative regulation of cell migration [GO:0030336]; positive regulation of ATPase activity [GO:0032781]; positive regulation of cell adhesion [GO:0045785]; positive regulation of heart rate by epinephrine [GO:0003065]; positive regulation of stress fiber assembly [GO:0051496]; regulation of heart contraction [GO:0008016]; regulation of muscle contraction [GO:0006937]; ruffle organization [GO:0031529]; sarcomere organization [GO:0045214]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; wound healing [GO:0042060]actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]bleb [GO:0032059]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; filamentous actin [GO:0031941]; muscle thin filament tropomyosin [GO:0005862]; ruffle membrane [GO:0032587]; sarcomere [GO:0030017]; stress fiber [GO:0001725]fFUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.Q9BZF9UACA>Uveal autoantigen with coiled-coil domains and ankyrin repeatsSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15358194}. Cytoplasm {ECO:0000269|PubMed:15358194}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15358194}. Note=Expressed diffusely in cytoplasm.\apoptotic signaling pathway [GO:0097190]; regulation of NIK/NF-kappaB signaling [GO:1901222]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1 (By similarity). {ECO:0000250}.; FUNCTION: Modulates isoactin dynamics to regulate the morphological alterations required for cell growth and motility. Interaction with ARF6 may modulate cell shape and motility after injury. May be involved in multiple neurite formation (By similarity). {ECO:0000250|UniProtKB:Q8CGB3, ECO:0000250|UniProtKB:Q8HYY4}.Q9H0X4ITFG3 Protein ITFG3P23443KS6B1"Ribosomal protein S6 kinase beta-1kinas target S6/eIF4BSUBCELLULAR LOCATION: Cell junction, synapse, synaptosome {ECO:0000250}. Mitochondrion outer membrane. Mitochondrion. Note=Colocalizes with URI1 at mitochondrion.; SUBCELLULAR LOCATION: Isoform Alpha I: Nucleus. Cytoplasm.; SUBCELLULAR LOCATION: Isoform Alpha II: Cytoplasm.aging [GO:0007568]; apoptotic process [GO:0006915]; behavioral fear response [GO:0001662]; cell migration [GO:0016477]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; cellular response to organic cyclic compound [GO:0071407]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell development [GO:0007281]; insulin receptor signaling pathway [GO:0008286]; long-term memory [GO:0007616]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of skeletal muscle tissue growth [GO:0048633]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of translation [GO:0045727]; positive regulation of translational initiation [GO:0045948]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; regulation of glucose import [GO:0046324]; response to drug [GO:0042493]; response to electrical stimulus involved in regulation of muscle adaptation [GO:0014878]; response to ethanol [GO:0045471]; response to glucagon [GO:0033762]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to heat [GO:0009408]; response to leucine [GO:0043201]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; response to nutrient [GO:0007584]; response to testosterone [GO:0033574]; response to toxic substance [GO:0009636]; response to tumor necrosis factor [GO:0034612]; response to wounding [GO:0009611]; signal transduction [GO:0007165]; skeletal muscle atrophy [GO:0014732]; skeletal muscle contraction [GO:0003009]; TOR signaling [GO:0031929]ATP binding [GO:0005524]; peptide binding [GO:0042277]; protein kinase activity [GO:0004672]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; ribosomal protein S6 kinase activity [GO:0004711]>cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; synapse [GO:0045202] FUNCTION: Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative f< eedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR. {ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:14673156, ECO:0000269|PubMed:15071500, ECO:0000269|PubMed:15341740, ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:17052453, ECO:0000269|PubMed:17053147, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:23429703}.Q96D70R3HD4R3H domain-containing protein 4P15289ARSAArylsulfatase Aarylsulfatase activity [GO:0004065]; calcium ion binding [GO:0005509]; cerebroside-sulfatase activity [GO:0004098]; sulfuric ester hydrolase activity [GO:0008484]endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764])FUNCTION: Hydrolyzes cerebroside sulfate.P62875RPAB5:DNA-directed RNA polymerases I, II, and III subunit RPABC5XSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:9852112}.r7-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of type I interferon production [GO:0032481]; positive regulation of viral transcription [GO:0050434]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription from RNA polymerase I promoter [GO:0006356]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; termination of RNA polymerase III transcription [GO:0006386]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase III promoter [GO:0006385]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase III promoter [GO:0006383]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]jFUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2L/RBP10 is part of the core element with the central large cleft (By similarity). {ECO:0000250}.P61586RHOATransforming protein RhoA?SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium {ECO:0000250}. Note=Localized to cell-cell contacts in calcium-treated keratinocytes (By similarity). Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in a activated form and in a myosin- and actin-independent manner. {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; apical junction assembly [GO:0043297]; apolipoprotein A-I-mediated signaling pathway [GO:0038027]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; cleavage furrow formation [GO:0036089]; ephrin receptor signaling pathway [GO:0048013]; mitotic spindle assembly [GO:0090307]; negative chemotaxis [GO:0050919]; negative regulation of axonogenesis [GO:0050771]; neurotrophin TRK receptor signaling pathway [GO:0048011]; ossification involved in bone maturation [GO:0043931]; phosphatidylinositol-mediated signaling [GO:0048015]; platelet activation [GO:0030168]; positive regulation of axonogenesis [GO:0050772]; positive regulation of cytokinesis [GO:0032467]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of lipase activity [GO:0060193]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of NF-kappaB import into nucleus [GO:0042346]; positive regulation of stress fiber assembly [GO:0051496]; regulation of axonogenesis [GO:0050770]; regulation of cell migration [GO:0030334]; regulation of osteoblast proliferation [GO:0033688]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; skeletal muscle satellite cell migration [GO:1902766]; small GTPase mediated signal transduction [GO:0007264]; substantia nigra development [GO:0021762]; trabecula morphogenesis [GO:0061383]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]; wound healing, spreading of cells [GO:0044319]SGTPase activity [GO:0003924]; GTP binding [GO:0005525]; myosin binding [GO:0017022]apical junction complex [GO:0043296]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cleavage furrow [GO:0032154]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; midbody [GO:0030496]; plasma membrane [GO:0005886]; vesicle [GO:0031982]_ FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization o< f microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436,PubMed:19403695). {ECO:0000250, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.Q07889SOS1Son of sevenless homolog 1apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; B cell homeostasis [GO:0001782]; blood coagulation [GO:0007596]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; leukocyte migration [GO:0050900]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of apoptotic process [GO:0043065]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of GTPase activity [GO:0043547]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; Ras protein signal transduction [GO:0007265]; regulation of pro-B cell differentiation [GO:2000973]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of T cell differentiation in thymus [GO:0033081]; regulation of T cell proliferation [GO:0042129]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]DNA binding [GO:0003677]; GTPase activator activity [GO:0005096]; Ras guanyl-nucleotide exchange factor activity [GO:0005088]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]vcytosol [GO:0005829]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity (By similarity). {ECO:0000250}.Q9Y5Q0FADS3Fatty acid desaturase 3O15164TIF1A)Transcription intermediary factor 1-alphaSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480}. Cytoplasm {ECO:0000269|PubMed:21164480}. Note=Colocalizes with sites of active transcription. Detected both in nucleus and cytoplasm in some breast cancer samples. Predominantly nuclear.calcium ion homeostasis [GO:0055074]; cellular response to estrogen stimulus [GO:0071391]; negative regulation of cell proliferation [GO:0008285]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of transcription, DNA-templated [GO:0045893]; protein autophosphorylation [GO:0046777]; protein catabolic process [GO:0030163]; protein ubiquitination [GO:0016567]; regulation of apoptotic process [GO:0042981]; regulation of protein stability [GO:0031647]; regulation of signal transduction by p53 class mediator [GO:1901796]; regulation of vitamin D receptor signaling pathway [GO:0070562]; transcription from RNA polymerase II promoter [GO:0006366]chromatin binding [GO:0003682]; estrogen response element binding [GO:0034056]; ligase activity [GO:0016874]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039]; protein kinase activity [GO:0004672]; receptor binding [GO:0005102]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]cytosol [GO:0005829]; nuclear euchromatin [GO:0005719]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726]mFUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis, at least in part via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, including RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes (By similarity). {ECO:0000250}.Q9P2N5RBM27RNA-binding protein 27SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle. Note=Incorporated into the nuclear speckles and to speckles proximal to the nuclear periphery. Also localizes to punctate structures in the cytoplasm termed cytospeckles (By similarity). {ECO:0000250}.mRNA processing [GO:0006397]Q96HN2SAHH3!Putative adenosylhomocysteinase 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A6QLP2, ECO:0000250|UniProtKB:Q68FL4}. Microsome {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1. {ECO:0000250|UniProtKB:Q68FL4}.Rone-carbon metabolic process [GO:0006730]; S-adenosylmethionine cycle [GO:0033353]8cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783],FUNCTION: May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 acitivity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (PubMed:19220705). {ECO:0000250|UniProtKB:A6QLP2, ECO:0000269|PubMed:19220705}.Q53H96P5CR3#Pyrroline-5-carboxylate reductase 3Q9NY33DPP3Dipeptidyl peptidase 3qdipeptidyl-peptidase activity [GO:0008239]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]rcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Cleaves and degrades of the opioid peptide enkephalin. Also cleaves Arg-Arg-beta-naphthylamide. {ECO:0000269|PubMed:22493238}.Q9Y4Z0LSM4(U6 snRNA-associated Sm-like protein LSm4activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA processing [GO:0006397]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of defense response to virus by host [GO:0002230]; RNA splicing [GO:0008380]cytosol [GO:0005829]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]; U6 snRNP [GO:0005688]Q96QE2MYCT!Proton myo-inositol cotransporterxSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11500374}; Multi-pass membrane protein {ECO:0000269|PubMed:11500374}.glucose import [GO:0046323]; hexose transmembrane transport [GO:0035428]; proton transport [GO:0015992]; transmembrane transport [GO:0055085]sFUNCTION: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers. {ECO:0000269|PubMed:11500374}.A5A3E0POTEF#POTE ankyrin domain family member FrSUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:17101985}. Note=Colocalizes with actin filaments.blood microparticle [GO:0072562]; cell cortex [GO:0005938]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]Q9H254SPTN4'Spectrin beta chain, non-erythrocytic 4bSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.< Cytoplasm, cell cortex {ECO:0000250}.actin filament capping [GO:0051693]; adult walking behavior [GO:0007628]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cardiac conduction [GO:0061337]; central nervous system projection neuron axonogenesis [GO:0021952]; clustering of voltage-gated sodium channels [GO:0045162]; cytoskeletal anchoring at plasma membrane [GO:0007016]; establishment of protein localization to plasma membrane [GO:0090002]; fertilization [GO:0009566]; negative regulation of heart rate [GO:0010459]; positive regulation of multicellular organism growth [GO:0040018]; regulation of peptidyl-serine phosphorylation [GO:0033135]; regulation of sodium ion transport [GO:0002028]; sensory perception of sound [GO:0007605]; transmission of nerve impulse [GO:0019226]; vesicle-mediated transport [GO:0016192]actin binding [GO:0003779]; ankyrin binding [GO:0030506]; phosphatase binding [GO:0019902]; phospholipid binding [GO:0005543]; spectrin binding [GO:0030507]; structural constituent of cytoskeleton [GO:0005200]adherens junction [GO:0005912]; axon hillock [GO:0043203]; axon initial segment [GO:0043194]; cell body fiber [GO:0070852]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; nuclear matrix [GO:0016363]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; PML body [GO:0016605]; spectrin [GO:0008091]Q15413RYR3Ryanodine receptor 3SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic. {ECO:0000250}.calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; cellular response to magnesium ion [GO:0071286]; ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; protein homotetramerization [GO:0051289]; striated muscle contraction [GO:0006941]; transmembrane transport [GO:0055085]calcium-induced calcium release activity [GO:0048763]; calcium ion binding [GO:0005509]; calcium-release channel activity [GO:0015278]; ryanodine-sensitive calcium-release channel activity [GO:0005219]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; junctional membrane complex [GO:0030314]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum membrane [GO:0033017]FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis (By similarity). Plays a role in cellular calcium signaling. {ECO:0000250, ECO:0000269|PubMed:12354756}.Q96D15RCN3Reticulocalbin-3P27487DPP4Dipeptidyl peptidase 4SUBCELLULAR LOCATION: Dipeptidyl peptidase 4 soluble form: Secreted. Note=Detected in the serum and the seminal fluid.; SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell junction. Membrane raft. Note=Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface.behavioral fear response [GO:0001662]; endothelial cell migration [GO:0043542]; locomotory exploration behavior [GO:0035641]; negative regulation of extracellular matrix disassembly [GO:0010716]; positive regulation of cell proliferation [GO:0008284]; psychomotor behavior [GO:0036343]; regulation of cell-cell adhesion mediated by integrin [GO:0033632]; response to hypoxia [GO:0001666]; T cell activation [GO:0042110]; T cell costimulation [GO:0031295]; viral entry into host cell [GO:0046718]Ddipeptidyl-peptidase activity [GO:0008239]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; receptor binding [GO:0005102]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; virus receptor activity [GO:0001618]apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endocytic vesicle [GO:0030139]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intercellular canaliculus [GO:0046581]; invadopodium membrane [GO:0071438]; lamellipodium [GO:0030027]; lamellipodium membrane [GO:0031258]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000269|PubMed:10570924, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.Q9BTV7CABL2 CDK5 and ABL1 enzyme substrate 2Zcell cycle [GO:0007049]; cell division [GO:0051301]; regulation of cell cycle [GO:0051726]CFUNCTION: Unknown. Probably involved in G1-S cell cycle transition.O15379HDAC3Histone deacetylase 3\SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21030595}. Cytoplasm {ECO:0000269|PubMed:25190803}. Cytoplasm, cytosol {ECO:0000269|PubMed:21030595}. Note=Colocalizes with XBP1 and AKT1 in the cytoplasm (PubMed:25190803). Predominantly expressed in the nucleus in the presence of CCAR2. {ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:25190803}.cellular lipid metabolic process [GO:0044255]; cellular response to fluid shear stress [GO:0071498]; chromatin modification [GO:0016568]; chromatin organization [GO:000632< 5]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of cell cycle [GO:0045786]; negative regulation of JNK cascade [GO:0046329]; negative regulation of nucleic acid-templated transcription [GO:1903507]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch signaling pathway [GO:0007219]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of TOR signaling [GO:0032008]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein deacetylation [GO:0006476]; regulation of mitotic cell cycle [GO:0007346]; regulation of multicellular organism growth [GO:0040014]; regulation of protein stability [GO:0031647]; small molecule metabolic process [GO:0044281]; spindle assembly [GO:0051225]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; enzyme binding [GO:0019899]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; NAD-dependent histone deacetylase activity (H3-K14 specific) [GO:0032041]; NF-kappaB binding [GO:0051059]; protein deacetylase activity [GO:0033558]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle microtubule [GO:0005876]; transcriptional repressor complex [GO:0017053]>FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:21444723, PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803). {ECO:0000269|PubMed:21444723, ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:25190803}.P04264K2C1Keratin, type II cytoskeletal 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17956333}. Note=Located on plasma membrane of neuroblastoma NMB7 cells.)complement activation, lectin pathway [GO:0001867]; establishment of skin barrier [GO:0061436]; fibrinolysis [GO:0042730]; negative regulation of inflammatory response [GO:0050728]; regulation of angiogenesis [GO:0045765]; response to oxidative stress [GO:0006979]; retina homeostasis [GO:0001895]lcarbohydrate binding [GO:0030246]; receptor activity [GO:0004872]; structural molecule activity [GO:0005198]blood microparticle [GO:0072562]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]+FUNCTION: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein kinase C (RACK1/GNB2L1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK. {ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21544310}.Q8WXI7MUC16Mucin-16,SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Secreted, extracellular space. Note=May be liberated into the extracellular space following the phosphorylation of the intracellular C-terminus which induces the proteolytic cleavage and liberation of the extracellular domain.cell adhesion [GO:0007155]; cellular protein metabolic process [GO:0044267]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; extrinsic component of membrane [GO:0019898]; Golgi lumen [GO:0005796]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; vesicle [GO:0031982]FUNCTION: Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. {ECO:0000250}.Q92503S14L1SEC14-like protein 1P54284CACB37Voltage-dependent L-type calcium channel subunit beta-3Daxon guidance [GO:0007411]; calcium ion transport [GO:0006816]; membrane depolarization [GO:0051899]; neuromuscular junction development [GO:0007528]; regulation of voltage-gated calcium channel activity [GO:1901385]; synaptic transmission [GO:0007268]; T cell receptor signaling pathway [GO:0050852]; transport [GO:0006810]mhigh voltage-gated calcium channel activity [GO:0008331]; voltage-gated calcium channel activity [GO:0005245]apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; membrane [GO:0016020]; voltage-gated calcium channel complex [GO:0005891]1FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.Q9NZ43USE1Vesicle transport protein USE1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15029241}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15029241}.5endoplasmic reticulum tubular network organization [GO:0071786]; lysosomal transport [GO:0007041]; protein catabolic process [GO:0030163]; protein transport [GO:0015031]; regulation of ER to Golgi vesicle-mediated transport [GO:0060628]; secretion by cell [GO:0032940]; vesicle-mediated transport [GO:0016192]FUNCTION: SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. {ECO:0000269|PubMed:15272311}.Q5TAT6CODA1Collagen alpha-1(XIII) chainSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11013208}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9R1N9, ECO:0000269|PubMed:11013208}.\cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; collagen catabolic process [GO:0030574]; endochondral ossification [GO:0001958]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; morphogenesis of a branching structure [GO:0001763]; single organismal cell-cell adhesion [GO:0016337]cell-cell junction [GO:0005911]; collagen type XIII trimer [GO:0005600]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]}FUNCTION: Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. {ECO:0000250|UniProtKB:Q9R1N9, ECO:0000< 269|PubMed:10865988, ECO:0000269|PubMed:11956183}.Q9H7E9CH033UPF0488 protein C8orf33Q12872SFSWA4Splicing factor, suppressor of white-apricot homologmRNA processing [GO:0006397]; mRNA splice site selection [GO:0006376]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]SFUNCTION: Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:8940107}.Q9UEU0VTI1B>Vesicle transport through interaction with t-SNAREs homolog 1BSUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:23217709}; Single-pass type IV membrane protein {ECO:0000269|PubMed:23217709}. Lysosome membrane {ECO:0000269|PubMed:23217709}. Cytoplasmic granule {ECO:0000269|PubMed:23217709}.cell proliferation [GO:0008283]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi to vacuole transport [GO:0006896]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane fusion [GO:0061025]; protein targeting to vacuole [GO:0006623]; regulation of protein localization to plasma membrane [GO:1903076]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle docking involved in exocytosis [GO:0006904]; vesicle fusion with Golgi apparatus [GO:0048280]; vesicle-mediated transport [GO:0016192]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; vesicle [GO:0031982][FUNCTION: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence.P31321KAP1<cAMP-dependent protein kinase type I-beta regulatory subunitKactivation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; blood coagulation [GO:0007596]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; learning or memory [GO:0007611]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; neurotrophin TRK receptor signaling pathway [GO:0048011]; protein phosphorylation [GO:0006468]; regulation of insulin secretion [GO:0050796]; renal water homeostasis [GO:0003091]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; water transport [GO:0006833]cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236]cAMP-dependent protein kinase complex [GO:0005952]; ciliary base [GO:0097546]; cytosol [GO:0005829]; plasma membrane [GO:0005886]FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:20819953}.P08727K1C19Keratin, type I cytoskeletal 19cell differentiation involved in embryonic placenta development [GO:0060706]; response to estrogen [GO:0043627]; sarcomere organization [GO:0045214]; viral process [GO:0016032]bstructural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]cell periphery [GO:0071944]; costamere [GO:0043034]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; terminal web [GO:1990357]; Z disc [GO:0030018]FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}.Q13018PLA2R#Secretory phospholipase A2 receptorSUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: Soluble secretory phospholipase A2 receptor: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}."cytokine production [GO:0001816]; endocytosis [GO:0006897]; negative regulation of arachidonic acid secretion [GO:1900139]; negative regulation of phospholipase A2 activity [GO:1900138]; oxidative stress-induced premature senescence [GO:0090403]; positive regulation of arachidonic acid secretion [GO:0090238]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; reactive oxygen species metabolic process [GO:0072593]; receptor-mediated endocytosis [GO:0006898]; replicative senescence [GO:0090399]ecarbohydrate binding [GO:0030246]; phospholipase binding [GO:0043274]; receptor activity [GO:0004872]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] FUNCTION: Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phosholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B. {ECO:0000269|PubMed:15611272, ECO:0000269|PubMed:7721806}.P55145MANF3Mesencephalic astrocyte-derived neurotrophic factorZSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12794311, ECO:0000269|PubMed:18561914}.)response to unfolded protein [GO:0006986]FUNCTION: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons (By similarity). Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. {ECO:0000250, ECO:0000269|PubMed:12794311, ECO:0000269|PubMed:18561914}.P23284PPIB%Peptidyl-prolyl cis-trans isomerase Bbone development [GO:0060348]; chaperone-mediated protein folding [GO:0061077]; extracellular matrix organization [GO:0030198]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation by host of viral process [GO:0044794]; positive regulation of multicellular o< rganism growth [GO:0040018]; protein peptidyl-prolyl isomerization [GO:0000413]; protein stabilization [GO:0050821]peptide binding [GO:0042277]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]; protein complex binding [GO:0032403]; RNA polymerase binding [GO:0070063]; unfolded protein binding [GO:0051082]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; macromolecular complex [GO:0032991]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; smooth endoplasmic reticulum [GO:0005790]Q05193DYN1 Dynamin-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15703209}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15703209}. Note=Microtubule-associated.adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; endocytosis [GO:0006897]; endosome organization [GO:0007032]; ephrin receptor signaling pathway [GO:0048013]; protein tetramerization [GO:0051262]; receptor-mediated endocytosis [GO:0006898]; sensory perception of sound [GO:0007605]; synaptic transmission, GABAergic [GO:0051932]; toxin transport [GO:1901998]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]extracellular exosome [GO:0070062]; membrane coat [GO:0030117]; microtubule [GO:0005874]; myelin sheath [GO:0043209]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886]FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.P54802ANAGAlpha-N-acetylglucosaminidasecarbohydrate metabolic process [GO:0005975]; cerebellar Purkinje cell layer development [GO:0021680]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; inner ear receptor cell development [GO:0060119]; locomotor rhythm [GO:0045475]; lysosome organization [GO:0007040]; middle ear morphogenesis [GO:0042474]; nervous system development [GO:0007399]; retinal rod cell development [GO:0046548]; small molecule metabolic process [GO:0044281]3alpha-N-acetylglucosaminidase activity [GO:0004561]Wextracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]9FUNCTION: Involved in the degradation of heparan sulfate.Q99536VAT1/Synaptic vesicle membrane protein VAT-1 homologSUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein. Note=The majority is localized in the cytoplasm and a small amount is associated with mitochondria. {ECO:0000250}.8negative regulation of mitochondrial fusion [GO:0010637]zextracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]tFUNCTION: Possesses ATPase activity (By similarity). Plays a part in calcium-regulated keratinocyte activation in epidermal repair mechanisms. Has no effect on cell proliferation. Negatively regulates mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2). {ECO:0000250, ECO:0000269|PubMed:12898150, ECO:0000269|PubMed:17105775, ECO:0000269|PubMed:19508442}.P02452CO1A1Collagen alpha-1(I) chainvblood coagulation [GO:0007596]; blood vessel development [GO:0001568]; bone trabecula formation [GO:0060346]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to amino acid stimulus [GO:0071230]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to fluoride [GO:1902618]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin E [GO:0071306]; collagen biosynthetic process [GO:0032964]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; embryonic skeletal system development [GO:0048706]; endochondral ossification [GO:0001958]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; intramembranous ossification [GO:0001957]; leukocyte migration [GO:0050900]; negative regulation of cell-substrate adhesion [GO:0010812]; osteoblast differentiation [GO:0001649]; platelet activation [GO:0030168]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of transcription, DNA-templated [GO:0045893]; protein heterotrimerization [GO:0070208]; protein localization to nucleus [GO:0034504]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; response to cAMP [GO:0051591]; response to corticosteroid [GO:0031960]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to peptide hormone [GO:0043434]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; skin morphogenesis [GO:0043589]; tooth eruption [GO:0044691]; tooth mineralization [GO:0034505]; visual perception [GO:0007601]extracellular matrix structural constituent [GO:0005201]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]collagen type I trimer [GO:0005584]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; secretory granule [GO:0030141]P02458CO2A1Collagen alpha-1(II) chainqaxon guidance [GO:0007411]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to BMP stimulus [GO:0071773]; central nervous system development [GO:0007417]; chondrocyte differentiation [GO:0002062]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; embryonic skeletal joint morphogenesis [GO:0060272]; endochondral ossification [GO:0001958]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; heart morphogenesis [GO:0003007]; inner ear morphogenesis [GO:0042472]; limb bud formation [GO:0060174]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; notochord development [GO:0030903]; otic vesicle development [GO:0071599]; palate development [GO:0060021]; proteoglycan metabolic process [GO:0006029]; regulation of gene expression [GO:0010468]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; tissue homeostasis [GO:0001894]; visual perception [GO:0007601]extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]basement membrane [GO:0005604]; collagen type II trimer [GO:0005585]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.O75340PDCD6Programmed cell death protein 6SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Endosome. Note=Interaction wit< h RBM22 induces relocalization from the cytoplasm to the nucleus. Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules.zactivation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; angiogenesis [GO:0001525]; apoptotic signaling pathway [GO:0097190]; cellular response to heat [GO:0034605]; intracellular protein transport [GO:0006886]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; proteolysis [GO:0006508]; response to calcium ion [GO:0051592]; vascular endothelial growth factor receptor-2 signaling pathway [GO:0036324]&binding, bridging [GO:0060090]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; calcium-dependent protein binding [GO:0048306]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; protein anchor [GO:0043495]; protein dimerization activity [GO:0046983]'cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]FUNCTION: Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca(2+)-regulated signals along the death pathway (By similarity). Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 has a lower Ca(2+) affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5. {ECO:0000250, ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:17889823, ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:21893193}.Q9H4P4RNF41!E3 ubiquitin-protein ligase NRDP1=autophagy [GO:0006914]; extrinsic apoptotic signaling pathway [GO:0097191]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; proteasomal protein catabolic process [GO:0010498]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; regulation of establishment of cell polarity [GO:2000114]; regulation of lymphocyte differentiation [GO:0045619]; regulation of MAPK cascade [GO:0043408]; regulation of myeloid cell differentiation [GO:0045637]; regulation of protein kinase B signaling [GO:0051896]; regulation of reactive oxygen species metabolic process [GO:2000377]acid-amino acid ligase activity [GO:0016881]; protein tag [GO:0031386]; Ral GTPase binding [GO:0017160]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PARK2 modifier that accelerates its degradation, resulting in a reduction of PARK2 activity, influencing the balance of intracellular redox state. The RNF41-PARK2 pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control (PubMed:24949970). {ECO:0000250, ECO:0000250|UniProtKB:Q8BH75, ECO:0000269|PubMed:12411582, ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15632191, ECO:0000269|PubMed:17210635, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:19483718, ECO:0000269|PubMed:24949970}.O43657TSN6 Tetraspanin-6negative regulation of NIK/NF-kappaB signaling [GO:1901223]; negative regulation of viral-induced cytoplasmic pattern recognition receptor signaling pathway [GO:0039532]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; signal transduction [GO:0007165]Q9UMF0ICAM5!Intercellular adhesion molecule 5hcell adhesion [GO:0007155]; phagocytosis [GO:0006909]; single organismal cell-cell adhesion [GO:0016337]gFUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).P10909CLUS ClusterinSUBCELLULAR LOCATION: Isoform 1: Secreted. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress.; SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250}. Note=Isoforms lacking the N-terminal signal sequence have been shown to be cytoplasmic and/or nuclear. Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis.blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; central nervous system myelin maintenance [GO:0032286]; chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; lipid metabolic process [GO:0006629]; microglial cell activation [GO:0001774]; microglial cell proliferation [GO:0061518]; negative regulation of beta-amyloid formation [GO:1902430]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of protein homooligomerization [GO:0032463]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of apoptotic process [GO:0043065]; positive regulation of beta-amyloid formation [GO:1902004]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of neurofibrillary tangle assembly [GO:1902998]; positive regulation of neuron death [GO:1901216]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; positive regulation of tau-protein kinase activity [GO:1902949]; positive < regulation of tumor necrosis factor production [GO:0032760]; protein import [GO:0017038]; protein stabilization [GO:0050821]; regulation of beta-amyloid clearance [GO:1900221]; regulation of neuronal signal transduction [GO:1902847]; regulation of neuron death [GO:1901214]; release of cytochrome c from mitochondria [GO:0001836]; response to misfolded protein [GO:0051788]; response to virus [GO:0009615]; reverse cholesterol transport [GO:0043691]uchaperone binding [GO:0051087]; misfolded protein binding [GO:0051787]; ubiquitin protein ligase binding [GO:0031625]apical dendrite [GO:0097440]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; chromaffin granule [GO:0042583]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; intracellular [GO:0005622]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; neurofibrillary tangle [GO:0097418]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; platelet alpha granule lumen [GO:0031093]; protein complex [GO:0043234]; spherical high-density lipoprotein particle [GO:0034366]zFUNCTION: Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. {ECO:0000269|PubMed:11123922, ECO:0000269|PubMed:12047389, ECO:0000269|PubMed:12176985, ECO:0000269|PubMed:12551933, ECO:0000269|PubMed:12882985, ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:17260971, ECO:0000269|PubMed:17407782, ECO:0000269|PubMed:17412999, ECO:0000269|PubMed:17689225, ECO:0000269|PubMed:19137541, ECO:0000269|PubMed:19535339, ECO:0000269|PubMed:19996109, ECO:0000269|PubMed:20068069, ECO:0000269|PubMed:21505792}.Q8TEY7UBP33(Ubiquitin carboxyl-terminal hydrolase 33SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase.; SUBCELLULAR LOCATION: Isoform 3: Golgi apparatus.axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular response to starvation [GO:0009267]; centrosome duplication [GO:0051298]; endocytosis [GO:0006897]; negative regulation of protein binding [GO:0032091]; positive regulation of protein binding [GO:0032092]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; regulation of autophagy [GO:0010506]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; regulation of proteasomal protein catabolic process [GO:0061136]; ubiquitin-dependent protein catabolic process [GO:0006511]cysteine-type endopeptidase activity [GO:0004197]; G-protein coupled receptor binding [GO:0001664]; Ral GTPase binding [GO:0017160]; ubiquitin-specific protease activity [GO:0004843]; zinc ion binding [GO:0008270]centrosome [GO:0005813]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intermediate filament cytoskeleton [GO:0045111]; perinuclear region of cytoplasm [GO:0048471]; VCB complex [GO:0030891]FUNCTION: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:19363159, ECO:0000269|PubMed:19424180, ECO:0000269|PubMed:23486064}.P37275ZEB1$Zinc finger E-box-binding homeobox 1Upregulated in cancerYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:25190660}.cartilage development [GO:0051216]; cell proliferation [GO:0008283]; cellular response to amino acid stimulus [GO:0071230]; central nervous system development [GO:0007417]; cochlea morphogenesis [GO:0090103]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic skeletal system morphogenesis [GO:0048704]; immune response [GO:0006955]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; pattern specification process [GO:0007389]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of mesenchymal cell proliferation [GO:0010464]; regulation of smooth muscle cell differentiation [GO:0051150]; regulation of T cell differentiation in thymus [GO:0033081]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; semicircular canal morphogenesis [GO:0048752]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; E-box binding [GO:0070888]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]FUNCTION: Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the p< resence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs. {ECO:0000269|PubMed:19935649, ECO:0000269|PubMed:20175752, ECO:0000269|PubMed:20418909}.P20701ITALIntegrin alpha-LSactivated T cell proliferation [GO:0050798]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; extracellular matrix organization [GO:0030198]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; movement of cell or subcellular component [GO:0006928]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of T cell proliferation [GO:0042102]; receptor clustering [GO:0043113]; regulation of immune response [GO:0050776]; signal transduction [GO:0007165]; T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:0002291]rcell adhesion molecule binding [GO:0050839]; ICAM-3 receptor activity [GO:0030369]; metal ion binding [GO:0046872]1cell-cell junction [GO:0005911]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; integrin alphaL-beta2 complex [GO:0034687]; integrin complex [GO:0008305]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.O60684IMA7Importin subunit alpha-7maternal process involved in female pregnancy [GO:0060135]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]fFUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:10523667}.Q8N6Y2LRC17)Leucine-rich repeat-containing protein 17bone marrow development [GO:0048539]; negative regulation of osteoclast differentiation [GO:0045671]; ossification [GO:0001503]FUNCTION: Involved in bone homeostasis. Acts as a negative regulator of RANKL-induced osteoclast precursor differentiation from bone marrow precursors (By similarity). {ECO:0000250}.Q9HAU4SMUF2"E3 ubiquitin-protein ligase SMURF20SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12717440}. Cytoplasm {ECO:0000269|PubMed:12717440}. Cell membrane {ECO:0000269|PubMed:12717440}. Membrane raft {ECO:0000269|PubMed:12717440}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.BMP signaling pathway [GO:0030509]; gene expression [GO:0010467]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of trophoblast cell migration [GO:1901165]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent SMAD protein catabolic process [GO:0030579]identical protein binding [GO:0042802]; ligase activity [GO:0016874]; SMAD binding [GO:0046332]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level. {ECO:0000269|PubMed:11389444, ECO:0000269|PubMed:12717440}.P06865HEXA!Beta-hexosaminidase subunit alpha carbohydrate metabolic process [GO:0005975]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan metabolic process [GO:0030203]; glycosphingolipid metabolic process [GO:0006687]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]cbeta-N-acetylhexosaminidase activity [GO:0004563]; protein heterodimerization activity [GO:0046982]Wextracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. The form B is active against certain oligosaccharides. The form S has no measurable activity.Q9UNP9PPIE%Peptidyl-prolyl cis-trans isomerase EmRNA splicing, via spliceosome [GO:0000398]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; regulation of transcription, DNA-templated [GO:0006355]cyclosporin A binding [GO:0016018]; nucleotide binding [GO:0000166]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.Q9UHJ6SHPKSedoheptulokinasecarbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; cellular response to interleukin-13 [GO:0035963]; cellular response to interleukin-4 [GO:0071353]; cellular response to lipopolysaccharide [GO:0071222]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]; phosphorylation [GO:0016< 310]; regulation of inflammatory response [GO:0050727]; regulation of macrophage activation [GO:0043030]AATP binding [GO:0005524]; sedoheptulokinase activity [GO:0050277]lFUNCTION: Acts as a modulator of macrophage activation through control of glucose metabolism. {ECO:0000250}.Q9H4B6SAV1Protein salvador homolog 1eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19212654}. Cytoplasm {ECO:0000269|PubMed:19212654}.hair follicle development [GO:0001942]; hippo signaling [GO:0035329]; intestinal epithelial cell differentiation [GO:0060575]; keratinocyte differentiation [GO:0030216]; lung epithelial cell differentiation [GO:0060487]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of epithelial cell proliferation [GO:0050680]; positive regulation of apoptotic process [GO:0043065]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; protein stabilization [GO:0050821]; regulation of stem cell maintenance [GO:2000036]; ventricular septum morphogenesis [GO:0060412]FUNCTION: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. {ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:19212654, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:21104395}.P35637FUSRNA-binding protein FUSYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19251627, ECO:0000269|PubMed:19251628}.cellular response to calcium ion [GO:0071277]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; regulation of nucleic acid-templated transcription [GO:1903506]; RNA splicing [GO:0008380]DNA binding [GO:0003677]; identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]dendritic spine head [GO:0044327]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]FUNCTION: Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.Q8WY36BBX HMG box transcription factor BBXbone development [GO:0060348]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]~FUNCTION: Transcription factor that is necessary for cell cycle progression from G1 to S phase. {ECO:0000269|PubMed:11680820}.O75164KDM4ALysine-specific demethylase 4ASUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16024779}.:cardiac muscle hypertrophy in response to stress [GO:0014898]; chromatin organization [GO:0006325]; histone demethylation [GO:0016577]; histone H3-K36 demethylation [GO:0070544]; negative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]histone demethylase activity (H3-K36 specific) [GO:0051864]; methylated histone binding [GO:0035064]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.; FUNCTION: Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.P43235CATK Cathepsin Kbone resorption [GO:0045453]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; intramembranous ossification [GO:0001957]; positive regulation of protein targeting to mitochondrion [GO:1903955]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of mitochondrion degradation [GO:1903146]; toll-like receptor signaling pathway [GO:0002224]collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; fibronectin binding [GO:0001968]; proteoglycan binding [GO:0043394]{endolysosome lumen [GO:0036021]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]FUNCTION: Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.Q75N03HAKAI!E3 ubiquitin-protein ligase Hakainegative regulation of cell adhesion [GO:0007162]; positive regulation of cell migration [GO:0030335]; positive regulation of endocytosis [GO:0045807]; protein ubiquitination [GO:0016567]; regulation of cell adhesion [GO:0030155]; single organismal cell-cell adhesion [GO:0016337]%ubiquitin ligase complex [GO:0000151]FUNCTION: Promotes ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1. Targets CDH1 for endocytosis and degradation (By similarity). {ECO:0000250}.Q7LC44ARC2Activity-regulated cytoskeleton-associated proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:Q63053, ECO:0000250|UniProtKB:Q9WV31}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q63053, ECO:0000250|UniProtKB:Q9WV31}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Note=Associated with the cell cortex of neuronal soma and dendrites. Enriched in postsynaptic density of dendritic spines. Associated with the sperm tail (By similarity). Enriched on the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:21834987}.anterior/posterior pattern specification [GO:0009952]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; endoderm development [GO:0007492]; learning [GO:0007612]; positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity [GO:2000969]; regulation of cell morphogenesis [GO:0022604]; regulation of neuronal synaptic plasticity [GO:0048168] acrosomal vesicle [GO:0001669]; actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; end< osome [GO:0005768]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]FUNCTION: Required for consolidation of synaptic plasticity as well as formation of long-term memory. Regulates endocytosis of AMPA receptors in response to synaptic activity. Required for homeostatic synaptic scaling of AMPA receptors (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. {ECO:0000250, ECO:0000269|PubMed:21834987}.P54821PRRX1"Paired mesoderm homeobox protein 1~artery morphogenesis [GO:0048844]; cartilage development [GO:0051216]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic limb morphogenesis [GO:0030326]; inner ear morphogenesis [GO:0042472]; middle ear morphogenesis [GO:0042474]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuronal stem cell maintenance [GO:0097150]; neuron fate determination [GO:0048664]; palate development [GO:0060021]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of smoothened signaling pathway [GO:0045880]; regulation of neuron projection regeneration [GO:0070570]RNA polymerase II transcription coactivator activity [GO:0001105]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]FUNCTION: Acts as a transcriptional regulator of muscle creatine kinase (MCK) and so has a role in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer (By similarity). {ECO:0000250}.Q9NZ08ERAP1&Endoplasmic reticulum aminopeptidase 1SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15908954}; Single-pass type II membrane protein {ECO:0000305|PubMed:15908954}.angiogenesis [GO:0001525]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; fat cell differentiation [GO:0045444]; membrane protein ectodomain proteolysis [GO:0006509]; peptide catabolic process [GO:0043171]; positive regulation of angiogenesis [GO:0045766]; regulation of blood pressure [GO:0008217]; regulation of innate immune response [GO:0045088]; response to bacterium [GO:0009617]aminopeptidase activity [GO:0004177]; interleukin-1, Type II receptor binding [GO:0005151]; interleukin-6 receptor binding [GO:0005138]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270]<cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; membrane [GO:0016020]LFUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653, ECO:0000269|PubMed:21478864}.Q15311RBP1RalA-binding protein 1xSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11437348}; Peripheral membrane protein {ECO:0000269|PubMed:11437348}.pchemotaxis [GO:0006935]; endocytosis [GO:0006897]; positive regulation of GTPase activity [GO:0043547]; regulation of GTPase activity [GO:0043087]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]; transmembrane transport [GO:0055085]; transport [GO:0006810]ATPase activity [GO:0016887]; ATPase activity, coupled to movement of substances [GO:0043492]; GTPase activator activity [GO:0005096]; Rac GTPase binding [GO:0048365]; Ral GTPase binding [GO:0017160]; transmembrane transporter activity [GO:0022857]FUNCTION: Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. {ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:7673236}.Q14694UBP10(Ubiquitin carboxyl-terminal hydrolase 10SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Early endosome. Note=Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM.autophagy [GO:0006914]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA repair [GO:0006281]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of autophagy [GO:0010506]; regulation of proteasomal protein catabolic process [GO:0061136]; translesion synthesis [GO:0019985]cysteine-type endopeptidase activity [GO:0004197]; ion channel binding [GO:0044325]; p53 binding [GO:0002039]; poly(A) RNA binding [GO:0044822]; ubiquitin-specific protease activity [GO:0004843]ccytoplasm [GO:0005737]; early endosome [GO:0005769]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]_FUNCTION: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. {ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:21962518}.Q96JP5ZFP91!E3 ubiquitin-protein ligase ZFP91<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12738986}.mactivation of NF-kappaB-inducing kinase activity [GO:0007250]; protein K63-linked ubiquitination [GO:0070534]ligase activity [GO:0016874]; metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; ubiquitin-protein transferase activity [GO:0004842]sFUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF-kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis. {ECO:0000269|PubMed:12738986, ECO:0000269|PubMed:20682767}.Q9HD26GOPC=Golgi-associated PDZ and coiled-coi< l motif-containing protein<SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Cell junction, synapse {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides. {ECO:0000250}.wapical protein localization [GO:0045176]; cytoplasmic sequestering of CFTR protein [GO:0043004]; ER to Golgi vesicle-mediated transport [GO:0006888]; Golgi to plasma membrane transport [GO:0006893]; protein homooligomerization [GO:0051260]; protein transport [GO:0015031]; small GTPase mediated signal transduction [GO:0007264]; spermatid nucleus differentiation [GO:0007289]HGTPase regulator activity [GO:0030695]; ion channel binding [GO:0044325]cell junction [GO:0030054]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle membrane [GO:0030660]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; protein complex [GO:0043234]; trans-Golgi network transport vesicle [GO:0030140]FUNCTION: Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes. {ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:14570915, ECO:0000269|PubMed:15358775}.Q7Z2K8GRIN12G protein-regulated inducer of neurite outgrowth 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Highly enriched in growth cone. {ECO:0000250}.6growth cone [GO:0030426]; plasma membrane [GO:0005886]>FUNCTION: May be involved in neurite outgrowth. {ECO:0000250}.P37840SYUAAlpha-synucleinzSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023}. Membrane {ECO:0000269|PubMed:24936070}. Nucleus {ECO:0000269|PubMed:12859192, ECO:0000269|PubMed:24936070}. Cell junction, synapse {ECO:0000269|PubMed:15282274}. Secreted {ECO:0000269|PubMed:24936070}. Note=Membrane-bound in dopaminergic neurons. {ECO:0000269|PubMed:15282274}.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; adult locomotory behavior [GO:0008344]; aging [GO:0007568]; behavioral response to cocaine [GO:0048148]; cellular response to copper ion [GO:0071280]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to oxidative stress [GO:0034599]; dopamine biosynthetic process [GO:0042416]; dopamine uptake involved in synaptic transmission [GO:0051583]; extracellular fibril organization [GO:0043206]; fatty acid metabolic process [GO:0006631]; long-term synaptic potentiation [GO:0060291]; microglial cell activation [GO:0001774]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; mitochondrial membrane organization [GO:0007006]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of dopamine metabolic process [GO:0045963]; negative regulation of dopamine uptake involved in synaptic transmission [GO:0051585]; negative regulation of exocytosis [GO:0045920]; negative regulation of histone acetylation [GO:0035067]; negative regulation of microtubule polymerization [GO:0031115]; negative regulation of mitochondrial electron transport, NADH to ubiquinone [GO:1902957]; negative regulation of monooxygenase activity [GO:0032769]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of norepinephrine uptake [GO:0051622]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of serotonin uptake [GO:0051612]; negative regulation of thrombin receptor signaling pathway [GO:0070495]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transporter activity [GO:0032410]; neutral lipid metabolic process [GO:0006638]; oxidation-reduction process [GO:0055114]; phospholipid metabolic process [GO:0006644]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endocytosis [GO:0045807]; positive regulation of glutathione peroxidase activity [GO:1903284]; positive regulation of hydrogen peroxide catabolic process [GO:1903285]; positive regulation of inositol phosphate biosynthetic process [GO:0060732]; positive regulation of neurotransmitter secretion [GO:0001956]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; positive regulation of receptor recycling [GO:0001921]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; protein destabilization [GO:0031648]; receptor internalization [GO:0031623]; regulation of acyl-CoA biosynthetic process [GO:0050812]; regulation of dopamine secretion [GO:0014059]; regulation of excitatory postsynaptic membrane potential [GO:0060079]; regulation of glutamate secretion [GO:0014048]; regulation of locomotion [GO:0040012]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of macrophage activation [GO:0043030]; regulation of phospholipase activity [GO:0010517]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; regulation of synaptic vesicle recycling [GO:1903421]; response to drug [GO:0042493]; response to interferon-gamma [GO:0034341]; response to interleukin-1 [GO:0070555]; response to iron(II) ion [GO:0010040]; response to lipopolysaccharide [GO:0032496]; response to magnesium ion [GO:0032026]; synapse organization [GO:0050808]; synaptic vesicle endocytosis [GO:0048488]alpha-tubulin binding [GO:0043014]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; dynein binding [GO:0045502]; ferrous iron binding [GO:0008198]; histone binding [GO:0042393]; Hsp70 protein binding [GO:0030544]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491]; phospholipid binding [GO:0005543]; phosphoprotein binding [GO:0051219]; tau protein binding [GO:0048156]; transcription regulatory region DNA binding [GO:0044212]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; axon [GO:0030424]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibril [GO:0043205]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; inclusion body [GO:0016234]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear outer membrane [GO:0005640]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ribosome [GO:0005840]; rough endoplasmic reticulum [GO:0005791]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]FUNCTION: May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.P27448MARK3,MAP/microtubule affinity-regulating kinase 3}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2114< 5462}; Peripheral membrane protein {ECO:0000269|PubMed:21145462}.@extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]oFUNCTION: Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C on 'Ser-216'. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. {ECO:0000269|PubMed:16980613}.Q9GZV5WWTR16WW domain-containing transcription regulator protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Concentrates along specific portions of the plasma membrane, and accumulates in punctate nuclear bodies. When phosphorylated, is retained in cytoplasm by YWHAZ. Can be retained in the nucleus by MED15.cilium morphogenesis [GO:0060271]; gene expression [GO:0010467]; glomerulus development [GO:0032835]; hippo signaling [GO:0035329]; kidney morphogenesis [GO:0060993]; mesenchymal cell differentiation [GO:0048762]; multicellular organism growth [GO:0035264]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of catenin import into nucleus [GO:0035414]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; osteoblast differentiation [GO:0001649]; positive regulation of cell proliferation [GO:0008284]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein ubiquitination [GO:0016567]; regulation of metanephric nephron tubule epithelial cell differentiation [GO:0072307]; regulation of SMAD protein import into nucleus [GO:0060390]; regulation of transcription, DNA-templated [GO:0006355]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; stem cell division [GO:0017145]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]`transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation. Regulates the nuclear accumulation of SMADS and has a key role in coupling them to the transcriptional machinery such as the mediator complex. Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition. {ECO:0000269|PubMed:11118213, ECO:0000269|PubMed:18227151, ECO:0000269|PubMed:18568018, ECO:0000269|PubMed:19010321}.Q6UXH8CCBE1<Collagen and calcium-binding EGF domain-containing protein 1lymphangiogenesis [GO:0001946]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of lymphangiogenesis [GO:1901492]; positive regulation of protein processing [GO:0010954]; positive regulation of vascular endothelial growth factor production [GO:0010575]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; sprouting angiogenesis [GO:0002040]; venous blood vessel morphogenesis [GO:0048845]^calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; protease binding [GO:0002020]ocollagen trimer [GO:0005581]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. {ECO:0000269|PubMed:19935664}.Q9NVM1EVA1BProtein eva-1 homolog BQ9BUR4WAP53Telomerase Cajal body protein 15SUBCELLULAR LOCATION: Nucleus, Cajal body. Cytoplasm.gpositive regulation of telomerase activity [GO:0051973]; telomere formation via telomerase [GO:0032203]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]FUNCTION: Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes. In the telomerase holoenzyme complex, it controls telomerase localization to Cajal body. Required for delivery of TERC to telomeres during S phase and for telomerase activity. Binds small Cajal body RNAs (scaRNAs). The mRNA encoding this protein plays a critical role in the regulation of p53 expression at the post-transcriptional level; it is involved both in maintaining basal p53 mRNA levels and in p53 induction upon DNA damage. {ECO:0000269|PubMed:19179534, ECO:0000269|PubMed:19250907}.Q15389ANGP1Angiopoietin-1activation of transmembrane receptor protein tyrosine kinase activity [GO:0007171]; blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cell-substrate adhesion [GO:0031589]; glomerulus vasculature development [GO:0072012]; hemopoiesis [GO:0030097]; heparin biosynthetic process [GO:0030210]; in utero embryonic development [GO:0001701]; leukocyte migration [GO:0050900]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cytokine secretion involved in immune response [GO:0002740]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of vascular permeability [GO:0043116]; positive chemotaxis [GO:0050918]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell adhesion [GO:0045785]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of receptor internalization [GO:0002092]; protein localization to cell surface [GO:0034394]; regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043122]; regulation of macrophage migration inhibitory factor signaling pathway [GO:2000446]; regulation of protein binding [GO:0043393]; regulation of satellite cell proliferation [GO:0014842]; regulation of tumor necrosis factor production [GO:0032680]; sprouting angiogenesis [GO:0002040]; Tie signaling pathway [GO:0048014]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; microvillus [GO:0005902]; plasma membrane [GO:0005886] FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or< inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. {ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:9204896}.Q15274NADC7Nicotinate-nucleotide pyrophosphorylase [carboxylating](NAD biosynthetic process [GO:0009435]; NAD metabolic process [GO:0019674]; protein oligomerization [GO:0051259]; quinolinate catabolic process [GO:0034213]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]{nicotinate-nucleotide diphosphorylase (carboxylating) activity [GO:0004514]; protein homodimerization activity [GO:0042803]\FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000269|PubMed:17868694}.P06753TPM3Tropomyosin alpha-3 chainbrain development [GO:0007420]; movement of cell or subcellular component [GO:0006928]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]brush border [GO:0005903]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle thin filament tropomyosin [GO:0005862]; stress fiber [GO:0001725]Q9BTT0AN32E=Acidic leucine-rich nuclear phosphoprotein 32 family member Ehistone exchange [GO:0043486]Ihistone binding [GO:0042393]; phosphatase inhibitor activity [GO:0019212]bcytoplasmic membrane-bounded vesicle [GO:0016023]; nucleus [GO:0005634]; Swr1 complex [GO:0000812]lFUNCTION: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. {ECO:0000269|PubMed:24463511}.O75940SPF303Survival of motor neuron-related-splicing factor 30SUBCELLULAR LOCATION: Nucleus speckle. Nucleus, Cajal body. Note=Detected in nuclear speckles containing snRNP and in Cajal (coiled) bodies.apoptotic process [GO:0006915]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Necessary for spliceosome assembly. Overexpression causes apoptosis. {ECO:0000269|PubMed:11331295, ECO:0000269|PubMed:11331595, ECO:0000269|PubMed:9817934}.Q92600RCD1)Cell differentiation protein RCD1 homologSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.xcytokine-mediated signaling pathway [GO:0019221]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of ligand-dependent nuclear receptor transcription coactivator activity [GO:2000327]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; sex differentiation [GO:0007548]; transcription, DNA-templated [GO:0006351]\protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]CCR4-NOT complex [GO:0030014]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation (By similarity). Can bind oligonucleotides, such as poly-G, poly-C or poly-T (in vitro), but the physiological relevance of this is not certain. Does not bind poly-A. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors, including RARA, expect ESR1-mediated transcription that is not only slightly increased, if at all. {ECO:0000250, ECO:0000269|PubMed:17189474, ECO:0000269|PubMed:18180299}.Q14938NFIXNuclear factor 1 X-typeastrocyte differentiation [GO:0048708]; cerebellar granule cell differentiation [GO:0021707]; cerebellar Purkinje cell layer development [GO:0021680]; DNA replication [GO:0006260]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription from RNA polymerase II promoter [GO:0006366]DNA binding [GO:0003677]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; sequence-specific DNA binding transcription factor activity [GO:0003700]Q96D09GASP27G-protein coupled receptor-associated sorting protein 2!beta-amyloid binding [GO:0001540]sFUNCTION: May play a role in regulation of a variety of G-protein coupled receptors. {ECO:0000269|PubMed:15086532}.Q14667K0100UPF0378 protein KIAA0100RFUNCTION: May be involved in membrane trafficking. {ECO:0000250|UniProtKB:K7VLR4}.Q08AE8SPIR1Protein spire homolog 1*actin family cytoskeletal protein(PC00041)dSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11747823}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11747823}. Cell membrane {ECO:0000269|PubMed:11747823}; Peripheral membrane protein {ECO:0000269|PubMed:11747823}; Cytoplasmic side {ECO:0000269|PubMed:11747823}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11. {ECO:0000250}.actin cytoskeleton organization [GO:0030036]; actin nucleation [GO:0045010]; cleavage furrow formation [GO:0036089]; establishment of meiotic spindle localization [GO:0051295]; formin-nucleated actin cable assembly [GO:0070649]; Golgi vesicle transport [GO:0048193]; intracellular transport [GO:0046907]; polar body extrusion after meiotic divisions [GO:0040038]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]cell cortex [GO:0005938]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Acts as a actin nucleation factor, remains associated with< the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. {ECO:0000269|PubMed:11747823, ECO:0000269|PubMed:21620703}.Q01167FOXK2Forkhead box protein K2danatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription from RNA polymerase II promoter [GO:0006366]magnesium ion binding [GO:0000287]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]AFUNCTION: Recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements. {ECO:0000269|PubMed:1339390, ECO:0000269|PubMed:1909027}.Q8IXK0PHC2Polyhomeotic-like protein 2cellular protein metabolic process [GO:0044267]; multicellular organismal development [GO:0007275]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; spermatogenesis [GO:0007283]_DNA binding [GO:0003677]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.P52756RBM5RNA-binding protein 5<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18851835}.apoptotic process [GO:0006915]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cell proliferation [GO:0008285]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]DNA binding [GO:0003677]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]^FUNCTION: Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis. {ECO:0000269|PubMed:10949932, ECO:0000269|PubMed:12207175, ECO:0000269|PubMed:12581154, ECO:0000269|PubMed:15192330, ECO:0000269|PubMed:16585163, ECO:0000269|PubMed:18840686, ECO:0000269|PubMed:18851835}.Q99797MIPEP$Mitochondrial intermediate peptidaseNprotein processing involved in protein targeting to mitochondrion [GO:0006627]RFUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size.Q9H1J7WNT5BProtein Wnt-5bcell fate commitment [GO:0045165]; cellular response to retinoic acid [GO:0071300]; chondrocyte differentiation [GO:0002062]; fat cell differentiation [GO:0045444]; lens fiber cell development [GO:0070307]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; neuron differentiation [GO:0030182]; positive regulation of cell migration [GO:0030335]; positive regulation of fat cell differentiation [GO:0045600]; Wnt signaling pathway [GO:0016055]<frizzled binding [GO:0005109]; receptor binding [GO:0005102]cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]Q13336UT1Urea transporter 13SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23219802}; Multi-pass membrane protein {ECO:0000269|PubMed:23219802}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Restricted to the basolateral membrane in various portions of the urothelium. {ECO:0000250}.ltransmembrane transport [GO:0055085]; urea transmembrane transport [GO:0071918]; urea transport [GO:0015840]urea channel activity [GO:0015265]; urea transmembrane transporter activity [GO:0015204]; water transmembrane transporter activity [GO:0005372]zbasolateral plasma membrane [GO:0016323]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Urea channel that facilitates transmembrane urea transport down a concentration gradient. A constriction of the transmembrane channel functions as selectivity filter through which urea is expected to pass in dehydrated form. The rate of urea conduction is increased by hypotonic stress. Plays an important role in the kidney medulla collecting ducts, where it allows rapid equilibration between the lumen of the collecting ducts and the interstitium, and thereby prevents water loss driven by the high concentration of urea in the urine. Facilitates urea transport across erythrocyte membranes. May also play a role in transmembrane water transport, possibly by indirect means.Q9UJ68MSRA4Mitochondrial peptide methionine sulfoxide reductaseSUBCELLULAR LOCATION: Isoform 1: Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Membrane; Lipid-anchor.cellular protein modification process [GO:0006464]; methionine metabolic process [GO:0006555]; protein repair [GO:0030091]; response to oxidative stress [GO:0006979]>peptide-methionine (S)-S-oxide reductase activity [GO:0008113]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.P48454PP2BCGSerine/threonine-protein phosphatase 2B catalytic subunit gamma isoformapoptotic process [GO:0006915]; intrinsic apoptotic signaling pathway [GO:0097193]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]Q9NQG5RPR1B;Regulation of nuclear pre-mRNA domain-containing protein 1B<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22264791}.*dephosphorylation of RNA polymerase II C-terminal domain [GO:0070940]; positive regulation of cell proliferation [GO:0008284]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell cycle process [GO:0010564]; transcription, DNA-templated [GO:0006351]< MDNA-directed RNA polymerase II, holoenzyme [GO:0016591]; nucleus [GO:0005634]CFUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation. {ECO:0000269|PubMed:22231121, ECO:0000269|PubMed:22264791}.P51114FXR17Fragile X mental retardation syndrome-related protein 1=SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7781595}.apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; muscle organ development [GO:0007517]; negative regulation of translation [GO:0017148]G-quadruplex RNA binding [GO:0002151]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]axon [GO:0030424]; costamere [GO:0043034]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]; ribonucleoprotein granule [GO:0035770]FUNCTION: RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs (By similarity). {ECO:0000250}.P28799GRN Granulinsblastocyst hatching [GO:0001835]; chondrocyte proliferation [GO:0035988]; embryo implantation [GO:0007566]; male mating behavior [GO:0060179]; neural precursor cell proliferation [GO:0061351]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of epithelial cell proliferation [GO:0050679]; response to estradiol [GO:0032355]; signal transduction [GO:0007165]; synaptic vesicle endocytosis [GO:0048488]Egrowth factor activity [GO:0008083]; poly(A) RNA binding [GO:0044822]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]*FUNCTION: Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling.; FUNCTION: Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.P52597HNRPF)Heterogeneous nuclear ribonucleoprotein Fnucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state. {ECO:0000269|PubMed:20526337}.Q99622C10 Protein C10>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23453666}.cFUNCTION: In brain, may be required for corpus callusum development. {ECO:0000269|PubMed:23453666}.Q07817B2CL1Bcl-2-like protein 1SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner membrane {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner (By similarity). Localizes to the centrosome when phosphorylated at Ser-49. {ECO:0000250}.T apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; apoptotic process in bone marrow [GO:0071839]; cell proliferation [GO:0008283]; cellular process regulating host cell cycle in response to virus [GO:0060154]; cellular response to alkaloid [GO:0071312]; cellular response to amino acid stimulus [GO:0071230]; cellular response to gamma radiation [GO:0071480]; cytokinesis [GO:0000910]; endocytosis [GO:0006897]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fertilization [GO:0009566]; germ cell development [GO:0007281]; growth [GO:0040007]; hepatocyte apoptotic process [GO:0097284]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; in utero embryonic development [GO:0001701]; male gonad development [GO:0008584]; mitochondrion morphogenesis [GO:0070584]; mitotic cell cycle checkpoint [GO:0007093]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of establishment of protein localization to plasma membrane [GO:0090005]; negative regulation of execution phase of apoptosis [GO:1900118]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; neuron apoptotic process [GO:0051402]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; ovarian follicle development [GO:0001541]; positive regulation of cell proliferation [GO:0008284]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; programmed cell death [GO:0012501]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane potential [GO:0051881]; release of cytochrome c from mitochondria [GO:0001836]; response to cycloheximide [GO:0046898]; response to cytokine [GO:0034097]; spermatogenesis [GO:0007283]; suppression by virus of host apoptotic process [GO:0019050]BH3 domain binding [GO:0051434]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]Bcl-2 family protein complex [GO:0097136]; cell junction [GO:0030054]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleus [GO:0005634]; synaptic vesicle membrane [GO:0030672]FUNCTION: Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.; FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal < neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles.; FUNCTION: Isoform Bcl-X(S) promotes apoptosis.Q96MW5COG8,Conserved oligomeric Golgi complex subunit 8SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11703943}; Peripheral membrane protein {ECO:0000269|PubMed:11703943}.XGolgi membrane [GO:0000139]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]Q9P2L0WDR35WD repeat-containing protein 35SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}.cilium assembly [GO:0042384]; intraciliary retrograde transport [GO:0035721]; organelle organization [GO:0006996]; protein localization to cilium [GO:0061512]axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; cilium [GO:0005929]; intraciliary transport particle A [GO:0030991]; primary cilium [GO:0072372]FUNCTION: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. Required for ciliogenesis. May promote CASP3 activation and TNF-stimulated apoptosis. {ECO:0000269|PubMed:20193664, ECO:0000269|PubMed:21473986}.P13645K1C10Keratin, type I cytoskeletal 10Xcellular response to calcium ion [GO:0071277]; keratinocyte differentiation [GO:0030216]0structural constituent of epidermis [GO:0030280]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634]O14827RGRF22Ras-specific guanine nucleotide-releasing factor 2SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Translocates to membranes when activated. Found both at cell periphery and along the axon of neurons (By similarity). {ECO:0000250}.apoptotic signaling pathway [GO:0097190]; long-term synaptic potentiation [GO:0060291]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; regulation of N-methyl-D-aspartate selective glutamate receptor activity [GO:2000310]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; synaptic transmission [GO:0007268]_cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]oFUNCTION: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation. {ECO:0000269|PubMed:15128856}.Q9NNX1TUFT1TuftelinSUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P27628}. Note=Secreted at a very early stage of enamel formation, concentrated at the dentin-enamel junction and tightly bound to the surface of the growing crystallites. {ECO:0000250|UniProtKB:P27628}.<bone mineralization [GO:0030282]; odontogenesis [GO:0042476]3structural constituent of tooth enamel [GO:0030345]9cytoplasm [GO:0005737]; extracellular region [GO:0005576]oFUNCTION: Involved in the mineralization and structural organization of enamel. {ECO:0000250|UniProtKB:P27628}.Q96BI1S22AI"Solute carrier family 22 member 18SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localized at the apical membrane surface of renal proximal tubules. {ECO:0000269|PubMed:9744804}.drug transmembrane transport [GO:0006855]; drug transport [GO:0015893]; excretion [GO:0007588]; organic cation transport [GO:0015695]; transmembrane transport [GO:0055085]drug transmembrane transporter activity [GO:0015238]; symporter activity [GO:0015293]; ubiquitin protein ligase binding [GO:0031625]apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]FUNCTION: May act as a transporter of organic cations based on a proton efflux antiport mechanism. May play a role in the transport of chloroquine and quinidine-related compounds in kidney. {ECO:0000269|PubMed:9744804}.Q86Y79PTH Probable peptidyl-tRNA hydrolasePaminoacyl-tRNA hydrolase activity [GO:0004045]; poly(A) RNA binding [GO:0044822]O95427PIGN(GPI ethanolamine phosphate transferase 1=mannose-ethanolamine phosphotransferase activity [GO:0051377]uFUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation. {ECO:0000250, ECO:0000269|PubMed:23446422}.Q8WXE0CSKI2Caskin-2Q92615LAR4BLa-related protein 4BSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20573744}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs in response to arsenite treatment./positive regulation of translation [GO:0045727]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; polysomal ribosome [GO:0042788]EFUNCTION: Stimulates mRNA translation. {ECO:0000269|PubMed:20573744}.Q9UKN8TF3C4-General transcription factor 3C polypeptide 45S class rRNA transcription from RNA polymerase III type 1 promoter [GO:0042791]; gene expression [GO:0010467]; histone acetylation [GO:0016573]; positive regulation of catalytic activity [GO:0043085]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase III promoter [GO:0006383]; transcription initiation from RNA polymerase III promoter [GO:0006384]; tRNA transcription from RNA polymerase III promoter [GO:0042797]qDNA binding [GO:0003677]; enzyme activator activity [GO:0008047]; histone acetyltransferase activity [GO:0004402]FUNCTION: Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box.Q9NY93DDX56)Probable ATP-dependent RNA helicase DDX56FUNCTION: May play a role in later stages of the processing of the pre-ribosomal particles leading to mature 60S ribosomal subunits. Has intrinsic ATPase activity.A2RTX5SYTC2.Probable threonine--tRNA ligase 2, cytoplasmic)threonyl-tRNA aminoacylation [GO:0006435]P84090ERHEnhancer of rudimentary homolog+cell cycle [GO:0007049]; nucleobase-containing compound metabolic process [GO:0006139]; osteoblast differentiation [GO:0001649]; positive regulation of Notch signaling pathway [GO:0045747]; pyrimidine nucleoside metabolic process [GO:0006213]; pyrimidine nucleotide biosynthetic process [GO:0006221]+membrane [GO:0016020]; midbody [GO:0030496],FUNCTION: May have a role in the cell cycle.Q7RTN6STRAA*STE20-related kinase adapter protein alphaSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248}. Cytoplasm {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248}.actin cytoskeleton organization [GO:0030036]; activation of protein kinase activity [GO:0032147]; cell cycle arrest [GO:0007050]; cell migration [GO:0016477]; insulin receptor signaling pathway [GO:0008286]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; protein export from nucleus [GO:0006611]< ; protein heterooligomerization [GO:0051291]; regulation of apoptotic process [GO:0042981]; regulation of MAPK cascade [GO:0043408]; regulation of mitotic cell cycle [GO:0007346]; Rho protein signal transduction [GO:0007266]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; kinase binding [GO:0019900]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activator activity [GO:0043539]zcytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation. {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:19892943}.P02795MT2Metallothionein-2{cellular copper ion homeostasis [GO:0006878]; cellular response to drug [GO:0035690]; cellular response to erythropoietin [GO:0036018]; cellular response to interleukin-3 [GO:0036016]; cellular response to zinc ion [GO:0071294]; cytokine-mediated signaling pathway [GO:0019221]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of growth [GO:0045926]8drug binding [GO:0008144]; zinc ion binding [GO:0008270]FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.O60231DHX16BPutative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16icytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]Q14527HLTF"Helicase-like transcription factorSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:8672239}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is stimulated by progesterone. {ECO:0000250}.chromatin modification [GO:0016568]; postreplication repair [GO:0006301]; protein polyubiquitination [GO:0000209]; regulation of transcription, DNA-templated [GO:0006355]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]FUNCTION: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA. {ECO:0000250, ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:7876228, ECO:0000269|PubMed:8672239, ECO:0000269|PubMed:9126292}.P13995MTDCRBifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrialfolic acid-containing compound biosynthetic process [GO:0009396]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate metabolic process [GO:0046653]magnesium ion binding [GO:0000287]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]; phosphate ion binding [GO:0042301]Q16595FRDAFrataxin, mitochondrialvSUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=PubMed:18725397 reports localization exclusively in mitochondria.adult walking behavior [GO:0007628]; aerobic respiration [GO:0009060]; cellular iron ion homeostasis [GO:0006879]; cellular response to hydrogen peroxide [GO:0070301]; embryo development ending in birth or egg hatching [GO:0009792]; heme biosynthetic process [GO:0006783]; ion transport [GO:0006811]; iron incorporation into metallo-sulfur cluster [GO:0018283]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of organ growth [GO:0046621]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; oxidative phosphorylation [GO:0006119]; positive regulation of aconitate hydratase activity [GO:1904234]; positive regulation of cell growth [GO:0030307]; positive regulation of cell proliferation [GO:0008284]; positive regulation of lyase activity [GO:0051349]; positive regulation of metalloenzyme activity [GO:0048554]; positive regulation of succinate dehydrogenase activity [GO:1904231]; proprioception [GO:0019230]; protein autoprocessing [GO:0016540]; regulation of ferrochelatase activity [GO:0010722]; response to iron ion [GO:0010039]; small molecule metabolic process [GO:0044281]2 iron, 2 sulfur cluster binding [GO:0051537]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; iron chaperone activity [GO:0034986]; iron-sulfur cluster binding [GO:0051536]RFUNCTION: Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1. {ECO:0000269|PubMed:12785837, ECO:0000269|PubMed:15247478, ECO:0000269|PubMed:15641778, ECO:0000269|PubMed:16239244, ECO:0000269|PubMed:16608849, ECO:0000269|PubMed:20053667}.Q9P2B7K1430UPF0501 protein KIAA1430Q12986NFX1Transcriptional repressor NF-X1inflammatory response [GO:0006954]; negative regulation of MHC class II biosynthetic process [GO:0045347]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]ligase activity [GO:0016874]; poly(A) RNA binding [GO:0044822]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270](FUNCTION: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Isoform 3 binds to the X-box motif of TERT promoter and represses its expression. Together with PABPC1 or PABPC4, isoform 1 acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:15371341, ECO:0000269|PubMed:17267499}.Q8IWA0WDR75WD repeat-containing protein 75|positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of mitochondrion degradation [GO:1903146]Q8TBX8PI42C< 6Phosphatidylinositol 5-phosphate 4-kinase type-2 gammaSUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Mostly found in the cytosol and surrounding plasma membrane. However, its presence in the endoplasmic reticulum seems to be a prerequisite for PIP2 synthesis (By similarity). {ECO:0000250}.1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane [GO:0016020]FUNCTION: May play an important role in the production of Phosphatidylinositol bisphosphate (PIP2), in the endoplasmic reticulum. {ECO:0000250}.Q8WUF5IASPPRelA-associated inhibitorZSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic but also nuclear.Dapoptotic process [GO:0006915]; cardiac muscle contraction [GO:0060048]; cardiac right ventricle morphogenesis [GO:0003215]; embryonic camera-type eye development [GO:0031076]; hair cycle [GO:0042633]; multicellular organismal homeostasis [GO:0048871]; multicellular organism growth [GO:0035264]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cell differentiation [GO:0045597]; post-embryonic development [GO:0009791]; transcription, DNA-templated [GO:0006351]; ventricular cardiac muscle tissue development [GO:0003229]identical protein binding [GO:0042802]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]kcell junction [GO:0030054]; cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; nucleus [GO:0005634]FUNCTION: Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis. {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:12134007, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15489900}.P54252ATX3Ataxin-3SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9580663}. Note=Predominantly nuclear, but not exclusively, inner nuclear matrix.5actin cytoskeleton organization [GO:0030036]; cellular response to heat [GO:0034605]; cellular response to misfolded protein [GO:0071218]; intermediate filament cytoskeleton organization [GO:0045104]; microtubule cytoskeleton organization [GO:0000226]; misfolded or incompletely synthesized protein catabolic process [GO:0006515]; monoubiquitinated protein deubiquitination [GO:0035520]; nervous system development [GO:0007399]; nucleotide-excision repair [GO:0006289]; positive regulation of ERAD pathway [GO:1904294]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; protein localization to cytosolic proteasome complex involved in ERAD pathway [GO:1904379]; regulation of cell-substrate adhesion [GO:0010810]; regulation of transcription, DNA-templated [GO:0006355]; synaptic transmission [GO:0007268]; transcription, DNA-templated [GO:0006351]; ubiquitin-dependent protein catabolic process [GO:0006511]6ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; Lys48-specific deubiquitinase activity [GO:1990380]; Lys63-specific deubiquitinase activity [GO:0061578]; omega peptidase activity [GO:0008242]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-specific protease activity [GO:0004843]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; nuclear inclusion body [GO:0042405]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins. Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. In response to misfolded substrate ubiquitination, mediates deubiquitination of monoubiquitinated STUB1/CHIP. Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription. {ECO:0000269|PubMed:12297501, ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:23625928}.Q8TB96TIPT-cell immunomodulatory proteinxSUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.FUNCTION: Modulator of T-cell function. Has a protective effect in graft versus host disease model (By similarity). {ECO:0000250}.Q8TAF3WDR48WD repeat-containing protein 48SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Lysosome. Note=Mainly cytoplasmic. In case of infection by papillomavirus HPV11, translocates to the nucleus via its interaction with papillomavirus HPV11.>double-strand break repair via homologous recombination [GO:0000724]; embryonic organ development [GO:0048568]; homeostasis of number of cells [GO:0048872]; multicellular organism growth [GO:0035264]; positive regulation of epithelial cell proliferation [GO:0050679]; protein deubiquitination [GO:0016579]; regulation of protein monoubiquitination [GO:1902525]; seminiferous tubule development [GO:0072520]; single fertilization [GO:0007338]; skeletal system morphogenesis [GO:0048705]; skin development [GO:0043588]; spermatogenesis [GO:0007283]; viral process [GO:0016032]bintracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; nucleus [GO:0005634]]FUNCTION: Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 by enhancing the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Also activates deubiquitinating activity of complexes containing USP12 and USP46, respectively. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. In case of infection by Herpesvirus saimiri, may play a role in vesicular transport or membrane fusion events necessary for transport to lysosomes. Induces lysosomal vesicle formation via interaction with Herpesvirus saimiri tyrosine kinase-interacting protein (TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK, resulting in down-regulation of T-cell antigen receptor TCR. May play a role in generation of enlarged endosomal vesicles via interaction with TIP. In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1. {ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014}.Q9H6R4NOL6Nucleolar protein 6SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Chromosome {ECO:0000250}. Note=Localizes to condensed chromosomes in mitosis. {ECO:0000250}.CrRNA processing [GO:0006364]; tRNA export from nucleus [GO:0006409]condensed nuclear chromosome [GO:0000794]; CURI complex [GO:0032545]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]; UTP-C complex [GO:0034456]P56537IF6*Eukaryotic translation initiation factor 6kSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus.mature ribosome assembly [GO:0042256]; ribosomal large subunit biogenesis [GO:0042273]; ribosomal subunit export from nucleus [GO:0000054]ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022]; translation initiation factor ac< tivity [GO:0003743]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; lamin filament [GO:0005638]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May behave as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (GNB2L1)-dependent protein kinase C activity. {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:10085284, ECO:0000269|PubMed:14654845, ECO:0000269|PubMed:21536732}.Q8NC42RN149"E3 ubiquitin-protein ligase RNF149cellular response to drug [GO:0035690]; negative regulation of MAPK cascade [GO:0043409]; regulation of protein stability [GO:0031647]FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation. {ECO:0000269|PubMed:22628551}.Q8TAG9EXOC6Exocyst complex component 6cellular protein metabolic process [GO:0044267]; erythrocyte differentiation [GO:0030218]; membrane organization [GO:0061024]; organelle organization [GO:0006996]; protein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]Hcytosol [GO:0005829]; exocyst [GO:0000145]; plasma membrane [GO:0005886]eFUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (By similarity). {ECO:0000250}.Q9NRN5OLFL3Olfactomedin-like protein 3=SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15280020}."extracellular vesicle [GO:1903561](FUNCTION: Secreted scaffold protein that plays an essential role in dorsoventral patterning during early development. Stabilizes axial formation by restricting chordin (CHRD) activity on the dorsal side. Acts by facilitating the association between the tolloid proteases and their substrate chordin (CHRD), leading to enhance chordin (CHRD) degradation (By similarity). May have matrix-related function involved in placental and embryonic development, or play a similar role in other physiological processes. {ECO:0000250, ECO:0000269|PubMed:15280020}.Q9H930SP14L'Nuclear body protein SP140-like proteinWchromatin binding [GO:0003682]; DNA binding [GO:0003677]; zinc ion binding [GO:0008270]Q9UEY8ADDG Gamma-adducinCresponse to drug [GO:0042493]; transmembrane transport [GO:0055085]Cbrush border [GO:0005903]; cell-cell junction [GO:0005911]; cell cortex [GO:0005938]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]Q9Y2M5KLH20Kelch-like protein 20SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Golgi apparatus, trans-Golgi network. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (PubMed:20389280). {ECO:0000269|PubMed:20389280}.wcytoskeleton organization [GO:0007010]; Golgi to endosome transport [GO:0006895]; negative regulation of apoptotic process [GO:0043066]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K33-linked ubiquitination [GO:1990390]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567]; response to interferon-alpha [GO:0035455]Zinterferon-gamma binding [GO:0019964]; ubiquitin-protein transferase activity [GO:0004842]actin cytoskeleton [GO:0015629]; axon [GO:0030424]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; PML body [GO:0016605]; trans-Golgi network [GO:0005802]FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486). {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17395875, ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212, ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:24768539}.P17707DCAM,S-adenosylmethionine decarboxylase proenzyme]cellular nitrogen compound metabolic process [GO:0034641]; polyamine metabolic process [GO:0006595]; S-adenosylmethioninamine biosynthetic process [GO:0006557]; S-adenosylmethionine metabolic process [GO:0046500]; small molecule metabolic process [GO:0044281]; spermidine biosynthetic process [GO:0008295]; spermine biosynthetic process [GO:0006597]Wadenosylmethionine decarboxylase activity [GO:0004014]; putrescine binding [GO:0019810]FUNCTION: Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels (By similarity). {ECO:0000250}.Q9NYZ1TV23B0Golgi apparatus membrane protein TVP23 homolog BGprotein secretion [GO:0009306]; vesicle-mediated transport [GO:0016192]Q13451FKBP5)Peptidyl-prolyl cis-trans isomerase FKBP5~FK506 binding [GO:0005528]; heat shock protein binding [GO:0031072]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]YFUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded.O95822DCMC(Malonyl-CoA decarboxylase, mitochondrial SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10417274}. Mitochondrion matrix {ECO:0000269|PubMed:10417274}. Peroxisome {ECO:0000269|PubMed:10417274}. Peroxisome matrix {ECO:0000250}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250}.wacetyl-CoA biosynthetic process [GO:0006085]; cellular lipid metabolic process [GO:0044255]; fatty acid biosynthetic process [GO:0006633]; malonyl-CoA catabolic process [GO:2001294]; positive regulation of fatty acid oxidation [GO:0046321]; regulation of glucose metabolic process [GO:0010906]; response to ischemia [GO:0002931]; small molecule metabolic process [GO:0044281]Nmalonyl-CoA decarboxylase activity [GO:0050080]; receptor binding [GO:0005102]cytoplasm [GO:0005737]; mitochondrial matrix< [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]7FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:18314420, ECO:0000269|PubMed:23482565}.Q86YP4P66A#Transcriptional repressor p66-alphaSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}. Note=Speckled nuclear localization requires both CR1 and CR2 regions.yanterior neuropore closure [GO:0021506]; blood vessel development [GO:0001568]; DNA methylation [GO:0006306]; embryonic body morphogenesis [GO:0010172]; in utero embryonic development [GO:0001701]; negative regulation of transcription, DNA-templated [GO:0045892]; neural fold formation [GO:0001842]; programmed cell death [GO:0012501]; transcription, DNA-templated [GO:0006351]protein binding, bridging [GO:0030674]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; zinc ion binding [GO:0008270]enuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B. {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.Q01831XPC+DNA repair protein complementing XP-C cellsSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions.ccellular protein metabolic process [GO:0044267]; DNA repair [GO:0006281]; intra-S DNA damage checkpoint [GO:0031573]; mismatch repair [GO:0006298]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; nucleotide-excision repair, DNA damage removal [GO:0000718]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; regulation of mitotic cell cycle phase transition [GO:1901990]; response to auditory stimulus [GO:0010996]; response to drug [GO:0042493]; response to UV-B [GO:0010224]; UV-damage excision repair [GO:0070914]bubble DNA binding [GO:0000405]; damaged DNA binding [GO:0003684]; heteroduplex DNA loop binding [GO:0000404]; single-stranded DNA binding [GO:0003697]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleotide-excision repair factor 2 complex [GO:0000111]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; XPC complex [GO:0071942]lFUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.; FUNCTION: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.Q70CQ2UBP34(Ubiquitin carboxyl-terminal hydrolase 34Rpositive regulation of canonical Wnt signaling pathway [GO:0090263]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; regulation of proteasomal protein catabolic process [GO:0061136]; Wnt signaling pathway [GO:0016055]|FUNCTION: Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000269|PubMed:21383061}.Q9HCG8CWC22&Pre-mRNA-splicing factor CWC22 homologSUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins.fmRNA splicing, via spliceosome [GO:0000398]; regulation of mRNA splicing, via spliceosome [GO:0048024]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]FUNCTION: Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay. {ECO:0000269|PubMed:22959432, ECO:0000269|PubMed:22961380, ECO:0000269|PubMed:23236153}.P39880CUX1Homeobox protein cut-like 1auditory receptor cell differentiation [GO:0042491]; kidney development [GO:0001822]; lung development [GO:0030324]; multicellular organismal development [GO:0007275]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of dendrite morphogenesis [GO:0050775]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; retrograde transport, vesicle recycling within Golgi [GO:0000301]7chromatin binding [GO:0003682]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; RNA polymerase II regulatory region sequence-specif< ic DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]Gcytosol [GO:0005829]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]aFUNCTION: Probably has a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator (By similarity). {ECO:0000250}.Q2KHT3CL16AProtein CLEC16ASUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q80U30}; Peripheral membrane protein. Lysosome membrane {ECO:0000250|UniProtKB:Q80U30}; Peripheral membrane protein. Note=Associates with the endolysosome membrane. {ECO:0000250|UniProtKB:Q80U30}.FUNCTION: Regulator of mitophagy through the upstream regulation of the RNF41/NRDP1-PARK2 pathway. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. The RNF41/NRDP1-PARK2 pathway regulates autophagosome-lysosome fusion during late mitophagy. May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which regulates proteosomal degradation of PARK2. Plays a key role in beta cells functions by regulating mitophagy/autophagy and mitochondrial health. {ECO:0000269|PubMed:24949970}.P31323KAP3=cAMP-dependent protein kinase type II-beta regulatory subunitSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in the cytoplasm and at the cell membrane.Aactivation of phospholipase C activity [GO:0007202]; activation of protein kinase A activity [GO:0034199]; blood coagulation [GO:0007596]; cellular response to glucagon stimulus [GO:0071377]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; fatty acid metabolic process [GO:0006631]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; learning [GO:0007612]; mitotic cell cycle [GO:0000278]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; regulation of insulin secretion [GO:0050796]; renal water homeostasis [GO:0003091]; response to antipsychotic drug [GO:0097332]; response to clozapine [GO:0097338]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; water transport [GO:0006833]cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]O75718CRTAPCartilage-associated protein2chaperone-mediated protein folding [GO:0061077]; extracellular matrix organization [GO:0030198]; negative regulation of post-translational protein modification [GO:1901874]; peptidyl-proline hydroxylation to 3-hydroxy-L-proline [GO:0018400]; protein stabilization [GO:0050821]; spermatogenesis [GO:0007283]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; macromolecular complex [GO:0032991]; proteinaceous extracellular matrix [GO:0005578]wFUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. {ECO:0000269|PubMed:17055431}.P50579MAP2Methionine aminopeptidase 2SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:21537465}. Note=About 30% of expressed METAP2 associates with polysomes.]N-terminal protein amino acid modification [GO:0031365]; peptidyl-methionine modification [GO:0018206]; phototransduction, visible light [GO:0007603]; protein initiator methionine removal [GO:0070084]; protein processing [GO:0016485]; regulation of rhodopsin mediated signaling pathway [GO:0022400]; rhodopsin mediated signaling pathway [GO:0016056]aminopeptidase activity [GO:0004177]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235]; poly(A) RNA binding [GO:0044822]FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.Q9BT25HAUS8"HAUS augmin-like complex subunit 8SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=During interphase, primarily cytoplasmic and associates with centrosomes and with the mitotic spindles, preferentially at the spindle pole vicinity. During anaphase and telophase, additionally associates with the spindle midzone and midbody, respectively.centrosome [GO:0005813]; cytoplasm [GO:0005737]; HAUS complex [GO:0070652]; microtubule [GO:0005874]; spindle pole [GO:0000922]FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:18362163, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.Q8N283ANR35+Ankyrin repeat domain-containing protein 35P07942LAMB1Laminin subunit beta-1@axon guidance [GO:0007411]; cell adhesion [GO:0007155]; embryo implantation [GO:0007566]; endodermal cell differentiation [GO:0035987]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; neuronal-glial interaction involved in cerebral cortex radial glia guided migration [GO:0021812]; neuron projection development [GO:0031175]; odontogenesis [GO:0042476]; positive regulation of cell migration [GO:0030335]; positive regulation of epithelial cell proliferation [GO:0050679]; substrate adhesion-dependent cell spreading [GO:0034446]extracellular matrix structural constituent [GO:0005201]; glycosphingolipid binding [GO:0043208]; structural molecule activity [GO:0005198]Ybasement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-10 complex [GO:0043259]; laminin-1 complex [GO:0005606]; laminin-2 complex [GO:0005607]; laminin-8 complex [GO:0043257]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaf< fold for neurons migrating toward the pial surface. {ECO:0000269|PubMed:23472759}.O15226NKRFNF-kappa-B-repressing factorknegative regulation of transcription, DNA-templated [GO:0045892]; transcription, DNA-templated [GO:0006351]Pendoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: Interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes. Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity. Also involved in the regulation of IL-8 transcription. {ECO:0000269|PubMed:12381793}.Q14139UBE4A!Ubiquitin conjugation factor E4 A?SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:E9Q735}.cprotein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511]Nligase activity [GO:0016874]; ubiquitin-ubiquitin ligase activity [GO:0034450]=cytoplasm [GO:0005737]; ubiquitin ligase complex [GO:0000151]FUNCTION: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates 'Lys-48'-linked polyubiquitination of substrates. {ECO:0000250|UniProtKB:E9Q735, ECO:0000250|UniProtKB:P54860}.Q8WUA7TB22ATBC1 domain family member 22AP17029ZKSC10Zinc finger protein with KRAB and SCAN domains 1Q02763TIE2Angiopoietin-1 receptorSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Secreted. Note=Recruited to cell-cell contacts in quiescent endothelial cells. Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell. Proteolytic processing gives rise to a soluble extracellular domain that is secreted. angiogenesis [GO:0001525]; blood coagulation [GO:0007596]; cell-cell signaling [GO:0007267]; cell-matrix adhesion [GO:0007160]; definitive hemopoiesis [GO:0060216]; endochondral ossification [GO:0001958]; endothelial cell proliferation [GO:0001935]; glomerulus vasculature development [GO:0072012]; heart development [GO:0007507]; heart trabecula formation [GO:0060347]; intracellular signal transduction [GO:0035556]; leukocyte migration [GO:0050900]; negative regulation of angiogenesis [GO:0016525]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of inflammatory response [GO:0050728]; organ regeneration [GO:0031100]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cytokine secretion involved in immune response [GO:0002741]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; protein autophosphorylation [GO:0046777]; protein oligomerization [GO:0051259]; regulation of endothelial cell apoptotic process [GO:2000351]; regulation of establishment or maintenance of cell polarity [GO:0032878]; regulation of NIK/NF-kappaB signaling [GO:1901222]; regulation of vascular permeability [GO:0043114]; response to cAMP [GO:0051591]; response to estrogen [GO:0043627]; response to hypoxia [GO:0001666]; response to peptide hormone [GO:0043434]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]; sprouting angiogenesis [GO:0002040]; substrate adhesion-dependent cell spreading [GO:0034446]; Tie signaling pathway [GO:0048014]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; receptor activity [GO:0004872]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; cytoskeleton [GO:0005856]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; microvillus [GO:0005902]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1. {ECO:0000269|PubMed:12816861, ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:18366015, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:20651738, ECO:0000269|PubMed:9204896}.A6NIV6LRIQ46Leucine-rich repeat and IQ domain-containing protein 4Q969J3L12R16Loss of heterozygosity 12 chromosomal region 1 proteinQ8NC38CA213+Putative uncharacterized protein ZNF436-AS1Q5M9Q1NKAPLNKAP-like proteinP07602SAP ProsaposinSUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:21835174}.; SUBCELLULAR LOCATION: Prosaposin: Secreted. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000250|UniProtKB:Q61207}.adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway [GO:0007193]; blood coagulati< on [GO:0007596]; cellular response to organic substance [GO:0071310]; epithelial cell differentiation involved in prostate gland development [GO:0060742]; glycosphingolipid metabolic process [GO:0006687]; lipid transport [GO:0006869]; negative regulation of hydrogen peroxide-induced cell death [GO:1903206]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of catalytic activity [GO:0043085]; positive regulation of MAPK cascade [GO:0043410]; prostate gland growth [GO:0060736]; regulation of lipid metabolic process [GO:0019216]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]Benzyme activator activity [GO:0008047]; lipid binding [GO:0008289]vextracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.; FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.; FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; FUNCTION: Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling. {ECO:0000250|UniProtKB:Q61207}.; FUNCTION: Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.Q96ST2IWS1Protein IWS1 homologSUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882}.mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; regulation of histone H3-K36 trimethylation [GO:2001253]; regulation of histone H4 acetylation [GO:0090239]; regulation of mRNA export from nucleus [GO:0010793]; regulation of mRNA processing [GO:0050684]; regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]1FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. {ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19141475}.P61244MAX Protein maxGSUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite {ECO:0000250}.mRNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity [GO:0000983]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]xcytoplasm [GO:0005737]; dendrite [GO:0030425]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.O00488ZN593Zinc finger protein 593activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; transcription, DNA-templated [GO:0006351]iDNA binding [GO:0003677]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]FUNCTION: Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins.Q9H8K7CJ088 Uncharacterized protein C10orf88Q9BZ72PITM2;Membrane-associated phosphatidylinositol transfer protein 2SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:22361696}; Peripheral membrane protein {ECO:0000269|PubMed:22361696}.6metabolic process [GO:0008152]; transport [GO:0006810]<calcium ion binding [GO:0005509]; lipid binding [GO:0008289]endomembrane system [GO:0012505]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions. {ECO:0000269|PubMed:10022914}.Q9UBP4DKK3Dickkopf-related protein 3adrenal gland development [GO:0030325]; anatomical structure morphogenesis [GO:0009653]; negative regulation of aldosterone biosynthetic process [GO:0032348]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cortisol biosynthetic process [GO:2000065]; negative regulation of transcription, DNA-templated [GO:0045892]; Wnt signaling pathway [GO:0016055]FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). {ECO:0000250}.O75110ATP9A-Probable phospholipid-transporting ATPase IIA`SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Recycling endosome {ECO:0000269|PubMed:21914794}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794}. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.endocytosis [GO:0006897]; phospholipid translocation [GO:0045332]; retrograde vesicle-mediated transport, Golgi to ER [GO:0006890]early endosome [GO:0005769]; early endosome membrane [GO:0031901]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]Q8IZ83A16A1*Aldehyde dehydrogenase family 16 member A1Q86X52CHSS1Chondroitin sulfate synthase 1SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted.$bone morphogenesis [GO:0060349]; carbohydrate metabolic process [GO:0005975]; chondrocyte development [GO:0002063]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroi< tin sulfate metabolic process [GO:0030204]; glycosaminoglycan metabolic process [GO:0030203]; negative regulation of ossification [GO:0030279]; positive regulation of smoothened signaling pathway [GO:0045880]; proximal/distal pattern formation [GO:0009954]; response to nutrient levels [GO:0031667]; small molecule metabolic process [GO:0044281]; sulfation [GO:0051923]glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity [GO:0047238]; metal ion binding [GO:0046872]; N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity [GO:0050510]extracellular region [GO:0005576]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Involved in the negative control of osteogenesis likely through the modulation of NOTCH signaling. {ECO:0000269|PubMed:11514575, ECO:0000269|PubMed:21129727}.P57768SNX16Sorting nexin-16SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}.early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; protein targeting to lysosome [GO:0006622]early endosome [GO:0005769]; early endosome membrane [GO:0031901]; extrinsic component of endosome membrane [GO:0031313]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosome [GO:0005764]FUNCTION: May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling. Plays a role in intracellular transport of vesicular stomatitis virus nucleocapsids from the endosome to the cytoplasm. {ECO:0000269|PubMed:12813048, ECO:0000269|PubMed:15951806}.Q96FX8PERP(p53 apoptosis effector related to PMP-22SUBCELLULAR LOCATION: Cell junction, desmosome. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Associated with desmosomes. {ECO:0000250}.'activation of cysteine-type endopeptidase activity [GO:0097202]; amelogenesis [GO:0097186]; desmosome organization [GO:0002934]; heterotypic cell-cell adhesion [GO:0034113]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; positive regulation of proteolysis [GO:0045862]desmosome [GO:0030057]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; mitochondrion [GO:0005739]FUNCTION: Component of intercellular desmosome junctions. Plays a role in stratified epithelial integrity and cell-cell adhesion by promoting desmosome assembly. Plays a role as an effector in the TP53-dependent apoptotic pathway (By similarity). {ECO:0000250}.O15400STX7 Syntaxin-7pSUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.yintracellular protein transport [GO:0006886]; organelle assembly [GO:0070925]; organelle localization [GO:0051640]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of protein localization to plasma membrane [GO:1903076]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]chloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]xazurophil granule [GO:0042582]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endomembrane system [GO:0012505]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; tertiary granule [GO:0070820]; vesicle [GO:0031982]FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.Q7L0J3SV2A Synaptic vesicle glycoprotein 2A0SUBCELLULAR LOCATION: Cell junction, synapse {ECO:0000250|UniProtKB:Q9JIS5}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q02563, ECO:0000250|UniProtKB:Q9JIS5}.Vcellular calcium ion homeostasis [GO:0006874]; neurotransmitter transport [GO:0006836]tprotein kinase binding [GO:0019901]; receptor activity [GO:0004872]; transmembrane transporter activity [GO:0022857]Vcell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]FUNCTION: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity). {ECO:0000250}.O95183VAMP5%Vesicle-associated membrane protein 5SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus (By similarity). {ECO:0000250}.cell differentiation [GO:0030154]; exocytosis [GO:0006887]; Golgi to plasma membrane protein transport [GO:0043001]; muscle organ development [GO:0007517]; skeletal muscle tissue development [GO:0007519]; vesicle fusion [GO:0006906]cell surface [GO:0009986]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; integral component of organelle membrane [GO:0031301]; integral component of plasma membrane [GO:0005887]; intercalated disc [GO:0014704]; late endosome [GO:0005770]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; trans-Golgi network [GO:0005802]FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.Q9BY67CADM1Cell adhesion molecule 1Cell adhesion molecules(8)SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11279526}; Single-pass type I membrane protein {ECO:0000269|PubMed:11279526}. Cell junction, synapse {ECO:0000250}. Note=Associates with perinuclear and plasma membranes in vivo. Localized to the basolateral plasma membrane of epithelial cells in gall bladder. {ECO:0000250|UniProtKB:Q8R5M8, ECO:0000255, ECO:0000269|PubMed:11279526}.adherens junction organization [GO:0034332]; apoptotic process [GO:0006915]; bone development [GO:0060348]; brain development [GO:0007420]; calcium-independent cell-cell adhesion via plasm< a membrane cell-adhesion molecules [GO:0016338]; cell-cell junction organization [GO:0045216]; cell differentiation [GO:0030154]; cell junction assembly [GO:0034329]; cell recognition [GO:0008037]; detection of stimulus [GO:0051606]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; immune system process [GO:0002376]; liver development [GO:0001889]; positive regulation of cytokine secretion [GO:0050715]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; spermatogenesis [GO:0007283]; susceptibility to natural killer cell mediated cytotoxicity [GO:0042271]; synapse assembly [GO:0007416]; unidimensional cell growth [GO:0009826]cell adhesion molecule binding [GO:0050839]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803]; receptor activity [GO:0004872]; receptor binding [GO:0005102]Vbasolateral plasma membrane [GO:0016323]; cell body fiber [GO:0070852]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; varicosity [GO:0043196]]FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly (By similarity). May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. {ECO:0000250, ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:12920246, ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:15905536, ECO:0000269|PubMed:22438059}.Q8N129CNPY4Protein canopy homolog 4oFUNCTION: Plays a role in the regulation of the cell surface expression of TLR4. {ECO:0000269|PubMed:16338228}.Q9NVU7SDA1Protein SDA1 homologdSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:14976432}.actin cytoskeleton organization [GO:0030036]; protein transport [GO:0015031]; ribosomal large subunit biogenesis [GO:0042273]; ribosomal large subunit export from nucleus [GO:0000055]YFUNCTION: Required for 60S pre-ribosomal subunits export to the cytoplasm. {ECO:0000250}.Q9BWM7SFXN3Sideroflexin-3rSUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|Ref.4}; Multi-pass membrane protein {ECO:0000269|Ref.4}.!iron ion homeostasis [GO:0055072]%FUNCTION: Potential iron transporter.Q6SZW1SARM10Sterile alpha and TIR motif-containing protein 1SUBCELLULAR LOCATION: Cytoplasm. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Mitochondrion. Note=Associated with microtubules. {ECO:0000250}.innate immune response [GO:0045087]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; regulation of apoptotic process [GO:0042981]; regulation of dendrite morphogenesis [GO:0048814]; regulation of neuron death [GO:1901214]; response to glucose [GO:0009749]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]axon [GO:0030424]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; extrinsic component of mitochondrial outer membrane [GO:0031315]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; synapse [GO:0045202]FUNCTION: Negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway which plays a pivotal role in activating axonal degeneration following injury. Promotes Wallerian degeneration an injury-induced axonal death pathway which involves degeneration of an axon distal to the injury site. Can activate neuronal death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway. Involved in innate immune response. Inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38. {ECO:0000269|PubMed:15123841, ECO:0000269|PubMed:16964262, ECO:0000269|PubMed:16985498, ECO:0000269|PubMed:20306472}.O15213WDR46WD repeat-containing protein 46GSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:23848194}.maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; positive regulation of protein targeting to mitochondrion [GO:1903955][90S preribosome [GO:0030686]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040]FUNCTION: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus. {ECO:0000269|PubMed:23848194}.Q9UBP9GULP12PTB domain-containing engulfment adapter protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16497666}. Note=May associate with the cytoplasmic side of the plasma membrane and early endosomes.apoptotic process [GO:0006915]; lipid transport [GO:0006869]; phagocytosis, engulfment [GO:0006911]; signal transduction [GO:0007165]FUNCTION: May function as an adapter protein. Required for efficient phagocytosis of apoptotic cells. Modulates cellular glycosphingolipid and cholesterol transport. May play a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increases cellular levels of GTP-bound ARF6. {ECO:0000269|PubMed:10574763, ECO:0000269|PubMed:10574771, ECO:0000269|PubMed:16497666, ECO:0000269|PubMed:17398097}.Q86WB0NIPA"Nuclear-interacting partner of ALK<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12748172}.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; protein ubiquitination [GO:0016567]3nuclear membrane [GO:0031965]; nucleus [GO:0005634]FUNCTION: Essential component of an SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events. {ECO:0000269|PubMed:16009132}.P43378PTN90Tyrosine-protein phosphatase non-receptor type 9|non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein tyrosine phosphatase activity [GO:0004725]FUNCTION: Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus. {ECO:0000269|PubMed:19167335}.Q9Y2G3AT11B,Probable phospholipid-transporting ATPase IF;SUBCELLULAR LOCATION: Recycling endosome membrane; Multi-pass membrane protein. Early endosome. Endoplasmic reticulum. Golgi apparatus, trans-Golgi network. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, mainly located < in recycling endosomes.aminophospholipid transport [GO:0015917]; ion transmembrane transport [GO:0034220]; ion transport [GO:0006811]; phospholipid translocation [GO:0045332]; transmembrane transport [GO:0055085]ATP binding [GO:0005524]; ion transmembrane transporter activity [GO:0015075]; magnesium ion binding [GO:0000287]; phospholipid-translocating ATPase activity [GO:0004012]/early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]QFUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). Involved in regulation of sensitivity to cisplatin; may contribute to secretory vesicle transport of cisplatin from Golgi to plasma membrane. {ECO:0000269|PubMed:23585472, ECO:0000305}.Q14956GPNMBTransmembrane glycoprotein NMB4SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Detected at the cell surface in different types of cancers cells, including glioblastoma multiforme cells and most melanoma cell lines.bone mineralization [GO:0030282]; cell adhesion [GO:0007155]; negative regulation of cell proliferation [GO:0008285]; negative regulation of tumor necrosis factor production [GO:0032720]; osteoblast differentiation [GO:0001649]xintegral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]7FUNCTION: Could be a melanogenic enzyme. {ECO:0000250}.P18084ITB5Integrin beta-5antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cell-matrix adhesion [GO:0007160]; endodermal cell differentiation [GO:0035987]; epithelial cell-cell adhesion [GO:0090136]; extracellular matrix organization [GO:0030198]; integrin-mediated signaling pathway [GO:0007229]; muscle contraction [GO:0006936]; stress fiber assembly [GO:0043149]; transforming growth factor beta receptor signaling pathway [GO:0007179]cell leading edge [GO:0031252]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integrin alphav-beta5 complex [GO:0034684]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]~FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.Q9NSD4ZN275Zinc finger protein 275Q6STE5SMRD3]SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14701856}. cardiac right ventricle formation [GO:0003219]; cellular lipid metabolic process [GO:0044255]; chromatin remodeling [GO:0006338]; muscle cell differentiation [GO:0042692]; neural retina development [GO:0003407]; nucleosome disassembly [GO:0006337]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of protein binding [GO:0043393]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; secondary heart field specification [GO:0003139]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]Schromatin binding [GO:0003682]; ligand-dependent nuclear receptor binding [GO:0016922]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; nuclear hormone receptor binding [GO:0035257]; receptor binding [GO:0005102]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]FUNCTION: Plays a role in ATP dependent nucleosome remodeling by SMARCA4 containing complexes. Stimulates nuclear receptor mediated transcription. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). {ECO:0000250}.Q5T3I0GPTC4#G patch domain-containing protein 4Q6IQ22RAB12Ras-related protein Rab-123SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Lysosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.autophagy [GO:0006914]; cellular protein catabolic process [GO:0044257]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; positive regulation of macroautophagy [GO:0016239]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of exocytosis [GO:0017157]; vesicle docking involved in exocytosis [GO:0006904]autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; recycling endosome membrane [GO:0055038]UFUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity). {ECO:0000250}.P39748FEN1Flap endonuclease 1SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.; SUBCELLULAR LOCATION: Isoform FENMIT: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:23675412}.abase-excision repair [GO:0006284]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication, removal of RNA primer [GO:0043137]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; memory [GO:0007613]; mitotic cell cycle [GO:0000278]; nucleic acid phosphodiester bond hydrolysis [< GO:0090305]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; UV protection [GO:0009650]5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; double-stranded DNA exodeoxyribonuclease activity [GO:0008309]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; RNA-DNA hybrid ribonuclease activity [GO:0004523]membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]TFUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741, ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037, ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:7961795, ECO:0000269|PubMed:8621570}.Q9Y3M2CBY1Protein chibby homolog 1SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16424001}. Golgi apparatus, trans-Golgi network. Note=Nuclear, in a punctate manner. Also found in the trans-Golgi.cardiac muscle cell differentiation [GO:0055007]; fat cell differentiation [GO:0045444]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of Wnt signaling pathway [GO:0030178]; protein localization [GO:0008104]Ibeta-catenin binding [GO:0008013]; identical protein binding [GO:0042802]cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; trans-Golgi network [GO:0005802]FUNCTION: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation. {ECO:0000269|PubMed:12712206, ECO:0000269|PubMed:15194699}.P15336ATF2/Cyclic AMP-dependent transcription factor ATF-27SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion outer membrane. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-52 is required for its nuclear localization and negatively regulates its mitochondrial localization. Co-localizes with the MRN complex in the IR-induced foci (IRIF).adipose tissue development [GO:0060612]; cellular response to DNA damage stimulus [GO:0006974]; chromatin organization [GO:0006325]; fat cell differentiation [GO:0045444]; histone acetylation [GO:0016573]; innate immune response [GO:0045087]; intra-S DNA damage checkpoint [GO:0031573]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; outflow tract morphogenesis [GO:0003151]; positive regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902110]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta2 production [GO:0032915]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to osmotic stress [GO:0006970]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription from RNA polymerase II promoter [GO:0006366]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]cAMP response element binding [GO:0035497]; cAMP response element binding protein binding [GO:0008140]; chromatin binding [GO:0003682]; enhancer sequence-specific DNA binding [GO:0001158]; histone acetyltransferase activity [GO:0004402]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; RNA polymerase II activating transcription factor binding [GO:0001102]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription factor binding transcription factor activity [GO:0001076]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]FUNCTION: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cel< l type. {ECO:0000269|PubMed:10821277, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:22304920}.Q9BYK8HELZ2"Helicase with zinc finger domain 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}.cellular lipid metabolic process [GO:0044255]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]/membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Helicase that acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. {ECO:0000269|PubMed:16239304, ECO:0000269|PubMed:23525231}.Q5HYJ3FA76BProtein FAM76BDSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19266028}."protein deneddylation [GO:0000338]-NEDD8-specific protease activity [GO:0019784]cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q06787FMR1&Fragile X mental retardation protein 1central nervous system development [GO:0007417]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation [GO:0045947]'cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; dendrite [GO:0030425]; membrane [GO:0016020]; mRNA cap binding complex [GO:0005845]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; polysome [GO:0005844]JFUNCTION: Translation repressor. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression (By similarity). RNA-binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C). {ECO:0000250}.O75369FLNB Filamin-BSUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=In differentiating myotubes, isoform 1, isoform 2 and isoform 3 are localized diffusely throughout the cytoplasm with regions of enrichment at the longitudinal actin stress fiber. In differentiated tubes, isoform 1 is also detected within the Z-lines.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton. Note=Predominantly localized at actin stress fibers.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton. Note=Predominantly localized at actin stress fibers.; SUBCELLULAR LOCATION: Isoform 6: Cytoplasm, cytoskeleton. Note=Polarized at the periphery of myotubes.<actin cytoskeleton organization [GO:0030036]; cytokine-mediated signaling pathway [GO:0019221]; cytoskeletal anchoring at plasma membrane [GO:0007016]; epithelial cell morphogenesis [GO:0003382]; keratinocyte development [GO:0003334]; signal transduction [GO:0007165]; skeletal muscle tissue development [GO:0007519]dactin binding [GO:0003779]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]>actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; Z disc [GO:0030018]FUNCTION: Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.Q6YP21KAT3'Kynurenine--oxoglutarate transaminase 3q2-oxoglutarate metabolic process [GO:0006103]; biosynthetic process [GO:0009058]; cellular amino acid metabolic process [GO:0006520]; cellular nitrogen compound metabolic process [GO:0034641]; kynurenine metabolic process [GO:0070189]; L-kynurenine metabolic process [GO:0097052]; small molecule metabolic process [GO:0044281]; tryptophan catabolic process [GO:0006569]cysteine-S-conjugate beta-lyase activity [GO:0047804]; kynurenine-glyoxylate transaminase activity [GO:0047315]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; poly(A) RNA binding [GO:0044822]; pyridoxal phosphate binding [GO:0030170]HFUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) (By similarity). {ECO:0000250}.Q7Z2T5TRM1LTRMT1-like protein3behavior [GO:0007610]; tRNA processing [GO:0008033]metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; poly(A) RNA binding [GO:0044822]; tRNA binding [GO:0000049]XFUNCTION: May play a role in motor coordination and exploratory behavior. {ECO:0000250}.Q13287NMIN-myc-interactorinflammatory response [GO:0006954]; JAK-STAT cascade [GO:0007259]; negative regulation of innate immune response [GO:0045824]; negative regulation of interferon-alpha biosynthetic process [GO:0045355]; negative regulation of interferon-beta biosynthetic process [GO:0045358]; positive regulation of protein K48-linked ubiquitination [GO:1902524]; regulation of nucleic acid-templated transcription [GO:1903506]; transcription from RNA polymerase II promoter [GO:0006366],transcription cofactor activity [GO:0003712]FUNCTION: May be involved in augmenting coactivator protein recruitment to a group of sequence-specific transcription factors. Augments cytokine-mediated STAT transcription. Enhances CBP/p300 coactivator protein recruitment to STAT1 and STAT5.Q9NZJ5E2AK39Eukaryotic translation initiation factor 2-alpha kinase 3activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; angiogenesis [GO:0001525]; bone mineralization [GO:0030282]; calcium-mediated signaling [GO:0019722]; cellular protein metabolic process [GO:0044267]; cellular response to glucose starvation [GO:0042149]; chondrocyte development [GO:0002063]; eiF2alpha phosphorylation in response to endoplasmic reticulum stress [GO:0036492]; endocrine pancreas development [GO:0031018]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; fat cell differentiation [GO:0045444]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin secretion [GO:0030073]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; lactation [GO:0007595]; negative regulation of apoptotic process [GO:0043066]; negative regulation of myelination [GO:0031642]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation in response to stress [GO:0032057]; ossification [GO:0001503]; peptidyl-serine phosphorylation [GO:0018105]; PERK-mediated unfolded protein response [GO:0036499]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of ge< ne expression [GO:0010628]; positive regulation of protein binding [GO:0032092]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transcription from RNA polymerase I promoter [GO:0045943]; positive regulation of vascular endothelial growth factor production [GO:0010575]; protein autophosphorylation [GO:0046777]; protein homooligomerization [GO:0051260]; protein phosphorylation [GO:0006468]; regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902235]; regulation of fatty acid metabolic process [GO:0019217]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]; response to endoplasmic reticulum stress [GO:0034976]; skeletal system development [GO:0001501]; SREBP signaling pathway [GO:0032933]; translation [GO:0006412]bATP binding [GO:0005524]; enzyme binding [GO:0019899]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; membrane [GO:0016020]FUNCTION: Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function (By similarity). {ECO:0000250}.Q13085ACACAAcetyl-CoA carboxylase 1Macetyl-CoA metabolic process [GO:0006084]; biotin metabolic process [GO:0006768]; carnitine shuttle [GO:0006853]; cellular lipid metabolic process [GO:0044255]; cellular response to prostaglandin E stimulus [GO:0071380]; energy reserve metabolic process [GO:0006112]; fatty acid biosynthetic process [GO:0006633]; lipid homeostasis [GO:0055088]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; malonyl-CoA biosynthetic process [GO:2001295]; multicellular organismal protein metabolic process [GO:0044268]; positive regulation of cellular metabolic process [GO:0031325]; protein homotetramerization [GO:0051289]; small molecule metabolic process [GO:0044281]; tissue homeostasis [GO:0001894]; triglyceride biosynthetic process [GO:0019432]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin carboxylase activity [GO:0004075]; metal ion binding [GO:0046872]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. {ECO:0000269|PubMed:20952656}.Q8IXL6DMP44Extracellular serine/threonine protein kinase FAM20CmSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26091039}. Golgi apparatus {ECO:0000250|UniProtKB:Q5MJS3}.biomineral tissue development [GO:0031214]; dentinogenesis [GO:0097187]; enamel mineralization [GO:0070166]; odontoblast differentiation [GO:0071895]; osteoclast maturation [GO:0036179]; positive regulation of bone mineralization [GO:0030501]; positive regulation of osteoblast differentiation [GO:0045669]; protein phosphorylation [GO:0006468]; regulation of fibroblast growth factor receptor signaling pathway [GO:0040036]; regulation of phosphorus metabolic process [GO:0051174]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; manganese ion binding [GO:0030145]; protein serine/threonine kinase activity [GO:0004674]bextracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth (PubMed:22582013, PubMed:23754375, PubMed:25789606). Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome (PubMed:26091039). Mainly phosphorylates proteins within the Ser-x-Glu/pSer motif, but also displays a broader substrate specificity (PubMed:26091039). Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1 (PubMed:22582013, PubMed:25789606). In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion (PubMed:26091039). {ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606, ECO:0000269|PubMed:26091039}.Q5THK1PR14LProtein PRR14LQ9NVF9EKI2Ethanolamine kinase 2rglycerophospholipid biosynthetic process [GO:0046474]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid metabolic process [GO:0006644]; placenta development [GO:0001890]; post-embryonic development [GO:0009791]; small molecule metabolic process [GO:0044281]CATP binding [GO:0005524]; ethanolamine kinase activity [GO:0004305]FUNCTION: Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity (By similarity). {ECO:0000250}.Q7Z2Y5NRKNik-related protein kinaseactin cytoskeleton reorganization [GO:0031532]; activation of JNKK activity [GO:0007256]; activation of protein kinase activity [GO:0032147]; MAPK cascade [GO:0000165]; negative regulation of cell proliferation [GO:0008285]; neuron projection morphogenesis [GO:0048812]; parturition [GO:0007567]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; regulation of spongiotrophoblast cell proliferation [GO:0060721]; stress-activated protein kinase signaling cascade [GO:0031098]FUNCTION: May phosphorylate cofilin-1 and induce actin polymerization through this process, during the late stages of embryogenesis. Involved in the TNF-alpha-induced signaling pathway (By similarity). {ECO:0000250}.Q99856ARI3A0AT-rich interactive domain-containing protein 3ASUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:17400556}. Cytoplasm {ECO:0000269|PubMed:17400556}. Note=Shuttles between nucleus and cytoplasm.chromatin binding [GO:0003682]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation. {ECO:0000269|PubMed:11812999, ECO:0000269|PubMed:12692263}.Q9Y6M1IF2B23Insulin-like growth factor 2 mRNA-binding protein 2SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules.anatomical structure morphogenesis [GO:0009653]; gene expression [GO:0010467]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; regulation of cytokine biosynthetic process [GO:0042035]mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; translation regulator activity [GO:0045182]]cytoplasm [GO:00057< 37]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]\FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts. {ECO:0000250, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9891060}.O95243MBD4#Methyl-CpG-binding domain protein 4base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; depyrimidination [GO:0045008]; DNA repair [GO:0006281]; response to estradiol [GO:0032355]; response to radiation [GO:0009314]endodeoxyribonuclease activity [GO:0004520]; pyrimidine-specific mismatch base pair DNA N-glycosylase activity [GO:0008263]; satellite DNA binding [GO:0003696]Fchromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]zFUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein. {ECO:0000269|PubMed:10097147, ECO:0000269|PubMed:10930409}.Q8N884CGASCyclic GMP-AMP synthaseGSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23258413}.oactivation of innate immune response [GO:0002218]; cellular response to exogenous dsRNA [GO:0071360]; cyclic nucleotide biosynthetic process [GO:0009190]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of type I interferon production [GO:0032481]ATP binding [GO:0005524]; cyclic-GMP-AMP synthase activity [GO:0061501]; DNA binding [GO:0003677]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p]. Has antiviral activity by acting as a key cytosolic DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production. {ECO:0000269|PubMed:21478870, ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722159, ECO:0000269|PubMed:24116191, ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:25131990}.P52926HMGA2"High mobility group protein HMGI-C base-excision repair [GO:0006284]; cell division [GO:0051301]; chondrocyte differentiation [GO:0002062]; chondrocyte proliferation [GO:0035988]; chromatin organization [GO:0006325]; chromosome breakage [GO:0031052]; chromosome condensation [GO:0030261]; DNA damage response, detection of DNA damage [GO:0042769]; endodermal cell differentiation [GO:0035987]; epithelial to mesenchymal transition [GO:0001837]; fat cell differentiation [GO:0045444]; heterochromatin assembly [GO:0031507]; histone H2A-S139 phosphorylation [GO:0035978]; mesenchymal cell differentiation [GO:0048762]; mesodermal cell differentiation [GO:0048333]; mesodermal-endodermal cell signaling [GO:0003131]; mitotic G2 DNA damage checkpoint [GO:0007095]; mitotic nuclear division [GO:0007067]; multicellular organismal development [GO:0007275]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA binding [GO:0043392]; negative regulation of double-strand break repair via nonhomologous end joining [GO:2001033]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; oncogene-induced cell senescence [GO:0090402]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of cellular response to X-ray [GO:2000685]; positive regulation of cellular senescence [GO:2000774]; positive regulation of gene expression [GO:0010628]; positive regulation of response to DNA damage stimulus [GO:2001022]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; regulation of cell cycle process [GO:0010564]; regulation of cellular response to drug [GO:2001038]; regulation of growth [GO:0040008]; regulation of stem cell maintenance [GO:2000036]; regulation of transcription, DNA-templated [GO:0006355]; response to virus [GO:0009615]; senescence-associated heterochromatin focus assembly [GO:0035986]; stem cell differentiation [GO:0048863]; transcription from RNA polymerase II promoter [GO:0006366]5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; AT DNA binding [GO:0003680]; C2H2 zinc finger domain binding [GO:0070742]; cAMP response element binding [GO:0035497]; core promoter binding [GO:0001047]; DNA-(apurinic or apyrimidinic site) lyase activity [GO:0003906]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; DNA-dependent protein kinase activity [GO:0004677]; MH1 domain binding [GO:0035501]; MH2 domain binding [GO:0035500]; nucleosomal DNA binding [GO:0031492]; regulatory region DNA binding [GO:0000975]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; SMAD binding [GO:0046332]; transcription factor binding [GO:0008134]nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; senescence-associated heterochromatin focus [GO:0035985]; SMAD protein complex [GO:0071141]FUNCTION: Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. {ECO:0000269|PubMed:14645522}.Q8IY63AMOL1Angiomotin-like protein 1BSUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.establishment of cell polarity involved in ameboidal cell migration [GO:0003365]; hippo signaling [GO:0035329]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; Wnt signaling pathway [GO:0016055]apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lamellipodium [GO:0030027]FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. {ECO:0000269|PubMed:22362771}.Q5QJE6TDIF2:Deoxynucleotidyltransferase terminal-interacting protein 2YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein. {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.O75815BCAR30Breast cancer anti-estrogen resistance protein 3lens morph< ogenesis in camera-type eye [GO:0002089]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; response to drug [GO:0042493]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]dFUNCTION: May act as an adapter protein and couple activated growth factor receptors to a signaling pathway that regulates the proliferation in breast cancer cells. When overexpressed, it confers anti-estrogen resistance in breast cancer cell lines. May also be regulated by cellular adhesion to extracellular matrix proteins. {ECO:0000269|PubMed:9582273}.Q8TDN6BRX1(Ribosome biogenesis protein BRX1 homolog?FUNCTION: Required for biogenesis of the 60S ribosomal subunit.Q9BZL6KPCD2"Serine/threonine-protein kinase D2SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Nucleus. Golgi apparatus, trans-Golgi network. Note=Translocation to the cell membrane is required for kinase activation (By similarity). Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import. {ECO:0000250}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; cell death [GO:0008219]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; endothelial tube morphogenesis [GO:0061154]; intracellular signal transduction [GO:0035556]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell adhesion [GO:0045785]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [GO:0038033]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of histone deacetylase activity [GO:1901727]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of T cell receptor signaling pathway [GO:0050862]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; protein autophosphorylation [GO:0046777]; protein kinase D signaling [GO:0089700]; protein phosphorylation [GO:0006468]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]= FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. In response to oxidative stress, is phosphorylated at Tyr-438 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B. In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77. Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens. In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway. During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane. Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis. In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN. Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells. Plays a regulatory role in angiogenesis and tumor growth by phosphorylating a downstream mediator CIB1 isoform 2, resulting in vascular endothelial growth factor A (VEGFA) secretion. {ECO:0000269|PubMed:14743217, ECO:0000269|PubMed:15604256, ECO:0000269|PubMed:16928771, ECO:0000269|PubMed:17077180, ECO:0000269|PubMed:17951978, ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:18262756, ECO:0000269|PubMed:19001381, ECO:0000269|PubMed:19192391, ECO:0000269|PubMed:23503467}.Q8N806UBR7)Putative E3 ubiquitin-protein ligase UBR7*FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.Q8N3E9PLCD3A1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow. Note=Localizes at the cleavage furrow during cytokinesis.:angiogenesis [GO:0001525]; inositol phosphate metabolic process [GO:0043647]; intracellular signal transduction [GO:0035556]; labyrinthine layer blood vessel development [GO:0060716]; lipid catabolic process [GO:0016042]; regulation of cell proliferation [GO:0042127]; small molecule metabolic process [GO:0044281]metal ion binding [GO:0046872]; phosphatidylinositol phospholipase C activity [GO:0004435]; signal transducer activity [GO:0004871]Pcleavage furrow [GO:0032154]; cytosol [GO:0005829]; plasma membrane [GO:0005886]FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 re< leases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.Q96II8LRCH3ELeucine-rich repeat and calponin homology domain-containing protein 3P43234CATO Cathepsin Oaproteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]7extracellular space [GO:0005615]; lysosome [GO:0005764]cFUNCTION: Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover.Q8TBZ3WDR20WD repeat-containing protein 20Q8IUG5MY18BUnconventional myosin-XVIIIbSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere. Note=Punctate pattern in undifferentiated myoblasts. Nuclear, on primary cardiomyocytes and adult muscle. A partial sarcomeric location was found in some cardiomyocytes.ucentrosome [GO:0005813]; nucleoplasm [GO:0005654]; sarcomere [GO:0030017]; unconventional myosin complex [GO:0016461]XFUNCTION: May be involved in intracellular trafficking of the muscle cell when in the cytoplasm, whereas entering the nucleus, may be involved in the regulation of muscle specific genes. May play a role in the control of tumor development and progression; restored MYO18B expression in lung cancer cells suppresses anchorage-independent growth.O75354ENTP60Ectonucleoside triphosphate diphosphohydrolase 6SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. Secreted. Note=But also occurs in a soluble extracellular form.Lresponse to calcium ion [GO:0051592]; response to magnesium ion [GO:0032026]guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity [GO:0008894]; nucleoside-triphosphatase activity [GO:0017111]; uridine-diphosphatase activity [GO:0045134]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP (By similarity). {ECO:0000250}.Q9UBS0KS6B2"Ribosomal protein S6 kinase beta-2Cepidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of translational initiation [GO:0045948]; protein kinase B signaling [GO:0043491]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]; translation [GO:0006412]ATP binding [GO:0005524]; peptide binding [GO:0042277]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; ribosomal protein S6 kinase activity [GO:0004711];FUNCTION: Phosphorylates specifically ribosomal protein S6.Q14164IKKE:Inhibitor of nuclear factor kappa-B kinase subunit epsilonSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24882218}. Nucleus. Nucleus, PML body {ECO:0000269|PubMed:20188669}. Note=Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent (PubMed:20188669). Located diffusely throughout the cytoplasm but locates to punctate cytoplasmic bodies when coexpressed with TRIM6 (PubMed:24882218). {ECO:0000269|PubMed:20188669, ECO:0000269|PubMed:24882218}.immune response [GO:0006955]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of type I interferon production [GO:0032480]; NIK/NF-kappaB signaling [GO:0038061]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; protein phosphorylation [GO:0006468]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]oATP binding [GO:0005524]; IkappaB kinase activity [GO:0008384]; NF-kappaB-inducing kinase activity [GO:0004704]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; mitochondrial membrane [GO:0031966]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]FUNCTION: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1. {ECO:0000269|PubMed:17568778, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:19153231, ECO:0000269|PubMed:20188669, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:22532683, ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:23478265}.Q86WA9S2611,Sodium-independent sulfate anion transporterSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12626430}; Multi-pass membrane protein {ECO:0000269|PubMed:12626430}. Lysosome membrane; Multi-pass membrane protein {ECO:0000269|PubMed:12626430}.Janion transmembrane transport [GO:0098656]; sulfate transport [GO:0008272]anion:anion antiporter activity [GO:0015301]; anion transmembrane transporter activity [GO:0008509]; secondary active sulfate transmembrane transporter activity [GO:0008271]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]FUNCTION: Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC). {ECO:0000269|PubMed:12626430}.Q9P266JCAD:Junctional protein associated with coronary artery diseaseSUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}. Note=Colocalizes with VE-Cadherin, in endothelial cells but not in epithelial cells. {ECO:< 0000250}.?adherens junction [GO:0005912]; cell-cell junction [GO:0005911]P49643PRI2DNA primase large subunitDNA replication, synthesis of RNA primer [GO:0006269]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA primase activity [GO:0003896]; metal ion binding [GO:0046872]8nucleoplasm [GO:0005654]; primosome complex [GO:1990077]FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.O43639NCK2Cytoplasmic protein NCK2sSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16835242}. Endoplasmic reticulum {ECO:0000269|PubMed:16835242}.actin filament organization [GO:0007015]; axon guidance [GO:0007411]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; immunological synapse formation [GO:0001771]; lamellipodium assembly [GO:0030032]; negative regulation of cell proliferation [GO:0008285]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress [GO:1990441]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; regulation of epidermal growth factor-activated receptor activity [GO:0007176]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]cytoskeletal adaptor activity [GO:0008093]; receptor signaling complex scaffold activity [GO:0030159]; SH3/SH2 adaptor activity [GO:0005070]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; neuronal postsynaptic density [GO:0097481]; vesicle membrane [GO:0012506]uFUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:16835242}.Q9H0L4CSTFT1Cleavage stimulation factor subunit 2 tau variantFUNCTION: May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs (By similarity). {ECO:0000250}.Q96RT1LAP2 Protein LAP2)SUBCELLULAR LOCATION: Cell junction, hemidesmosome {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus membrane {ECO:0000250}. Basolateral cell membrane {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250}.?basal protein localization [GO:0045175]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell growth [GO:0016049]; cellular response to tumor necrosis factor [GO:0071356]; epidermal growth factor receptor signaling pathway [GO:0007173]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; integrin-mediated signaling pathway [GO:0007229]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070433]; positive regulation of gene expression [GO:0010628]; protein targeting [GO:0006605]; response to lipopolysaccharide [GO:0032496]; response to muramyl dipeptide [GO:0032495]; signal transduction [GO:0007165]ErbB-2 class receptor binding [GO:0005176]; integrin binding [GO:0005178]; receptor binding [GO:0005102]; structural constituent of cytoskeleton [GO:0005200])basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; hemidesmosome [GO:0030056]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]qFUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.A7E2V4ZSWM8,Zinc finger SWIM domain-containing protein 8Q13428TCOFTreacle proteinGSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12777385}.skeletal system development [GO:0001501]; transcription of nuclear large rRNA transcript from RNA polymerase I promoter [GO:0042790]Cpoly(A) RNA binding [GO:0044822]; transporter activity [GO:0005215](FUNCTION: May be involved in nucleolar-cytoplasmic transport. May play a fundamental role in early embryonic development, particularly in development of the craniofacial complex (By similarity). May participate in certain stages of ribosome biogenesis. {ECO:0000250, ECO:0000269|PubMed:12777385}.Q9NWM8FKB14*Peptidyl-prolyl cis-trans isomerase FKBP14vSUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:22265013}.cellular protein metabolic process [GO:0044267]; chaperone-mediated protein folding [GO:0061077]; endoplasmic reticulum unfolded protein response [GO:0030968]; IRE1-mediated unfolded protein response [GO:0036498]; protein peptidyl-prolyl isomerization [GO:0000413]P49916DNLI3 DNA ligase 3SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}. Note=Contains an N-terminal mitochondrial transit peptide. {ECO:0000269|PubMed:10207110}.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion {ECO:0000305|PubMed:10207110}. Note=Contains an N-terminal mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.; SUBCELLULAR LOCATION: Isoform 3: Nucleus {ECO:0000269|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial transit peptide. {ECO:0000269|PubMed:10207110}.; SUBCELLULAR LOCATION: Isoform 4: Nucleus {ECO:0000305|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.base-excision repair [GO:0006284]; base-excision repair, DNA ligation [GO:0006288]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA ligation [GO:0006266]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; double-strand break repair [GO:0006302]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; double-strand break repair via nonhomologous end joining [GO:0006303]; mitochondrial DNA repair [GO:0043504]; mitochondrion organization [GO:0007005]; negative regulation of DNA recombination [GO:0045910]; negative regulation of mitochondrial DNA replication [GO:0090298]ATP binding [GO:0005524]; DNA binding [< GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA ligase activity [GO:0003909]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; DNA ligase III-XRCC1 complex [GO:0070421]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]FUNCTION: Isoform 3 functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as DNA ligase in mitochondrial base-excision DNA repair (PubMed:10207110, PubMed:24674627). {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.A6ND36FA83GProtein FAM83GSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24554596}. Nucleus {ECO:0000269|PubMed:24554596}. Note=Detected predominantly in cytosolic. Upon BMP stimulation, a small portion of PAWS1 is detected in the nucleus. {ECO:0000269|PubMed:24554596}."BMP signaling pathway [GO:0030509]dFUNCTION: May regulate the bone morphogenetic proteins (BMP) pathway. {ECO:0000269|PubMed:24554596}.P40938RFC3Replication factor C subunit 3@base-excision repair [GO:0006284]; DNA damage response, detection of DNA damage [GO:0042769]; DNA-dependent DNA replication [GO:0006261]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA synthesis involved in DNA repair [GO:0000731]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; response to organophosphorus [GO:0046683]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]&DNA clamp loader activity [GO:0003689]FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1.Q7Z3K3POGZ)Pogo transposable element with ZNF domainSUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasm. Note=According to some authors, it is not localized to mitotic chromatin (PubMed:19244240). Recruited to trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000269|PubMed:19244240}.mcell division [GO:0051301]; kinetochore assembly [GO:0051382]; mitotic sister chromatid cohesion [GO:0007064]fcytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]eFUNCTION: Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. {ECO:0000269|PubMed:20562864}.P17019ZN708Zinc finger protein 708zmetal ion binding [GO:0046872]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]Q9UKU9ANGL2Angiopoietin-related protein 2[FUNCTION: Induces sprouting in endothelial cells through an autocrine and paracrine action.P22413ENPP1@Ectonucleotide pyrophosphatase/phosphodiesterase family member 1SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted {ECO:0000250}. Note=The proteolytically processed form is secreted (By similarity). Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side. {ECO:0000250}.3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; biomineral tissue development [GO:0031214]; bone remodeling [GO:0046849]; cellular phosphate ion homeostasis [GO:0030643]; cellular response to insulin stimulus [GO:0032869]; generation of precursor metabolites and energy [GO:0006091]; immune response [GO:0006955]; inorganic diphosphate transport [GO:0030505]; negative regulation of cell growth [GO:0030308]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of glucose import [GO:0046325]; negative regulation of glycogen biosynthetic process [GO:0045719]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of ossification [GO:0030279]; negative regulation of protein autophosphorylation [GO:0031953]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; nucleoside triphosphate catabolic process [GO:0009143]; phosphate-containing compound metabolic process [GO:0006796]; regulation of bone mineralization [GO:0030500]; riboflavin metabolic process [GO:0006771]; sequestering of triglyceride [GO:0030730]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]"3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; insulin receptor binding [GO:0005158]; NADH pyrophosphatase activity [GO:0035529]; nucleic acid binding [GO:0003676]; nucleoside-triphosphate diphosphatase activity [GO:0047429]; nucleotide diphosphatase activity [GO:0004551]; phosphodiesterase I activity [GO:0004528]; polysaccharide binding [GO:0030247]; protein homodimerization activity [GO:0042803]; scavenger receptor activity [GO:0005044]; zinc ion binding [GO:0008270]basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]!FUNCTION: By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function. {ECO:0000269|PubMed:10615944, ECO:0000269|PubMed:8001561}.P49585PCY1A(Choline-phosphate cytidylyltransferase ASUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form. {ECO:0000250}.CDP-choline pathway [GO:0006657]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]Xcholine-phosphate cytidylyltransferase activity [GO:0004105]; lipid binding [GO:0008289]`cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; glycogen granule [GO:0042587]1FUNCTION: Controls phosphatidylcholine synthesis.O95571ETHE1+Persulfide dioxygenase ETHE1, mitochondrialSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion matrix. Note=According to PubMed:12398897, it is cytoplasmic and nuclear. According to PubMed:14732903, it is found in the mitochondrial matrix.ocellular nitrogen compound metabolic process [GO:0034641]; glutathione metabolic process [GO:0006749]; hydrogen sulfide metabolic process [GO:0070813]; small molecule metabolic process [GO:0044281]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]; sulfur amino acid cata< bolic process [GO:0000098]; sulfur amino acid metabolic process [GO:0000096]Giron ion binding [GO:0005506]; sulfur dioxygenase activity [GO:0050313]FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897). {ECO:0000269|PubMed:12398897, ECO:0000269|PubMed:14732903, ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459}.Q96BN8OTULUbiquitin thioesterase otulin>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23746843}.canonical Wnt signaling pathway [GO:0060070]; innate immune response [GO:0045087]; negative regulation of inflammatory response [GO:0050728]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; protein linear deubiquitination [GO:1990108]; sprouting angiogenesis [GO:0002040]`cysteine-type peptidase activity [GO:0008234]; ubiquitin-specific protease activity [GO:0004843]2cytoplasm [GO:0005737]; LUBAC complex [GO:0071797]mFUNCTION: Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Associates with the LUBAC complex via direct interaction with RNF31 and counteracts its action by cleaving linear polyubiquitin chains to substrates. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by counteracting activity of the LUBAC complex. Plays a key role in innate immune response: required to restrict linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling. {ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:23746843, ECO:0000269|PubMed:23806334, ECO:0000269|PubMed:23827681}.Q9UKG1DP13A DCC-interacting protein 13-alphaAPPL1SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane protein. Nucleus. Note=Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF.apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell proliferation [GO:0008283]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; insulin receptor signaling pathway [GO:0008286]; programmed cell death [GO:0012501]; regulation of establishment of protein localization to plasma membrane [GO:0090003]; regulation of glucose import [GO:0046324]; signal transduction [GO:0007165]Midentical protein binding [GO:0042802]; protein kinase B binding [GO:0043422]cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; vesicle membrane [GO:0012506]FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. {ECO:0000269|PubMed:10490823, ECO:0000269|PubMed:15016378}.P35221CTNA1Catenin alpha-1SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000269|PubMed:21708131}; Peripheral membrane protein {ECO:0000269|PubMed:21708131}; Cytoplasmic side {ECO:0000269|PubMed:21708131}.actin filament organization [GO:0007015]; adherens junction organization [GO:0034332]; aging [GO:0007568]; apical junction assembly [GO:0043297]; axon regeneration [GO:0031103]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cellular protein localization [GO:0034613]; cellular response to indole-3-methanol [GO:0071681]; epithelial cell-cell adhesion [GO:0090136]; establishment or maintenance of cell polarity [GO:0007163]; gap junction assembly [GO:0016264]; male gonad development [GO:0008584]; muscle cell differentiation [GO:0042692]; negative regulation of cell motility [GO:2000146]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of integrin-mediated signaling pathway [GO:2001045]; negative regulation of neuroblast proliferation [GO:0007406]; odontogenesis of dentin-containing tooth [GO:0042475]; ovarian follicle development [GO:0001541]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of smoothened signaling pathway [GO:0045880]; protein heterooligomerization [GO:0051291]; response to estrogen [GO:0043627]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; gamma-catenin binding [GO:0045295]; poly(A) RNA binding [GO:0044822]; structural molecule activity [GO:0005198]; vinculin binding [GO:0017166])acrosomal vesicle [GO:0001669]; actin cytoskeleton [GO:0015629]; catenin complex [GO:0016342]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; plasma membrane [GO:0005886]; zonula adherens [GO:0005915]FUNCTION: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.Q9HCE9ANO8 Anoctamin-8SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane.Fintracellular calcium activated chloride channel activity [GO:0005229]NFUNCTION: Does not exhibit calcium-activated chloride channel (CaCC) activity.Q96GA7SDSLSerine dehydratase-likeQL-serine catabolic process [GO:0006565]; threonine catabolic process [GO:0006567]L-serine ammonia-lyase activity [GO:0003941]; L-threonine ammonia-lyase activity [GO:0004794]; pyridoxal phosphate binding [GO:0030170]HFUNCTION: Has low serine dehydratase and threonine dehydratase activity.P52294IMA5Importin subunit alpha-5apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0< 006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cytokine-mediated signaling pathway [GO:0019221]; intracellular transport of virus [GO:0075733]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of protein import into nucleus [GO:0042307]; programmed cell death [GO:0012501]; regulation of DNA recombination [GO:0000018]; viral life cycle [GO:0019058]; viral process [GO:0016032]cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.Q9NXA8SIR58NAD-dependent protein deacylase sirtuin-5, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion intermembrane space. Cytoplasm, cytosol. Nucleus. Note=Mainly mitochondrial. Also present extramitochondrially: a fraction is present in the cytosol and very small amounts are also detected in the nucleus.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000269|PubMed:21143562}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21143562}.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160, ECO:0000269|PubMed:21143562}.achromatin silencing [GO:0006342]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; peptidyl-lysine deglutarylation [GO:0061699]; peptidyl-lysine demalonylation [GO:0036047]; peptidyl-lysine desuccinylation [GO:0036049]; protein ADP-ribosylation [GO:0006471]; protein deacetylation [GO:0006476]; protein deglutarylation [GO:0061698]; protein demalonylation [GO:0036046]; protein desuccinylation [GO:0036048]; regulation of ketone biosynthetic process [GO:0010566]; response to nutrient levels [GO:0031667]NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ binding [GO:0070403]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; zinc ion binding [GO:0008270]cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]:FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000250|UniProtKB:Q8K2C6, ECO:0000269|PubMed:18680753, ECO:0000269|PubMed:21908771, ECO:0000269|PubMed:22076378, ECO:0000269|PubMed:24140062, ECO:0000269|PubMed:24703693}.Q8NBF6AVL9+Late secretory pathway protein AVL9 homologSUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:22595670}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.cell migration [GO:0016477]Lintegral component of membrane [GO:0016021]; recycling endosome [GO:0055037]EFUNCTION: Functions in cell migration. {ECO:0000269|PubMed:22595670}.Q9Y5K5UCHL50Ubiquitin carboxyl-terminal hydrolase isozyme L5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18922472}. Nucleus {ECO:0000269|PubMed:18922472}. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus.DNA recombination [GO:0006310]; DNA repair [GO:0006281]; forebrain morphogenesis [GO:0048853]; lateral ventricle development [GO:0021670]; midbrain development [GO:0030901]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; protein deubiquitination [GO:0016579]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ubiquitin-dependent protein catabolic process [GO:0006511]endopeptidase inhibitor activity [GO:0004866]; omega peptidase activity [GO:0008242]; poly(A) RNA binding [GO:0044822]; proteasome binding [GO:0070628]; ubiquitin-specific protease activity [GO:0004843]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Ino80 complex [GO:0031011]; nucleus [GO:0005634]; proteasome complex [GO:0000502]FUNCTION: Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1. {ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:18922472}.O95235KI20AKinesin-like protein KIF20AtSUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12939256}.(cell separation after cytokinesis [GO:0000920]; cytokinesis [GO:0000910]; microtubule-based movement [GO:0007018]; microtubule bundle formation [GO:0001578]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; microtubule motor activity [GO:0003777]; protein kinase binding [GO:0019901]; transporter activity [GO:0005215]Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; spindle [GO:0005819]FUNCTION: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}.Q13033STRN3 Striatin-3anegative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; response to estradiol [GO:0032355]armadillo repeat domain binding [GO:0070016]; calmodulin binding [GO:0005516]; protein complex binding [GO:0032403]; protein phosphat< ase 2A binding [GO:0051721]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytoplasm [GO:0005737]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein complex [GO:0043234]P50750CDK9Cyclin-dependent kinase 9<SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, PML body. Note=Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1-dependent. Associates with PML body when acetylated.cell proliferation [GO:0008283]; cellular response to cytokine stimulus [GO:0071345]; DNA repair [GO:0006281]; gene expression [GO:0010467]; negative regulation of cell cycle arrest [GO:0071157]; negative regulation of mRNA polyadenylation [GO:1900364]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of histone H2B ubiquitination [GO:2001168]; positive regulation of histone phosphorylation [GO:0033129]; positive regulation of mRNA 3'-UTR binding [GO:1903839]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of viral transcription [GO:0050434]; protein phosphorylation [GO:0006468]; regulation of DNA repair [GO:0006282]; regulation of histone modification [GO:0031056]; replication fork arrest [GO:0043111]; response to drug [GO:0042493]; transcription, DNA-templated [GO:0006351]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]^ATP binding [GO:0005524]; chromatin binding [GO:0003682]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; DNA binding [GO:0003677]; protein kinase activity [GO:0004672]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]; snRNA binding [GO:0017069]; transcription regulatory region DNA binding [GO:0044212] cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; PML body [GO:0016605]; positive transcription elongation factor complex b [GO:0008024]; transcription elongation factor complex [GO:0008023]F FUNCTION: Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:11884399, ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16109376, ECO:0000269|PubMed:16109377, ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18362169, ECO:0000269|PubMed:19575011, ECO:0000269|PubMed:19844166, ECO:0000269|PubMed:20081228, ECO:0000269|PubMed:20493174, ECO:0000269|PubMed:20930849, ECO:0000269|PubMed:20980437, ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:9857195}.Q9NWU2GID8-Glucose-induced degradation protein 8 homolog<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12559565}.4cell junction [GO:0030054]; nucleoplasm [GO:0005654]Q9C0B5ZDHC5Palmitoyltransferase ZDHHC5#protein palmitoylation [GO:0018345]wdendrite [GO:0030425]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Palmitoyl acyltransferase for the G-protein coupled receptor SSTR5. Also palmitoylates FLOT2 (By similarity). {ECO:0000250}.P54792DVLP1<Putative segment polarity protein dishevelled homolog DVL1P1rheart development [GO:0007507]; intracellular signal transduction [GO:0035556]; Wnt signaling pathway [GO:0016055]Q96R06SPAG5Sperm-associated antigen 5_SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic granule. Note=In a punctate pattern in interphase cells. During mitosis, detected at spindle poles during prophase, throughout the spindle in metaphase and anaphase, and at midzone microtubules in anaphase and telophase. Efficient targeting to the mitotic spindle may depend upon phosphorylation by GSK3B. Detected on kinetochores of chromosomes that have congressed. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends (By similarity). In non-mitotic non-stressed cells, shows a microtubuli pattern. In arsenite-stressed cells, accumulates in stress granules. {ECO:0000250}.cell division [GO:0051301]; chromosome segregation [GO:0007059]; establishment of spindle orientation [GO:0051294]; mitotic sister chromatid segregation [GO:0000070]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; spindle organization [GO:0007051]Ocondensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule organizing center [GO:0005815]; microtubule plus-end [GO:0035371]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]FUNCTION: Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes. In non-mitotic cells, upon stress induction, inhibits mammalian < target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis. May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU. {ECO:0000269|PubMed:11724960, ECO:0000269|PubMed:12356910, ECO:0000269|PubMed:17664331, ECO:0000269|PubMed:18055457, ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:23953116}.O75962TRIO Triple functional domain proteinapoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185]ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine/threonine kinase activity [GO:0004674]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]FUNCTION: Promotes the exchange of GDP by GTP. Together with leukocyte antigen-related (LAR) protein, it could play a role in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration and cell growth.P27540ARNT.Aryl hydrocarbon receptor nuclear translocatorUcell differentiation [GO:0030154]; cellular response to hypoxia [GO:0071456]; embryonic placenta development [GO:0001892]; mRNA transcription from RNA polymerase II promoter [GO:0042789]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of glycolytic process [GO:0045821]; positive regulation of hormone biosynthetic process [GO:0046886]; positive regulation of protein sumoylation [GO:0033235]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of vascular endothelial growth factor production [GO:0010575]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061418]; regulation of transcription from RNA polymerase II promoter in response to oxidative stress [GO:0043619]; response to hypoxia [GO:0001666]; transcription, DNA-templated [GO:0006351]Varyl hydrocarbon receptor activity [GO:0004874]; aryl hydrocarbon receptor binding [GO:0017162]; enhancer binding [GO:0035326]; protein heterodimerization activity [GO:0046982]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription factor complex [GO:0090575]FUNCTION: Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.P04156PRIOMajor prion proteinSUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19936054}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000269|PubMed:19936054}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:19059915}. Nucleus {ECO:0000269|PubMed:19059915}. Note=Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus. {ECO:0000269|PubMed:19059915}.Saxon guidance [GO:0007411]; cell cycle arrest [GO:0007050]; cellular copper ion homeostasis [GO:0006878]; cellular response to copper ion [GO:0071280]; cellular response to drug [GO:0035690]; learning or memory [GO:0007611]; metabolic process [GO:0008152]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of T cell receptor signaling pathway [GO:0050860]; protein homooligomerization [GO:0051260]; regulation of potassium ion transmembrane transport [GO:1901379]; regulation of protein localization [GO:0032880]; response to cadmium ion [GO:0046686]; response to oxidative stress [GO:0006979]copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; tubulin binding [GO:0015631]Banchored component of membrane [GO:0031225]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (PubMed:12732622, PubMed:19936054, PubMed:20564047). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). {ECO:0000250|UniProtKB:P04925, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:20564047, ECO:0000305}.Q8WXI4ACO11Acyl-coenzyme A thioesterase 11fatty acid metabolic process [GO:0006631]; intracellular signal transduction [GO:0035556]; response to cold [GO:0009409]; response to temperature stimulus [GO:0009266]vacyl-CoA hydrolase activity [GO:0047617]; carboxylic ester hydrolase activity [GO:0052689]; lipid binding [GO:0008289]qFUNCTION: Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.Q86W74ANR46+Ankyrin repeat domain-containing protein 46Q9H1E3NUCKSANuclear ubiquitous casein and cyclin-dependent kinase substrate 1Q8WWQ0PHIPPH-interacting proteincytoskeleton organization [GO:0007010]; insulin receptor signaling pathway [GO:0008286]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; positive regulation of cell proliferation [GO:0008284]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein import into nucleus [GO:0006606]; regulation of cell morphogenesis [GO:0022604]; regulation of cell shape [GO:0008360]; regulation of growth [GO:0040008]; regulation of protein phosphorylation [GO:0001932]Uinsulin receptor binding [GO:00051< 58]; lysine-acetylated histone binding [GO:0070577]FUNCTION: Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:12242307, ECO:0000269|PubMed:21834987}.P23763VAMP1%Vesicle-associated membrane protein 1SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Mitochondrion outer membrane; Single-pass type IV membrane protein.}exocytosis [GO:0006887]; SNARE complex assembly [GO:0035493]; synaptic transmission [GO:0007268]; vesicle fusion [GO:0006906]{cell junction [GO:0030054]; cell surface [GO:0009986]; cytosol [GO:0005829]; integral component of plasma membrane [GO:0005887]; mitochondrial outer membrane [GO:0005741]; SNARE complex [GO:0031201]; specific granule membrane [GO:0035579]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]; tertiary granule membrane [GO:0070821]aFUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane.Q8TEQ8PIGO(GPI ethanolamine phosphate transferase 3FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond (By similarity). {ECO:0000250}.Q92542NICA NicastrinSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.Xamyloid precursor protein catabolic process [GO:0042987]; apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; beta-amyloid metabolic process [GO:0050435]; ephrin receptor signaling pathway [GO:0048013]; epithelial cell proliferation [GO:0050673]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; membrane protein ectodomain proteolysis [GO:0006509]; membrane protein intracellular domain proteolysis [GO:0031293]; myeloid cell homeostasis [GO:0002262]; neurotrophin TRK receptor signaling pathway [GO:0048011]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]; proteolysis [GO:0006508]; T cell proliferation [GO:0042098]Qendoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]EFUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.Q6QEF8CORO6 Coronin-6actin cytoskeleton [GO:0015629]P51911CNN1 Calponin-1dactomyosin structure organization [GO:0031032]; regulation of smooth muscle contraction [GO:0006940]6cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]9FUNCTION: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity). {ECO:0000250}.Q96HR9REEP6'Receptor expression-enhancing protein 6SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24098485}; Multi-pass membrane protein {ECO:0000269|PubMed:24098485}.2regulation of intracellular transport [GO:0032386]apical part of cell [GO:0045177]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; rod spherule [GO:0044317]FUNCTION: May play a role in intracellular protein transport from the endoplasmic reticulum to the cell surface. May play a role in retinal development (By similarity). {ECO:0000250}.P57678GEMI4Gem-associated protein 4SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs and in the nucleolus.gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; rRNA processing [GO:0006364]; spliceosomal snRNP assembly [GO:0000387]4cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Gemini of coiled bodies [GO:0097504]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]NFUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:18984161}.Q9BT88SYT11Synaptotagmin-11SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12925569}; Single-pass membrane protein {ECO:0000269|PubMed:12925569}. Cell junction, synapse {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=In substantia nigra, observed in neuronal cell bodies and neurites. Found in the core of the Lewy bodies in the brain of sporadic Parkinson disease patients.calcium ion-dependent exocytosis of neurotransmitter [GO:0048791]; negative regulation of neurotransmitter secretion [GO:0046929]; regulation of calcium ion-dependent exocytosis [GO:0017158]; synaptic vesicle exocytosis [GO:0016079]calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; clathrin binding [GO:0030276]; syntaxin binding [GO:0019905]cell junction [GO:0030054]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. {ECO:0000250}.P19971TYPHThymidine phosphorylaseangiogenesis [GO:0001525]; cell differentiation [GO:0030154]; chemotaxis [GO:0006935]; DNA replication [GO:0006260]; mitochondrial genome maintenance [GO:0000002]; nucleobase-containing small molecule metabolic process [GO:0055086]; pyrimidine nucleobase metabolic process [GO:0006206]; pyrimidine nucleoside catabolic process [GO:0046135]; pyrimidine nucleoside salvage < [GO:0043097]; pyrimidine nucleotide metabolic process [GO:0006220]; small molecule metabolic process [GO:0044281] phosphorylase activity [GO:0004645]; platelet-derived growth factor receptor binding [GO:0005161]; pyrimidine-nucleoside phosphorylase activity [GO:0016154]; thymidine phosphorylase activity [GO:0009032]; transferase activity, transferring pentosyl groups [GO:0016763]FUNCTION: May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro. {ECO:0000269|PubMed:1590793}.; FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. {ECO:0000269|PubMed:1590793}.O15355PPM1GProtein phosphatase 1Gycell cycle arrest [GO:0007050]; peptidyl-threonine dephosphorylation [GO:0035970]; protein dephosphorylation [GO:0006470]Q13503MED216Mediator of RNA polymerase II transcription subunit 21blastocyst development [GO:0001824]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; stem cell maintenance [GO:0019827]; transcription, DNA-templated [GO:0006351]DNA-directed RNA polymerase activity [GO:0003899]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]CFUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15249124, ECO:0000269|PubMed:9660976}.Q9Y6V7DDX49)Probable ATP-dependent RNA helicase DDX49Q96RT7GCP6!Gamma-tubulin complex component 6wSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11694571}.xG2/M transition of mitotic cell cycle [GO:0000086]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]centrosome [GO:0005813]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; gamma-tubulin ring complex [GO:0008274]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle pole [GO:0000922]yFUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. {ECO:0000269|PubMed:11694571}.Q8N4V1MMGT1 Membrane magnesium transporter 1ySUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Early endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Detected in the Golgi apparatus and in post-Golgi vesicles including early endosomes. {ECO:0000250}.Jmagnesium ion transport [GO:0015693]; transmembrane transport [GO:0055085]early endosome [GO:0005769]; early endosome membrane [GO:0031901]; ER membrane protein complex [GO:0072546]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]3FUNCTION: Mediates Mg(2+) transport. {ECO:0000250}.Q9Y2L5TPPC8.Trafficking protein particle complex subunit 8autophagosome assembly [GO:0000045]; CVT pathway [GO:0032258]; ER to Golgi vesicle-mediated transport [GO:0006888]; nucleophagy [GO:0044804]; peroxisome degradation [GO:0030242]; protein localization to pre-autophagosomal structure [GO:0034497]rcytoplasmic vesicle [GO:0031410]; pre-autophagosomal structure [GO:0000407]; TRAPPIII protein complex [GO:1990072]FUNCTION: May be involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage. {ECO:0000269|PubMed:21525244}.O75147OBSL1Obscurin-like protein 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Golgi apparatus. Note=Colocalizes with CUL7 at the Golgi apparatus in neurons.Kcardiac myofibril assembly [GO:0055003]; cytoskeleton organization [GO:0007010]; Golgi organization [GO:0007030]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of dendrite morphogenesis [GO:0050775]; protein localization to Golgi apparatus [GO:0034067]; regulation of mitotic nuclear division [GO:0007088]3M complex [GO:1990393]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intercalated disc [GO:0014704]; M band [GO:0031430]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]mFUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons. {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, ECO:0000269|PubMed:24793696}.Q7L523RRAGA!Ras-related GTP-binding protein AcSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}. Nucleus {ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}. Lysosome {ECO:0000269|PubMed:20381137}. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (PubMed:8995684, PubMed:9394008). Colocalizes in vivo with adenovirus E3-14.7K mainly to the cytoplasm especially near the nuclear membrane and in discrete foci on or near the plasma membrane (PubMed:8995684). {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}.0apoptotic process [GO:0006915]; cell death [GO:0008219]; cellular protein localization [GO:0034613]; cellular response to amino acid starvation [GO:0034198]; cellular response to amino acid stimulus [GO:0071230]; cellular response to starvation [GO:0009267]; modulation by virus of host morphology or physiology [GO:0019048]; negative regulation of autophagy [GO:0010507]; positive regulation of cytolysis [GO:0045919]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of TOR signaling [GO:0032008]; regulation of autophagy [GO:0010506]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; phosphoprotein binding [GO:0051219]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; ubiquitin protein ligase binding [GO:0031625]cytoplasm [GO:0005737]; EGO complex [GO:0034448]; Golgi apparatus [GO:0005794]; Gtr1-Gtr2 GTPase complex [GO:1990131]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; nucleus [GO:0005634].FUNCTION: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates to the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death. {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:25936802, ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}.Q99549MPP8M-phase phosphoprotein 8SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Pub< Med:20871592, ECO:0000269|PubMed:23416073, ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:8885239}. Chromosome {ECO:0000269|PubMed:23416073, ECO:0000269|PubMed:26022416}. Note=Detected on heterochromatin (PubMed:20871592, PubMed:26022416). Dissociates from chromatin during interphase and early mitosis (PubMed:23416073). Detected on nucleosomes (PubMed:20871592). {ECO:0000269|PubMed:20871592, ECO:0000269|PubMed:23416073, ECO:0000269|PubMed:26022416}.negative regulation of transcription, DNA-templated [GO:0045892]; regulation of DNA methylation [GO:0044030]; transcription, DNA-templated [GO:0006351]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nuclear heterochromatin [GO:0005720]; nuclear nucleosome [GO:0000788]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]4FUNCTION: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:20871592, PubMed:26022416). Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3 (PubMed:26022416). Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene (PubMed:20871592). Mediates down-regulation of CDH1 expression (PubMed:20871592). {ECO:0000269|PubMed:20871592, ECO:0000269|PubMed:26022416}.Q9H3P2NELFANegative elongation factor A<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11150502}.gene expression [GO:0010467]; multicellular organismal development [GO:0007275]; negative regulation of transcription elongation from RNA polymerase II promoter [GO:0034244]; positive regulation of viral transcription [GO:0050434]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]FUNCTION: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. Probably required to interact with the RNA polymerase II complex. {ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:12563561, ECO:0000269|PubMed:12612062}.Q13145BAMBI0BMP and activin membrane-bound inhibitor homologjcell migration [GO:0016477]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of catenin import into nucleus [GO:0035413]; positive regulation of cell proliferation [GO:0008284]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of protein binding [GO:0032092]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of cell shape [GO:0008360]; transforming growth factor beta receptor signaling pathway [GO:0007179]dfrizzled binding [GO:0005109]; type II transforming growth factor beta receptor binding [GO:0005114]2FUNCTION: Negatively regulates TGF-beta signaling.Q9HB90RRAGC!Ras-related GTP-binding protein CSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Lysosome. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA.apoptotic process [GO:0006915]; cell growth [GO:0016049]; cellular protein localization [GO:0034613]; cellular response to amino acid starvation [GO:0034198]; cellular response to amino acid stimulus [GO:0071230]; cellular response to starvation [GO:0009267]; positive regulation of TOR signaling [GO:0032008]; regulation of autophagy [GO:0010506]; regulation of TOR signaling [GO:0032006]; RNA splicing [GO:0008380]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351]GDP binding [GO:0019003]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; protein heterodimerization activity [GO:0046982]cytoplasm [GO:0005737]; EGO complex [GO:0034448]; Gtr1-Gtr2 GTPase complex [GO:1990131]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]EFUNCTION: Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. {ECO:0000269|PubMed:20381137}.Q92963RIT1GTP-binding protein Rit1neurotrophin TRK receptor signaling pathway [GO:0048011]; Ras protein signal transduction [GO:0007265]; signal transduction [GO:0007165]; small GTPase mediated signal transduction [GO:0007264]9calmodulin binding [GO:0005516]; GTP binding [GO:0005525]8intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation. Involved in ELK1 transactivation through the Ras-MAPK signaling cascade that mediates a wide variety of cellular functions, including cell proliferation, survival, and differentiation. {ECO:0000269|PubMed:15632082, ECO:0000269|PubMed:23791108}.Q9HCJ6VAT1L4Synaptic vesicle membrane protein VAT-1 homolog-likeQ9NTG7SIR3:NAD-dependent protein deacetylase sirtuin-3, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:12186850, ECO:0000269|PubMed:12374852, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:18215119}.aerobic respiration [GO:0009060]; aging [GO:0007568]; mitochondrion organization [GO:0007005]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; organelle organization [GO:0006996]; peptidyl-lysine deacetylation [GO:0034983]; positive regulation of insulin secretion [GO:0032024]; protein ADP-ribosylation [GO:0006471]; protein deacetylation [GO:0006476]NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity (H3-K14 specific) [GO:0032041]; zinc ion binding [GO:0008270]FUNCTION: NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels. {ECO:0000269|PubMed:16788062, ECO:0000269|PubMed:18680753, ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:19535340, ECO:0000269|PubMed:24121500, ECO:0000269|PubMed:24252090}.P18754RCC1$Regulator of chromosome condensationSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17435751}. Cytoplasm {ECO:0000269|PubMed:17435751}. Note=Becomes dispersed throughout the cytoplasm during mitosis.jcell division [GO:0051301]; chromosome segregation [GO:0007059]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic nuclear division [GO:0007067]; mitotic spindle organization [GO:0007052]; positive regulation of GTPase activity [GO:0043547]; regulation of mitotic nuclear division [GO:0007088]; spindle assembly [GO:0051225]; viral process [GO:0016032]chromatin binding [GO:0003682]; histone binding [GO:0042393]; nucleosomal DNA binding [GO:0031492]; Ran guanyl-nucleotide exchange factor activity [GO:0005087]condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Guanine-nucleotide releasing< factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo-cytoplasmic transport, mitosis and nuclear-envelope assembly. {ECO:0000269|PubMed:1944575}.Q9NZM1MYOF MyoferlinSUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Nucleus membrane; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Note=Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels (By similarity). Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures. {ECO:0000250}.blood circulation [GO:0008015]; cellular response to heat [GO:0034605]; muscle contraction [GO:0006936]; myoblast fusion [GO:0007520]; plasma membrane repair [GO:0001778]; regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030947]Ecaveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]XFUNCTION: Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}.Q9H792PEAK1'Pseudopodium-enriched atypical kinase 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20534451}. Cell junction, focal adhesion {ECO:0000269|PubMed:20534451}. Note=Colocalizes with F-actin in serum-rich medium. Actin colocalization is reduced during serum starvation.cell migration [GO:0016477]; peptidyl-tyrosine phosphorylation [GO:0018108]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; substrate adhesion-dependent cell spreading [GO:0034446]ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Tyrosine kinase that may play a role in cell spreading and migration on fibronectin. May directly or indirectly affect phosphorylation levels of cytoskeleton-associated proteins MAPK1/ERK and PXN. {ECO:0000269|PubMed:20534451}.O95429BAG4*BAG family molecular chaperone regulator 4negativeDcell surface receptor signaling pathway [GO:0007166]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to heat [GO:0034605]; cellular response to tumor necrosis factor [GO:0071356]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:2001145]; negative regulation of protein targeting to mitochondrion [GO:1903215]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell adhesion [GO:0045785]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of stress fiber assembly [GO:0051496]; protein folding [GO:0006457]; protein localization to plasma membrane [GO:0072659]; regulation of cellular response to heat [GO:1900034]; ruffle assembly [GO:0097178]; tumor necrosis factor-mediated signaling pathway [GO:0033209]poly(A) RNA binding [GO:0044822]; receptor signaling protein activity [GO:0005057]; ubiquitin protein ligase binding [GO:0031625]FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PARK2 translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.Q96CS2HAUS1"HAUS augmin-like complex subunit 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes with the spindle poles in mitotic cells. In metaphase, localizes to the mitotic asters and is highly punctate on the microtubule array. During later stages of mitosis, remains on the spindle but is not present at the interzone, and is finally observed at the microtubule bundles proximal to the midbody, clearly excluded from the midbody. In contrast, does not colocalize with the tubulin cytoskeleton in interphase cells. In interphase, localized at the centrosome and diffusely in the cytoplasm.FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. {ECO:0000269|PubMed:15082789, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}.Q8WXI9P66B"Transcriptional repressor p66-betaSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11756549, ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}. Note=Speckled nuclear localization requires both CR1 and CR2 regions.ZATP-dependent chromatin remodeling [GO:0043044]; transcription, DNA-templated [GO:0006351]rnuclear chromatin [GO:0000790]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A. Targets MBD3 to discrete loci in the nucleus. May play a role in synapse development. {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.Q8NDW8TT21A$Tetratricopeptide repeat protein 21A~cilium morphogenesis [GO:0060271]; intraciliary retrograde transport [GO:0035721]; protein localization to cilium [GO:0061512]Ccilium [GO:0005929]; intraciliary transport particle A [GO:0030991]Q96FV9THOC1THO complex subunit 1XSUBCELLULAR LOCATION: Isoform 1: Nucleus speckle. Nucleus, nucleoplasm. Nucleus matrix. Cytoplasm. Note=Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.apoptotic process [GO:0006915]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; negative regulation of DNA damage checkpoint [GO:2000002]; negative regulation of isotype switching to IgA isotypes [GO:0048297]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; regulation of DNA recombination [GO:0000018]; regulation of DNA-templated transcription, elongation [GO:0032784]; replication fork processing [GO:0031297]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; viral mRNA export from host cell nucleus [GO:0046784]&cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; THO complex [GO:0000347]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346]FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mech< anism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.; FUNCTION: Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1.O95613PCNT PericentrinvSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:22797915}. Note=Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome.cilium assembly [GO:0042384]; G2/M transition of mitotic cell cycle [GO:0000086]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; positive regulation of intracellular protein transport [GO:0090316]centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]9FUNCTION: Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736}.Q9NWT1PK1IP2p21-activated protein kinase-interacting protein 1ycell proliferation [GO:0008283]; negative regulation of signal transduction [GO:0009968]; palate development [GO:0060021]Nnucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. {ECO:0000269|PubMed:11371639}.O60907TBL1X-F-box-like/WD repeat-containing protein TBL1Xcanonical Wnt signaling pathway [GO:0060070]; cellular lipid metabolic process [GO:0044255]; chromatin organization [GO:0006325]; histone deacetylation [GO:0016575]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; proteolysis [GO:0006508]; sensory perception of sound [GO:0007605]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351],beta-catenin binding [GO:0008013]; histone binding [GO:0042393]; protein C-terminus binding [GO:0008022]; protein domain specific binding [GO:0019904]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange. {ECO:0000269|PubMed:14980219}.Q8WZ42TITINTitineSUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16410549}. Nucleus {ECO:0000269|PubMed:16410549}.yblood coagulation [GO:0007596]; cardiac muscle contraction [GO:0060048]; cardiac muscle fiber development [GO:0048739]; cardiac muscle hypertrophy [GO:0003300]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac myofibril assembly [GO:0055003]; detection of muscle stretch [GO:0035995]; mitotic chromosome condensation [GO:0007076]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; regulation of catalytic activity [GO:0050790]; regulation of protein kinase activity [GO:0045859]; response to calcium ion [GO:0051592]; sarcomere organization [GO:0045214]; sarcomerogenesis [GO:0048769]; skeletal muscle myosin thick filament assembly [GO:0030241]; skeletal muscle thin filament assembly [GO:0030240]; striated muscle contraction [GO:0006941]pactin filament binding [GO:0051015]; actinin binding [GO:0042805]; ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; muscle alpha-actinin binding [GO:0051371]; protease binding [GO:0002020]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; structural constituent of muscle [GO:0008307]; structural molecule activity conferring elasticity [GO:0097493]; telethonin binding [GO:0031433]condensed nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; I band [GO:0031674]; M band [GO:0031430]; striated muscle thin filament [GO:0005865]; Z disc [GO:0030018]PFUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. {ECO:0000269|PubMed:9804419}.Q9NW81AT5SL#ATP synthase subunit s-like proteinQ6P2P2ANM9/Putative protein arginine N-methyltransferase 9 protein methylation [GO:0006479]P09619PGFRB,Platelet-derived growth factor receptor betaSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. adrenal gland development [GO:0030325]; aorta morphogenesis [GO:0035909]; cardiac myofibril assembly [GO:0055003]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; cell migration involved in coronary angiogenesis [GO:0060981]; cell migration involved in vasculogenesis [GO:0035441]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glycosaminoglycan biosynthetic process [GO:0006024]; G-protein < coupled receptor signaling pathway [GO:0007186]; innate immune response [GO:0045087]; inner ear development [GO:0048839]; in utero embryonic development [GO:0001701]; metanephric comma-shaped body morphogenesis [GO:0072278]; metanephric glomerular capillary formation [GO:0072277]; metanephric glomerular mesangial cell proliferation involved in metanephros development [GO:0072262]; metanephric mesenchymal cell migration [GO:0035789]; metanephric mesenchyme development [GO:0072075]; metanephric S-shaped body morphogenesis [GO:0072284]; negative regulation of apoptotic process [GO:0043066]; neurotrophin TRK receptor signaling pathway [GO:0048011]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol metabolic process [GO:0046488]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway [GO:0038091]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway [GO:0035793]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of phospholipase C activity [GO:0010863]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to estradiol [GO:0032355]; response to fluid shear stress [GO:0034405]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to retinoic acid [GO:0032526]; response to toxic substance [GO:0009636]; retina vasculature development in camera-type eye [GO:0061298]; signal transduction [GO:0007165]; skeletal system morphogenesis [GO:0048705]; smooth muscle cell chemotaxis [GO:0071670]; smooth muscle tissue development [GO:0048745]; tissue homeostasis [GO:0001894]; wound healing [GO:0042060]ATP binding [GO:0005524]; platelet activating factor receptor activity [GO:0004992]; platelet-derived growth factor-activated receptor activity [GO:0005017]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; vascular endothelial growth factor binding [GO:0038085]apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intrinsic component of plasma membrane [GO:0031226]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]W FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708, ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.Q8TF01PNISR"Arginine/serine-rich protein PNISRP11166GTR1ASolute carrier family 2, facilitated glucose transporter member 1SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Melanosome. Note=Localizes primarily at the cell surface. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.carbohydrate metabolic process [GO:0005975]; cellular response to glucose starvation [GO:0042149]; energy reserve metabolic process [GO:0006112]; glucose import [GO:0046323]; glucose transport [GO:0015758]; hexose transmembrane transport [GO:0035428]; hexose transport [GO:0008645]; lactose biosynthetic process [GO:0005989]; L-ascorbic acid metabolic process [GO:0019852]; protein complex assembly [GO:0006461]; proton transport [GO:0015992]; regulation of insulin secretion [GO:0050796]; response to osmotic stress [GO:0006970]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]Udehydroascorbic acid transporter activity [GO:0033300]; D-glucose transmembrane transporter activity [GO:0055056]; glucose transmembrane transporter activity [GO:0005355]; identical protein binding [GO:0042802]; protein self-association [GO:0043621]; sugar:proton symporter activity [GO:0005351]; xenobiotic transporter activity [GO:0042910]basolateral plasma membrane [GO:0016323]; blood microparticle [GO:0072562]; caveola [GO:0005901]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; female pronucleus [GO:0001939]; Golgi membrane [GO:0000139]; int< egral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]; membrane [GO:0016020]; midbody [GO:0030496]; plasma membrane [GO:0005886]$FUNCTION: Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. {ECO:0000269|PubMed:18245775, ECO:0000269|PubMed:19449892}.O95983MBD3#Methyl-CpG-binding domain protein 3SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Nuclear, in discrete foci. Detected on chromatin, at promoter regions of active genes.raging [GO:0007568]; ATP-dependent chromatin remodeling [GO:0043044]; brain development [GO:0007420]; chromatin organization [GO:0006325]; embryonic organ development [GO:0048568]; heart development [GO:0007507]; histone acetylation [GO:0016573]; in utero embryonic development [GO:0001701]; methylation-dependent chromatin silencing [GO:0006346]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of DNA methylation [GO:0044030]; response to estradiol [GO:0032355]; response to nutrient levels [GO:0031667]; tissue development [GO:0009888]; transcription, DNA-templated [GO:0006351]Ychromatin binding [GO:0003682]; DNA binding [GO:0003677]; methyl-CpG binding [GO:0008327]cytoplasm [GO:0005737]; heterochromatin [GO:0000792]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; NuRD complex [GO:0016581]; protein complex [GO:0043234]!FUNCTION: Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to DNA by itself (PubMed:12124384). Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases. {ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12124384, ECO:0000269|PubMed:18644863, ECO:0000269|PubMed:23361464, ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:9774669}.Q9Y3Q8T22D4TSC22 domain family protein 4negative regulation of transcription, DNA-templated [GO:0045892]; response to osmotic stress [GO:0006970]; transcription, DNA-templated [GO:0006351]$FUNCTION: Transcriptional repressor.P07339CATD Cathepsin D'SUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted, extracellular space. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380). {ECO:0000269|PubMed:20551380}.@antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; autophagy [GO:0006914]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]FUNCTION: Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.Q96SZ6CK5P1,CDK5 regulatory subunit-associated protein 1brain development [GO:0007420]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; regulation of neuron differentiation [GO:0045664]; tRNA modification [GO:0006400]iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; transferase activity [GO:0016740]:FUNCTION: Specifically inhibits CDK5 activation by CDK5R1.P00750TPA!Tissue-type plasminogen activatorrblood coagulation [GO:0007596]; cellular protein modification process [GO:0006464]; fibrinolysis [GO:0042730]; negative regulation of proteolysis [GO:0045861]; plasminogen activation [GO:0031639]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; proteolysis [GO:0006508]; response to hypoxia [GO:0001666]; smooth muscle cell migration [GO:0014909]glycoprotein binding [GO:0001948]; phosphoprotein binding [GO:0051219]; receptor binding [GO:0005102]; serine-type endopeptidase activity [GO:0004252]apical part of cell [GO:0045177]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]dFUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration.Q86SQ0PHLB21Pleckstrin homology-like domain family B member 29SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12376540}. Membrane {ECO:0000269|PubMed:12376540}; Peripheral membrane protein {ECO:0000269|PubMed:12376540}. Note=Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments.Destablishment of protein localization [GO:0045184]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of stress fiber assembly [GO:0051497]; negative regulation of wound healing, spreading of epidermal cells [GO:1903690]; positive regulation of basement membrane assembly involved in embryonic body morphogenesis [GO:1904261]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gastrulation [GO:0010470]; regulation of microtubule cytoskeleton organization [GO:0070507]basal cortex [GO:0045180]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; intermediate filament cytoskeleton [GO:0045111]; plasma membrane [GO:0005886]FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). {ECO:0000250}.Q9BQ75CMS1 Protein CMSS1Q99661KIF2CKinesin-like protein KIF2CSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1 (By similarity). Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGOL2. {ECO:0000250}.Dantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cell division [GO:0051301]; cell proliferation [GO:0008283]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; microtubule-based movement [GO:0007018]; microtubule depolymerization [GO:0007019]; mitotic cell cycle [GO:0000278]; mitotic metaphase plate congression [GO:0007080]; mitotic nuclear division [GO:0007067]; regulation of chromosome segregation [GO:0051983]; small GTPase mediated signal transduction [GO:0007264]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; centromeric DNA binding [GO:0019237]; microtubule motor activity [GO:0003777]; microtubule plus-end binding [GO:0051010]chromosome, centromeric region [GO:0000775]; condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; nucleus [GO:0005634]$FUNCTION: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. {ECO:0000269|PubMed:190< 60894, ECO:0000269|PubMed:21820309}.Q9Y2S0RPAC24DNA-directed RNA polymerases I and III subunit RPAC2#FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.O43159RRP8"Ribosomal RNA-processing protein 8SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:18485871}. Note=Localizes at rDNA locus.cellular response to glucose starvation [GO:0042149]; chromatin modification [GO:0016568]; chromatin silencing at rDNA [GO:0000183]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of gene expression, epigenetic [GO:0045814]; positive regulation of cell cycle arrest [GO:0071158]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription by glucose [GO:0046015]; rRNA processing [GO:0006364]; transcription, DNA-templated [GO:0006351]methylated histone binding [GO:0035064]; poly(A) RNA binding [GO:0044822]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]chromatin silencing complex [GO:0005677]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; rDNA heterochromatin [GO:0033553]FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown. {ECO:0000269|PubMed:18485871}.O96013PAK4%Serine/threonine-protein kinase PAK 4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12356872}. Note=Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways.actin cytoskeleton organization [GO:0030036]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell growth [GO:0016049]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cytoskeleton organization [GO:0007010]; movement of cell or subcellular component [GO:0006928]; regulation of apoptotic process [GO:0042981]; regulation of MAPK cascade [GO:0043408]; regulation of mitotic cell cycle [GO:0007346]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165]; signal transduction by protein phosphorylation [GO:0023014]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; Rac GTPase binding [GO:0048365]Qcytoplasm [GO:0005737]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. {ECO:0000269|PubMed:11278822, ECO:0000269|PubMed:11313478, ECO:0000269|PubMed:14560027, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:20507994, ECO:0000269|PubMed:20631255, ECO:0000269|PubMed:20805321}.Q9UHB6LIMA1&LIM domain and actin-binding protein 1SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Note=This cytoskeletal protein co-localizes with actin stress fibers and focal adhesion plaques.actin filament bundle assembly [GO:0051017]; negative regulation of actin filament depolymerization [GO:0030835]; ruffle organization [GO:0031529]factin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; zinc ion binding [GO:0008270]actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]/FUNCTION: Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments. {ECO:0000269|PubMed:12566430}.Q96HJ9CG055UPF0562 protein C7orf55Q16527CSRP2#Cysteine and glycine-rich protein 2{cell differentiation [GO:0030154]; multicellular organismal development [GO:0007275]; myoblast differentiation [GO:0045445]1focal adhesion [GO:0005925]; nucleus [GO:0005634]FUNCTION: Drastically down-regulated in response to PDGF-BB or cell injury, that promote smooth muscle cell proliferation and dedifferentiation. Seems to play a role in the development of the embryonic vascular system.Q8WTT2NOC3L#Nucleolar complex protein 3 homolog%fat cell differentiation [GO:0045444]:FUNCTION: May be required for adipogenesis. {ECO:0000250}.Q92560BAP1*Ubiquitin carboxyl-terminal hydrolase BAP1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O (PubMed:24703950). {ECO:0000269|PubMed:24703950}. cellular protein modification process [GO:0006464]; monoubiquitinated histone H2A deubiquitination [GO:0035522]; monoubiquitinated protein deubiquitination [GO:0035520]; negative regulation of cell proliferation [GO:0008285]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; regulation of cell cycle [GO:0051726]; regulation of cell growth [GO:0001558]; ubiquitin-dependent protein catabolic process [GO:0006511]rchromatin binding [GO:0003682]; peptidase activity [GO:0008233]; ubiquitin-specific protease activity [GO:0004843]ccytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PR-DUB complex [GO:0035517]FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lea< d to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor. {ECO:0000269|PubMed:12485996, ECO:0000269|PubMed:18757409, ECO:0000269|PubMed:19117993, ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:20436459, ECO:0000269|PubMed:24703950, ECO:0000269|PubMed:9528852}.Q8N6M3FITM2,Fat storage-inducing transmembrane protein 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18160536}; Multi-pass membrane protein {ECO:0000269|PubMed:18160536}.{cellular triglyceride homeostasis [GO:0035356]; cytoskeleton organization [GO:0007010]; lipid particle organization [GO:0034389]; lipid storage [GO:0019915]; phospholipid biosynthetic process [GO:0008654]; positive regulation of sequestering of triglyceride [GO:0010890]; regulation of cell morphogenesis [GO:0022604]; regulation of triglyceride biosynthetic process [GO:0010866]endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]; mitochondrion [GO:0005739]FUNCTION: Plays an important role in lipid droplet accumulation. Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:18160536, ECO:0000269|PubMed:21834987}.Q8NCG7DGLB'Sn1-specific diacylglycerol lipase beta}SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610053}; Multi-pass membrane protein {ECO:0000269|PubMed:14610053}.arachidonic acid metabolic process [GO:0019369]; blood coagulation [GO:0007596]; lipid catabolic process [GO:0016042]; neuroblast proliferation [GO:0007405]; neurotransmitter biosynthetic process [GO:0042136]; platelet activation [GO:0030168]<lipase activity [GO:0016298]; metal ion binding [GO:0046872]jintegral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses. {ECO:0000269|PubMed:14610053}.P49005DPOD2DNA polymerase delta subunit 2ubase-excision repair [GO:0006284]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]KDNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]=FUNCTION: The function of the small subunit is not yet clear.Q13555KCC2GACalcium/calmodulin-dependent protein kinase type II subunit gammaSUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; dephosphorylation [GO:0016311]; G1/S transition of mitotic cell cycle [GO:0000082]; insulin secretion [GO:0030073]; interferon-gamma-mediated signaling pathway [GO:0060333]; nervous system development [GO:0007399]; protein autophosphorylation [GO:0046777]; protein oligomerization [GO:0051259]; regulation of calcium ion transport [GO:0051924]; regulation of cellular response to heat [GO:1900034]; regulation of relaxation of cardiac muscle [GO:1901897]; regulation of skeletal muscle adaptation [GO:0014733]; synaptic transmission [GO:0007268]ATP binding [GO:0005524]; calcium-dependent protein serine/threonine phosphatase activity [GO:0004723]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein homodimerization activity [GO:0042803]cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; membrane [GO:0016020]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; sarcoplasmic reticulum membrane [GO:0033017]FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplsamic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin. In neurons, may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. {ECO:0000269|PubMed:16690701}.Q8NFW1COMA1Collagen alpha-1(XXII) chaincSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Cytoplasm {ECO:0000250}.SFUNCTION: Acts as a cell adhesion ligand for skin epithelial cells and fibroblasts.P61966AP1S1AP-1 complex subunit sigma-1ASUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:9733768}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral membrane protein {ECO:0000269|PubMed:9733768}; Cytoplasmic side {ECO:0000269|PubMed:9733768}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:9733768}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; receptor-mediated endocytosis [GO:0006898]; regulation of defense response to virus by virus [GO:0050690]; response to virus [GO:0009615]; viral process [GO:0016032]XAP-1 adaptor complex [GO:0030121]; clathrin-coated endocytic vesicle membrane [GO:0030669]; coated pit [GO:0005905]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; trans-Golgi network membrane [GO:0032588]nFUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. {ECO:0000269|PubMed:9733768}.P13667PDIA4Protein disulfide-isomerase A4cell redox homeostasis [GO:0045454]; chaperone-mediated protein folding [GO:0061077]; protein folding [GO:0006457]; protein secretion [GO:0009306]; response to endoplasmic reticulum stress [GO:0034976]Spoly(A) RNA binding [GO:0044822]; protein disulfide isomerase activity [GO:0003756]\cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; melanosome [GO:0042470]Q8WXG6MADD*MAP kinase-activating death domain proteindSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8988362}. Cytoplasm {ECO:0000269|PubMed:8988362}./activation of MAPK activity [GO:0000187]; cell surface receptor signaling pathway [GO:0007166]; execution phase of apoptosis [GO:0097194]; negative regulation of apoptotic signaling pathway [GO:2001234]; positive regulation of GTPase activity [GO:0043547< ]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of extrinsic apoptotic signaling pathway [GO:2001236]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of Rab protein signal transduction [GO:0032483]death receptor binding [GO:0005123]; protein kinase activator activity [GO:0030295]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]FUNCTION: Plays a significant role in regulating cell proliferation, survival and death through alternative mRNA splicing. Isoform 5 shows increased cell proliferation and isoform 2 shows decreased. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms. Component of the TNFRSF1A signaling complex: MADD links TNFRSF1A with MAP kinase activation. Plays an important regulatory role in physiological cell death (TNF-alpha-induced, caspase-mediated apoptosis); isoform 1 is susceptible to inducing apoptosis, isoform 5 is resistant and isoform 3 and isoform 4 have no effect. {ECO:0000269|PubMed:11577081, ECO:0000269|PubMed:14716293, ECO:0000269|PubMed:14735464, ECO:0000269|PubMed:15007167, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9115275}.Q96QZ7MAGI1LMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 1SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11969287}. Cell membrane {ECO:0000269|PubMed:11969287}; Peripheral membrane protein {ECO:0000269|PubMed:11969287}. Note=Localizes to epithelial cells tight junctions.cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; neuron death [GO:0070997]; protein complex assembly [GO:0006461]ealpha-actinin binding [GO:0051393]; ATP binding [GO:0005524]; protein C-terminus binding [GO:0008022]bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cell junction [GO:0030054]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity). {ECO:0000250}.P38936CDN1A#Cyclin-dependent kinase inhibitor 1 activation of protein kinase activity [GO:0032147]; cell cycle arrest [GO:0007050]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to extracellular stimulus [GO:0031668]; cellular response to heat [GO:0034605]; cellular response to ionizing radiation [GO:0071479]; cellular response to UV-B [GO:0071493]; cellular senescence [GO:0090398]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; intestinal epithelial cell maturation [GO:0060574]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; mitotic cell cycle [GO:0000278]; mitotic cell cycle arrest [GO:0071850]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:0042326]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organ regeneration [GO:0031100]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of programmed cell death [GO:0043068]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0000079]; regulation of DNA biosynthetic process [GO:2000278]; regulation of protein import into nucleus, translocation [GO:0033158]; response to arsenic-containing substance [GO:0046685]; response to corticosterone [GO:0051412]; response to drug [GO:0042493]; response to hyperoxia [GO:0055093]; response to organonitrogen compound [GO:0010243]; response to toxic substance [GO:0009636]; response to X-ray [GO:0010165]; stress-induced premature senescence [GO:0090400]cyclin-dependent protein kinase activating kinase activity [GO:0019912]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625] cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PCNA-p21 complex [GO:0070557]; perinuclear region of cytoplasm [GO:0048471]KFUNCTION: May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. {ECO:0000269|PubMed:8242751, ECO:0000269|PubMed:9106657}.Q9BVG9PTSS2Phosphatidylserine synthase 2ICDP-diacylglycerol-serine O-phosphatidyltransferase activity [GO:0003882]FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine.Q9NWZ8GEMI8Gem-associated protein 8SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000269|PubMed:16434402}. Cytoplasm {ECO:0000269|PubMed:16434402}. Note=Found in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.(spliceosomal snRNP assembly [GO:0000387]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]kFUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:17023415, ECO:0000269|PubMed:18984161}.A6NK02TRI75/Putative tripartite motif-containing protein 75<extracellular space [GO:0005615]; intracellular [GO:0005622]Q9UBB5MBD2#Methyl-CpG-binding domain protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:9774669}. Note=Nuclear, in discrete foci. Detected at replication foci in late S phase.@ATP-dependent chromatin remodeling [GO:0043044]; cellular protein complex assembly [GO:0043623]; gene expression [GO:0010467]; maternal beh< avior [GO:0042711]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of cell proliferation [GO:0042127]; regulation of gene expression, epigenetic [GO:0040029]; transcription, DNA-templated [GO:0006351]C2H2 zinc finger domain binding [GO:0070742]; chromatin binding [GO:0003682]; methyl-CpG binding [GO:0008327]; mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]; satellite DNA binding [GO:0003696]; siRNA binding [GO:0035197]cytoplasm [GO:0005737]; heterochromatin [GO:0000792]; histone deacetylase complex [GO:0000118]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]wFUNCTION: Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters. {ECO:0000269|PubMed:10471499, ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12665568, ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:9774669}.Q8IW45NNRD-ATP-dependent (S)-NAD(P)H-hydrate dehydrataseFSUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157}.ADP-dependent NAD(P)H-hydrate dehydratase activity [GO:0052855]; ATP binding [GO:0005524]; ATP-dependent NAD(P)H-hydrate dehydratase activity [GO:0047453]|FUNCTION: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. {ECO:0000255|HAMAP-Rule:MF_03157}.Q7L5N7PCAT2)Lysophosphatidylcholine acyltransferase 2 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21498505}; Single-pass type II membrane protein {ECO:0000269|PubMed:21498505}. Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Lipid droplet {ECO:0000269|PubMed:21498505}.+glycerophospholipid biosynthetic process [GO:0046474]; membrane organization [GO:0061024]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phospholipid metabolic process [GO:0006644]; platelet activating factor biosynthetic process [GO:0006663]; small molecule metabolic process [GO:0044281]1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-alkylglycerophosphocholine O-acetyltransferase activity [GO:0047192]; calcium ion binding [GO:0005509]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]FUNCTION: Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2-diacyl-sn-glycero-3-phosphocholine. {ECO:0000269|PubMed:20363836, ECO:0000269|PubMed:21498505}.Q8N7Z5ANR314Putative ankyrin repeat domain-containing protein 31Q6PJG2EMSA1)ELM2 and SANT domain-containing protein 1Q8IXM2BAP18!Chromatin complexes subunit BAP18#chromatin modification [GO:0016568]4MLL1 complex [GO:0071339]; NURF complex [GO:0016589]SFUNCTION: Component of chromatin complexes such as the MLL1/MLL and NURF complexes.O00479HMGN4BHigh mobility group nucleosome-binding domain-containing protein 4,chromatin [GO:0000785]; nucleus [GO:0005634]P05114HMGN1&Non-histone chromosomal protein HMG-14SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus.'chromatin organization [GO:0006325]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; post-embryonic camera-type eye morphogenesis [GO:0048597]; pyrimidine dimer repair by nucleotide-excision repair [GO:0000720]; regulation of development, heterochronic [GO:0040034]; regulation of epithelial cell proliferation [GO:0050678]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to UV-B [GO:0010224]; response to UV-C [GO:0010225]; transcription-coupled nucleotide-excision repair [GO:0006283]Dchromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]gFUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity). {ECO:0000250}.Q96HP0DOCK6"Dedicator of cytokinesis protein 6SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17196961}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17196961}. Note=Mainly located near the cell surface.Zcytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42 and RAC1 small GTPases. Through its activation of CDC42 and RAC1, may regulate neurite outgrowth (By similarity). {ECO:0000250}.Q71RC2LARP4La-related protein 4Ucytoskeleton organization [GO:0007010]; regulation of cell morphogenesis [GO:0022604]O75175CNOT3(CCR4-NOT transcription complex subunit 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Cytoplasm, P-body {ECO:0000250}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of stem cell maintenance [GO:2000036]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; transcription, DNA-templated [GO:0006351]; trophectodermal cell differentiation [GO:0001829]xCCR4-NOT complex [GO:0030014]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. May be involved in metabolic regulation; may be involved in recruitment of the CCR4-NOT complex to deadenylation target mRNAs involved in energy metabolism. Involved in mitotic progression and regulation of the spindle assembly checkpoint by regulating the stability of MAD1L1 mRNA. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may involve histone deacetylases. Involved in the maintenance of emryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:22342980, ECO:0000269|PubMed:22367759}.< Q9NRW7VPS45.Vacuolar protein sorting-associated protein 45SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with Golgi/endosomal vesicles and the trans-Golgi network. {ECO:0000250}.blood coagulation [GO:0007596]; intracellular protein transport [GO:0006886]; vesicle docking involved in exocytosis [GO:0006904]endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]wFUNCTION: May play a role in vesicle-mediated protein trafficking from the Golgi stack through the trans-Golgi network.Q5R3I4TTC38#Tetratricopeptide repeat protein 38Q9NVF7FBX28F-box only protein 28FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}.Q86VY9T200ATransmembrane protein 200AQ8IZ52CHSS2Chondroitin sulfate synthase 2(SUBCELLULAR LOCATION: Isoform 1: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytosol.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol. Mitochondrion.; SUBCELLULAR LOCATION: Isoform 2: Mitochondrion matrix {ECO:0000305}.cytosol [GO:0005829]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; mitochondrial matrix [GO:0005759]FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress. {ECO:0000269|PubMed:12761225}.Q9NUQ3TXLNG Gamma-taxilingSUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15911876}. Cytoplasm, cytosol {ECO:0000250}.cell cycle [GO:0007049]; regulation of bone mineralization [GO:0030500]; regulation of cell cycle [GO:0051726]; regulation of cell cycle process [GO:0010564]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]3cytosol [GO:0005829]; nuclear membrane [GO:0031965]jFUNCTION: May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression. {ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:18068885}.P06493CDK1Cyclin-dependent kinase 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic during the interphase. Colocalizes with SIRT2 on centrosome during prophase and on splindle fibers during metaphase of the mitotic cell cycle. Reversibly translocated from cytoplasm to nucleus when phosphorylated before G2-M transition when associated with cyclin-B1. Accumulates in mitochondria in G2-arrested cells upon DNA-damage. activation of MAPK activity [GO:0000187]; activation of MAPKK activity [GO:0000186]; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; cell division [GO:0051301]; cell migration [GO:0016477]; centrosome cycle [GO:0007098]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell differentiation [GO:0030855]; Fc-epsilon receptor signaling pathway [GO:0038095]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; MAPK cascade [GO:0000165]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic G2 DNA damage checkpoint [GO:0007095]; mitotic nuclear division [GO:0007067]; mitotic nuclear envelope disassembly [GO:0007077]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; negative regulation of apoptotic process [GO:0043066]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437]; pronuclear fusion [GO:0007344]; protein localization to kinetochore [GO:0034501]; Ras protein signal transduction [GO:0007265]; regulation of embryonic development [GO:0045995]; regulation of Schwann cell differentiation [GO:0014038]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small GTPase mediated signal transduction [GO:0007264]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II carboxy-terminal domain kinase activity [GO:0008353]"centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]FFUNCTION: Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is s< witched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. {ECO:0000269|PubMed:16371510, ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773, ECO:0000269|PubMed:21063390}.Q86X95CIR1#Corepressor interacting with RBPJ 1SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with NEK6 in the centrosome.mRNA processing [GO:0006397]; negative regulation of transcription, DNA-templated [GO:0045892]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription corepressor activity [GO:0003714]tcytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nuclear speck [GO:0016607]; nucleus [GO:0005634]^FUNCTION: May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription. {ECO:0000250, ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:9874765}.Q9NX74DUS2L/tRNA-dihydrouridine(20) synthase [NAD(P)+]-likeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15994936}. Endoplasmic reticulum {ECO:0000269|PubMed:15994936}. Note=Mainly at the endoplasmic reticulum.|negative regulation of cell death [GO:0060548]; negative regulation of cyclin-dependent protein kinase activity [GO:1904030]double-stranded RNA binding [GO:0003725]; flavin adenine dinucleotide binding [GO:0050660]; protein kinase inhibitor activity [GO:0004860]; tRNA dihydrouridine synthase activity [GO:0017150]Vcytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]FUNCTION: Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR. {ECO:0000269|PubMed:15994936, ECO:0000269|PubMed:18096616}.Q8TAP6CEP76Centrosomal protein of 76 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Does not localize along the ciliary axoneme.G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; regulation of centriole replication [GO:0046599]ccentriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; protein complex [GO:0043234]FUNCTION: Centrosomal protein involved in regulation of centriole duplication. Required to limit centriole duplication to once per cell cycle by preventing centriole reduplication. {ECO:0000269|PubMed:19460342}.Q9H147TDIF1:Deoxynucleotidyltransferase terminal-interacting protein 1YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131}.iDNA binding [GO:0003677]; nucleosome binding [GO:0031491]; protein homodimerization activity [GO:0042803]phistone deacetylase complex [GO:0000118]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro) (PubMed:11473582). Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA. {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:23874396, ECO:0000305|PubMed:25653165}.Q6VN20RBP10Ran-binding protein 10SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18222118}. Nucleus {ECO:0000269|PubMed:18222118}. Note=Predominantly cytoplasmic.FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase (By similarity). May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway. {ECO:0000250, ECO:0000269|PubMed:18222118}.Q9UPW5CBPC1Cytosolic carboxypeptidase 17SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23085998}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000269|PubMed:23085998}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. Note=Localizes in both the cytoplasm and nuclei of interphase and dividing cells. {ECO:0000269|PubMed:23085998}.Bcerebellar Purkinje cell differentiation [GO:0021702]; C-terminal protein deglutamylation [GO:0035609]; eye photoreceptor cell differentiation [GO:0001754]; mitochondrion organization [GO:0007005]; neuromuscular process [GO:0050905]; olfactory bulb development [GO:0021772]; protein side chain deglutamylation [GO:0035610]jmetallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270]FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. {ECO:0000250|UniProtKB:Q641K1}.Q15024EXOS7Exosome complex component RRP42iexonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; RNA catab< olic process [GO:0006401]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; rRNA processing [GO:0006364]hcytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nucleolus [GO:0005730]; nucleus [GO:0005634]fFUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.P26583HMGB2High mobility group protein B2apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cell chemotaxis [GO:0060326]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; cellular response to lipopolysaccharide [GO:0071222]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; DNA geometric change [GO:0032392]; DNA ligation involved in DNA repair [GO:0051103]; DNA topological change [GO:0006265]; inflammatory response to antigenic stimulus [GO:0002437]; male gonad development [GO:0008584]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleosome assembly [GO:0006334]; positive chemotaxis [GO:0050918]; positive regulation of DNA binding [GO:0043388]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of megakaryocyte differentiation [GO:0045654]; positive regulation of nuclease activity [GO:0032075]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; programmed cell death [GO:0012501]; regulation of neurogenesis [GO:0050767]; regulation of stem cell proliferation [GO:0072091]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to drug [GO:0042493]; response to lipopolysaccharide [GO:0032496]; response to steroid hormone [GO:0048545]; spermatid nucleus differentiation [GO:0007289]; V(D)J recombination [GO:0033151]chemoattractant activity [GO:0042056]; chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; drug binding [GO:0008144]; enhancer sequence-specific DNA binding [GO:0001158]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; poly(A) RNA binding [GO:0044822]; RAGE receptor binding [GO:0050786]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]; supercoiled DNA binding [GO:0097100]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212] cell [GO:0005623]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]oFUNCTION: DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity). {ECO:0000250}.Q6PJT7ZC3HE-Zinc finger CCCH domain-containing protein 14SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:19303045, ECO:0000269|PubMed:24671764}.; SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle.; SUBCELLULAR LOCATION: Isoform 3: Nucleus speckle.; SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.cnegative regulation of mRNA polyadenylation [GO:1900364]; regulation of mRNA stability [GO:0043488]^metal ion binding [GO:0046872]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]FUNCTION: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides. {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:24671764}.P45973CBX5Chromobox protein homolog 5QSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410}. Chromosome {ECO:0000269|PubMed:10460410}. Chromosome, centromere {ECO:0000269|PubMed:10460410}. Note=Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase.|blood coagulation [GO:0007596]; negative regulation of transcription, DNA-templated [GO:0045892]; viral process [GO:0016032]chromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; protein binding, bridging [GO:0030674]; repressing transcription factor binding [GO:0070491]|chromocenter [GO:0010369]; histone deacetylase complex [GO:0000118]; histone methyltransferase complex [GO:0035097]; kinetochore [GO:0000776]; nuclear envelope [GO:0005635]; nuclear heterochromatin [GO:0005720]; nuclear pericentric heterochromatin [GO:0031618]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]FUNCTION: Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. {ECO:0000269|PubMed:19783980}.Q05639EF1A2Elongation factor 1-alpha 2positive regulation of apoptotic process [GO:0043065]; positive regulation of lipid kinase activity [GO:0090218]; response to inorganic substance [GO:0010035]GTPase activity [GO:0003924]; GTP binding [GO:0005525]; protein kinase binding [GO:0019901]; translation elongation factor activity [GO:0003746]; translation factor activity, RNA binding [GO:0008135]cytoplasm [GO:0005737]; eukaryotic translation elongation factor 1 complex [GO:0005853]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]Q53EL6PDCD4Programmed cell death protein 4SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and cytoplasm. Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457. Exported from the nucleus in the absence of serum.capoptotic process [GO:0006915]; cell aging [GO:0007569]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell cycle [GO:0045786]; negative regulation of JUN kinase activity [GO:0043508]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation o< f smooth muscle cell apoptotic process [GO:0034393]"FUNCTION: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity). {ECO:0000250}.Q658Y4F91A1Protein FAM91A1P37235HPCL1Hippocalcin-like protein 1[FUNCTION: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.P18887XRCC1DNA repair protein XRCC1eSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353262}. Note=Accumulates at sites of DNA damage.base-excision repair [GO:0006284]; DNA repair [GO:0006281]; hippocampus development [GO:0021766]; response to drug [GO:0042493]; response to hypoxia [GO:0001666]; response to organic substance [GO:0010033]; single strand break repair [GO:0000012]=damaged DNA binding [GO:0003684]; enzyme binding [GO:0019899]FUNCTION: Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.P31641SC6A62Sodium- and chloride-dependent taurine transporteramino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; cellular amino acid metabolic process [GO:0006520]; ion transport [GO:0006811]; taurine transport [GO:0015734]; transmembrane transport [GO:0055085]; transport [GO:0006810]gneurotransmitter:sodium symporter activity [GO:0005328]; taurine:sodium symporter activity [GO:0005369]FUNCTION: Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake. {ECO:0000269|PubMed:8382624}.Q6P582MZT2A%Mitotic-spindle organizing protein 2A{SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.Vcentrosome [GO:0005813]; gamma-tubulin ring complex [GO:0008274]; spindle [GO:0005819]Q6L8Q7PDE122',5'-phosphodiesterase 12SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541}.Smetal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]FUNCTION: Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system. {ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541}.P07864LDHCL-lactate dehydrogenase C chainATP biosynthetic process [GO:0006754]; carbohydrate metabolic process [GO:0005975]; lactate biosynthetic process from pyruvate [GO:0019244]; lactate oxidation [GO:0019516]; sperm motility [GO:0030317]-L-lactate dehydrogenase activity [GO:0004459]lcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; motile cilium [GO:0031514]; nucleus [GO:0005634]*FUNCTION: Possible role in sperm motility.O95171SCELSciellinqSUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=May become cross-linked to membrane proteins by transglutaminase.nembryo development [GO:0009790]; epidermis development [GO:0008544]; keratinocyte differentiation [GO:0030216][cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]FUNCTION: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope.Q3KRA6CB076UPF0538 protein C2orf76O14807RASMRas-related protein M-Rasactin cytoskeleton organization [GO:0030036]; multicellular organismal development [GO:0007275]; muscle organ development [GO:0007517]; Ras protein signal transduction [GO:0007265]bGTPase activity [GO:0003924]; GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]FUNCTION: May serve as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Weakly activates the MAP kinase pathway. {ECO:0000269|PubMed:16630891}.Q8WYP5ELYS Protein ELYSSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250}. Chromosome, centromere, kinetochore. Nucleus, nucleoplasm. Nucleus, nuclear pore complex. Note=Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase.cytokinesis [GO:0000910]; mitotic cell cycle [GO:0000278]; mRNA transport [GO:0051028]; nuclear pore complex assembly [GO:0051292]; protein transport [GO:0015031]; small GTPase mediated signal transduction [GO:0007264]condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:17235358}.Q92610ZN592Zinc finger protein 592Q13625ASPP2&Apoptosis-stimulating of p53 protein 2SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.cell cycle [GO:0007049]; central nervous system development [GO:0007417]; embryo development ending in birth or egg hatching [GO:0009792]; heart development [GO:0007507]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of cell cycle [GO:0045786]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of neuron death [GO:1901216]; positive regulation of signal transduction [GO:0009967]; response to ionizing radiation [GO:0010212]; signal transduction [GO:0007165]identical protein binding [GO:0042802]; NF-kappaB binding [GO:0051059]; p53 binding [GO:0002039]; SH3/SH2 adaptor activity [GO:0005070]4FUNCTION: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}.P78426NKX61Homeobox protein Nkx-6.1cell proliferation [GO:0008283]; cellular response to cytokine stimulus [GO:0071345]; cellular response to peptide hormone stimulus [GO:0071375]; detection of glucose [GO:0051594]; endocrine pancreas development [GO:0031018]; negative regulation of glial cell differentiation [GO:0045686]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; oligode< ndrocyte differentiation [GO:0048709]; organ morphogenesis [GO:0009887]; pancreas development [GO:0031016]; positive regulation of glial cell differentiation [GO:0045687]; positive regulation of insulin secretion [GO:0032024]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type B pancreatic cell development [GO:2000078]; regulation of axon extension [GO:0030516]; regulation of neuron migration [GO:2001222]; regulation of transcription from RNA polymerase II promoter involved in spinal cord motor neuron fate specification [GO:0021912]; regulation of transcription from RNA polymerase II promoter involved in ventral spinal cord interneuron specification [GO:0021913]; response to drug [GO:0042493]; response to nicotine [GO:0035094]; smoothened signaling pathway [GO:0007224]; transcription from RNA polymerase II promoter [GO:0006366]; type B pancreatic cell maturation [GO:0072560]%chromatin binding [GO:0003682]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]FUNCTION: Transcription factor which binds to specific A/T-rich DNA sequences in the promoter regions of a number of genes. Involved in transcriptional regulation in islet beta cells. Binds to the insulin promoter and is involved in regulation of the insulin gene. Together with NKX2-2 and IRX3 acts to restrict the generation of motor neurons to the appropriate region of the neural tube. Belongs to the class II proteins of neuronal progenitor factors, which are induced by SHH signals (By similarity). {ECO:0000250}.Q2NL82TSR1(Pre-rRNA-processing protein TSR1 homologbFUNCTION: Required during maturation of the 40S ribosomal subunit in the nucleolus. {ECO:0000250}.Q14444CAPR1Caprin-1vSUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, dendrite. Note=Associated with RNA granules. {ECO:0000250}.negative regulation of translation [GO:0017148]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of dendritic spine morphogenesis [GO:0061003]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]FUNCTION: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. {ECO:0000250}.Q16739CEGTCeramide glucosyltransferasehSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.aepidermis development [GO:0008544]; glucosylceramide biosynthetic process [GO:0006679]; glycosphingolipid biosynthetic process [GO:0006688]; glycosphingolipid metabolic process [GO:0006687]; positive regulation of protein targeting to mitochondrion [GO:1903955]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]2ceramide glucosyltransferase activity [GO:0008120]FUNCTION: Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase". {ECO:0000269|PubMed:8643456}.P27144KAD4!Adenylate kinase 4, mitochondrialSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03170, ECO:0000269|PubMed:11485571, ECO:0000269|PubMed:19766732}.`ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; brain development [GO:0007420]; GTP metabolic process [GO:0046039]; liver development [GO:0001889]; nucleoside diphosphate phosphorylation [GO:0006165]; nucleoside triphosphate biosynthetic process [GO:0009142]; response to drug [GO:0042493]adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside triphosphate adenylate kinase activity [GO:0046899]FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03170, ECO:0000269|PubMed:19073142, ECO:0000269|PubMed:19766732, ECO:0000269|PubMed:23416111}.Q13613MTMR1Myotubularin-related protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z2C4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z2C4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z2C4}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z2C4}.phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3-phosphatase activity [GO:0004438]; protein tyrosine phosphatase activity [GO:0004725]FUNCTION: Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate. {ECO:0000269|PubMed:11733541}.Q2TBE0C19L2CWF19-like protein 2Q9Y3D8KAD6Adenylate kinase isoenzyme 6SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body. Note=Displays widespread diffuse nucleoplasmic distribution but not detected in nucleoli. Detected in Cajal bodies but not in all cells.'nucleotide phosphorylation [GO:0046939]^adenylate kinase activity [GO:0004017]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]HCajal body [GO:0015030]; membrane [GO:0016020]; nucleoplasm [GO:0005654]FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. AMP and dAMP are the preferred substrates, but CMP and dCMP are also good substrates. IMP is phosphorylated to a much lesser extent. All nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and TTP are accepted as phosphate donors. CTP is the best phosphate donor, followed by UTP, ATP, GTP and dCTP. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation. {ECO:0000269|PubMed:15630091}.Q6N075MFSD5Molybdate-anion transportermolybdate ion transmembrane transporter activity [GO:0015098]; substrate-specific transmembrane transporter activity [GO:0022891]zFUNCTION: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum. {ECO:0000269|PubMed:21464289}.Q9BVW5TIPINTIMELESS-interacting protein~cell cycle phase transition [GO:0044770]; cell division [GO:0051301]; DNA replication checkpoint [GO:0000076]; intra-S DNA damage checkpoint [GO:0031573]; mitotic nuclear division [GO:0007067]; positive regulation of cell proliferation [GO:0008284]; regulation of nuclear cell cycle DNA replication [GO:0033262]; replication fork protection [GO:0048478]; response to UV [GO:0009411]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress. {ECO:0000269|PubMed:17102137, ECO:0000269|PubMed:17116885, ECO:0000269|PubMed:17296725}.O14981< BTAF1*TATA-binding protein-associated factor 172wnegative regulation of chromatin binding [GO:0035562]; negative regulation of transcription, DNA-templated [GO:0045892]ATP binding [GO:0005524]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner.A0PK00T120BTransmembrane protein 120BwSUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}.OFUNCTION: Necessary for efficient adipogenesis. {ECO:0000250|UniProtKB:Q3TA38}.Q5EB52MEST,Mesoderm-specific transcript homolog proteinsmesoderm development [GO:0007498]; regulation of lipid storage [GO:0010883]; response to retinoic acid [GO:0032526]P54803GALCGalactocerebrosidasecarbohydrate metabolic process [GO:0005975]; galactosylceramide catabolic process [GO:0006683]; glycosphingolipid metabolic process [GO:0006687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]*galactosylceramidase activity [GO:0004336]xFUNCTION: Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon. {ECO:0000269|PubMed:8281145, ECO:0000269|PubMed:8399327}.Q9UJV9DDX41)Probable ATP-dependent RNA helicase DDX41apoptotic process [GO:0006915]; cellular response to interferon-beta [GO:0035458]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; multicellular organismal development [GO:0007275]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of type I interferon production [GO:0032479]; RNA processing [GO:0006396]; RNA secondary structure unwinding [GO:0010501]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]zcatalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]FUNCTION: Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing.Q13683ITA7Integrin alpha-7rblood vessel morphogenesis [GO:0048514]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; regulation of cell shape [GO:0008360]cell surface [GO:0009986]; cytoplasm [GO:0005737]; integrin alpha7-beta1 complex [GO:0034677]; muscle tendon junction [GO:0005927]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]FUNCTION: Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. {ECO:0000250, ECO:0000269|PubMed:10694445, ECO:0000269|PubMed:17641293, ECO:0000269|PubMed:9307969}.Q96FV2SCRN2 Secernin-25cell [GO:0005623]; extracellular exosome [GO:0070062]P50747BPL1Biotin--protein ligase_biotin metabolic process [GO:0006768]; cell proliferation [GO:0008283]; histone biotinylation [GO:0071110]; histone modification [GO:0016570]; protein biotinylation [GO:0009305]; response to biotin [GO:0070781]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ATP binding [GO:0005524]; biotin-[acetyl-CoA-carboxylase] ligase activity [GO:0004077]; biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity [GO:0004078]; biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity [GO:0004079]; biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity [GO:0004080]; biotin binding [GO:0009374]; biotin-protein ligase activity [GO:0018271]; enzyme binding [GO:0019899]chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]FUNCTION: Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase.Q15858SCN9A+Sodium channel protein type 9 subunit alphafSUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Note=In neurite terminals. {ECO:0000250}.Ybehavioral response to pain [GO:0048266]; inflammatory response [GO:0006954]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; post-embryonic development [GO:0009791]; response to toxic substance [GO:0009636]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]Ssodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248]Oplasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518]FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain (By similarity). {ECO:0000250}.O60499STX10 Syntaxin-10Golgi vesicle transport [GO:0048193]; intracellular protein transport [GO:0006886]; regulation of protein localization [GO:0032880]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion [GO:0006906]Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]; vesicle [GO:0031982]O60244MED146Mediator of RNA polymerase II transcription subunit 14hligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; receptor activity [GO:0004872]; RNA polymerase II transcription cofactor activity [GO:0001104]; thyroid hormone receptor binding [GO:0046966]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; vitamin D receptor binding [GO:0042809]aFUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15340088, ECO:0000269|PubMed:15625066, ECO:0000269|PubMed:16595664}.< P98196AT11A,Probable phospholipid-transporting ATPase IHSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Early endosome {ECO:0000269|PubMed:21914794}. Recycling endosome {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum {ECO:0000269|PubMed:21914794}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, predominantly located in the plasma membrane.'phospholipid translocation [GO:0045332]early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. {ECO:0000269|PubMed:15860663, ECO:0000305}.O14966RAB7LRas-related protein Rab-7L1 SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Golgi apparatus, trans-Golgi network. Vacuole. Cytoplasm, cytoskeleton. Note=Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (By similarity). Colocalizes with GM130 at the Golgi apparatus. Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus. Colocalizes with TGN46 at the trans-Golgi network (TGN). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery. {ECO:0000250}.pcell differentiation [GO:0030154]; Golgi organization [GO:0007030]; Golgi to endosome transport [GO:0006895]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; positive regulation of intracellular protein transport [GO:0090316]; Rab protein signal transduction [GO:0032482]; retrograde transport, plasma membrane to Golgi [GO:0035526]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; vacuole [GO:0005773]FUNCTION: Rab GTPase key regulator in vesicle trafficking. Essential for maintaining the integrity of the endosome-trans-Golgi network structure. Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection. {ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816}.Q9BRT9SLD5)DNA replication complex GINS protein SLD5#DNA duplex unwinding [GO:0032508]; DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair via break-induced replication [GO:0000727]; inner cell mass cell proliferation [GO:0001833]; mitotic cell cycle [GO:0000278]}cytoplasm [GO:0005737]; GINS complex [GO:0000811]; nucleoplasm [GO:0005654]; replication fork protection complex [GO:0031298]FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is important for GINS complex assembly. GINS complex seems to bind preferentially to single-stranded DNA. {ECO:0000269|PubMed:17417653}.P46063RECQ1ATP-dependent DNA helicase Q1;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7961977}.DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand renaturation [GO:0000733]annealing helicase activity [GO:0036310]; ATP binding [GO:0005524]; ATP-dependent 3'-5' DNA helicase activity [GO:0043140]; ATP-dependent DNA helicase activity [GO:0004003]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]UFUNCTION: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:7961977, ECO:0000269|PubMed:8056767}.Q14562DHX8ATP-dependent RNA helicase DHX8cmRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]}FUNCTION: Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. {ECO:0000269|PubMed:8608946}.P07099HYEPEpoxide hydrolase 1SUBCELLULAR LOCATION: Microsome membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.aromatic compound catabolic process [GO:0019439]; response to organic cyclic compound [GO:0014070]; response to toxic substance [GO:0009636][cis-stilbene-oxide hydrolase activity [GO:0033961]; epoxide hydrolase activity [GO:0004301]FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water.P25440BRD2 Bromodomain-containing protein 2XSUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Detected on chromatin and nucleosomes.chromatin modification [GO:0016568]; nucleosome assembly [GO:0006334]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]Nchromatin binding [GO:0003682]; lysine-acetylated histone binding [GO:0070577]DFUNCTION: May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly. {ECO:0000250, ECO:0000269|PubMed:18406326}.Q9P2J3KLHL9Kelch-like protein 9dcytokinesis [GO:0000910]; mitotic nuclear division [GO:0007067]; protein ubiquitination [GO:0016567]ECul3-RING ubiquitin ligase complex [GO:0031463]; midbody [GO:0030496]FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:19995937}.Q15437SC23B Protein transport protein Sec23BSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}.ER to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; vesicle-mediated transport [GO:0016192]SCOPII vesicle coat [GO:0030127]; endomembrane system [GO:0012505]; endo< plasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]QFUNCTION: Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex (By similarity). {ECO:0000250}.Q15013MD2BPMAD2L1-binding proteinSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. Note=During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle.Xmitotic cell cycle checkpoint [GO:0007093]; regulation of exit from mitosis [GO:0007096]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819]FUNCTION: May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex. {ECO:0000269|PubMed:18022368}.Q9Y6M7S4A7"Sodium bicarbonate cotransporter 3SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein. Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, stereocilium {ECO:0000250}. Note=Also described at the apical cell membrane. Localizes to the stereocilia of cochlear outer hair cells and to the lateral membrane of cochlear inner hair cells (By similarity). {ECO:0000250}.anion transmembrane transport [GO:0098656]; auditory receptor cell development [GO:0060117]; bicarbonate transport [GO:0015701]; camera-type eye photoreceptor cell differentiation [GO:0060219]; cochlear nucleus development [GO:0021747]; ion transport [GO:0006811]; regulation of intracellular pH [GO:0051453]; retinal cell programmed cell death [GO:0046666]; retina vasculature morphogenesis in camera-type eye [GO:0061299]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]; visual perception [GO:0007601]apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]?FUNCTION: Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates intracellular pH and may play a role in bicarbonate salvage in secretory epithelia. May also have an associated sodium channel activity. {ECO:0000269|PubMed:10347222, ECO:0000269|PubMed:12403779}.O95210STBD1*Starch-binding domain-containing protein 1 SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:20810658, ECO:0000305|PubMed:21893048}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24837458}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Note=Distributed in the transverse tubules and/or near the junctional sarcoplasmic reticulum (PubMed:9794794). Concentrates at perinuclear structures (PubMed:21893048). {ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:9794794}.starch binding [GO:2001070]FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes. {ECO:0000269|PubMed:20810658, ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:24837458}.Q15800MSMO1Methylsterol monooxygenase 1cholesterol biosynthetic process [GO:0006695]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; small molecule metabolic process [GO:0044281]; steroid metabolic process [GO:0008202]MC-4 methylsterol oxidase activity [GO:0000254]; iron ion binding [GO:0005506]Q9H6S1AZI25-azacytidine-induced protein 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14560022}.sdendritic cell differentiation [GO:0097028]; dendritic cell proliferation [GO:0044565]; I-kappaB kinase/NF-kappaB signaling [GO:0007249]; interferon-alpha production [GO:0032607]; interferon-gamma production [GO:0032609]; interleukin-6 production [GO:0032635]; mitotic cell cycle [GO:0000278]; T cell activation [GO:0042110]; tumor necrosis factor production [GO:0032640]FUNCTION: Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1. {ECO:0000269|PubMed:14560022, ECO:0000269|PubMed:15611223, ECO:0000269|PubMed:21931631}.Q8IZL8PELP13Proline-, glutamic acid- and leucine-rich protein 1SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus. Cytoplasm. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasm (By similarity). Also found associated with the plasma membrane. Mainly in cytoplasm in a subset of breast tumors. Localization is widely deregulated in endometrial cancers with predominantly cytoplasm localization in high-grade endometrial tumors. {ECO:0000250}.cellular response to estrogen stimulus [GO:0071391]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]kchromatin binding [GO:0003682]; poly(A) RNA binding [GO:0044822]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; membrane [GO:0016020]; MLL1 complex [GO:0071339]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]OFUNCTION: Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. {ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108, ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770, ECO:0000269|PubMed:15579769, ECO:0000269|PubMed:15994929, ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611, ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:22872859}.Q9NZM5GSCR27Glioma tumor suppressor candidate region gene 2 proteindSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10196275, ECO:0000269|PubMed:12429849}.iintracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]Q96SB8SMC6/Structural maintenance of chromosomes protein 6$cellular protein metabolic process [GO:0044267]; cellular senescence [GO:0090398]; double-strand break repair via homologous recombination [GO:0000724]; post-translational protein modification [< GO:0043687]; protein sumoylation [GO:0016925]; telomere maintenance via recombination [GO:0000722]chromosome, telomeric region [GO:0000781]; intracellular [GO:0005622]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Smc5-Smc6 complex [GO:0030915]FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526}.Q96NT3GUCD1 Protein GUCD1Q52LW3RHG29 Rho GTPase-activating protein 29positive regulation of GTPase activity [GO:0043547]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]gGTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. {ECO:0000269|PubMed:15752761, ECO:0000269|PubMed:9305890}.Q6DT37MRCKG*Serine/threonine-protein kinase MRCK gammanSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15194684}. Note=Concentrates at the leading edge of cells.actin cytoskeleton reorganization [GO:0031532]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]6cell leading edge [GO:0031252]; cytoplasm [GO:0005737] FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q5VT25}.Q12789TF3C1-General transcription factor 3C polypeptide 1Z5S class rRNA transcription from RNA polymerase III type 1 promoter [GO:0042791]; gene expression [GO:0010467]; rRNA transcription [GO:0009303]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase III promoter [GO:0006383]; tRNA transcription [GO:0009304]; tRNA transcription from RNA polymerase III promoter [GO:0042797]membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]; transcription factor TFIIIC complex [GO:0000127] FUNCTION: Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. Binds to the box B promoter element.O95415BRI3Brain protein I3P61978HNRPK)Heterogeneous nuclear ribonucleoprotein KSUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Cell projection, podosome. Note=Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53. In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of low-density lipoprotein particle receptor biosynthetic process [GO:0045716]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter [GO:0072369]; regulation of low-density lipoprotein particle clearance [GO:0010988]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; signal transduction [GO:0007165]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]kpoly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; single-stranded DNA binding [GO:0003697]catalytic step 2 spliceosome [GO:0071013]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; podosome [GO:0002102]lFUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. {ECO:0000250, ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22825850}.Q5SNT2TM201Transmembrane protein 201SUBCELLULAR LOCATION: Isoform SAMP1: Nucleus inner membrane {ECO:0000269|PubMed:19494128}; Multi-pass membrane protein {ECO:0000269|PubMed:19494128}. Note=The C-terminal of isoform SAMP1 is located on the nucleoplasmic side. During interphase, isoform SAMP1 is distributed in the inner nuclear membrane and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle.Afibroblast migration [GO:0010761]; nuclear migration [GO:0007097]FUNCTION: Isoform SAMP1 may define a distinct membrane domain in the vicinity of the mitotic spindle. {ECO:0000269|PubMed:19494128}.Q9NVM6DJC17"DnaJ homolog subfamily C member 17onegative regulation of transcription from RNA polymerase II promoter [GO:0000122]; toxin transport [GO:1901998]Q14643ITPR1,Inositol 1,4,5-trisphosphate receptor type 1activation of phospholipase C activity [GO:0007202]; blood coagulation [GO:0007596]; calcium ion transport [GO:0006816]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; inositol phosphate-mediated signaling [GO:0048016]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of calcium-mediated signaling [GO:0050849]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; post-embryonic development [GO:0009791]; regulation of insulin secretion [GO:0050796]; release of sequestered calcium ion into cytosol [GO:0051209]; response to hypoxia [GO:0001666]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; voluntary musculoskeletal movement [GO:0050882]/calcium channel inhibitor activity [GO:0019855]; calcium ion transmembrane transporter ac< tivity [GO:0015085]; inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0005220]; intracellular ligand-gated calcium channel activity [GO:0005218]; phosphatidylinositol binding [GO:0035091]calcineurin complex [GO:0005955]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear inner membrane [GO:0005637]; nucleolus [GO:0005730]; platelet dense granule membrane [GO:0031088]; platelet dense tubular network [GO:0031094]; platelet dense tubular network membrane [GO:0031095]; postsynaptic density [GO:0014069]; sarcoplasmic reticulum [GO:0016529]FUNCTION: Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity). {ECO:0000250|UniProtKB:P11881}.Q9NUL7DDX28)Probable ATP-dependent RNA helicase DDX28SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350955}. Mitochondrion {ECO:0000269|PubMed:11350955}. Note=Transported between these two compartments. Nuclear localization depends on active RNA polymerase II transcription.cytoplasm [GO:0005737]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: May be involved in RNA processing or transport. Has RNA and Mg(2+)-dependent ATPase activity. {ECO:0000269|PubMed:11350955}.P23470PTPRG0Receptor-type tyrosine-protein phosphatase gammanegative regulation of epithelial cell migration [GO:0010633]; peptidyl-tyrosine dephosphorylation [GO:0035335]; toxin transport [GO:1901998]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]identical protein binding [GO:0042802]; protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]QFUNCTION: Possesses tyrosine phosphatase activity. {ECO:0000269|PubMed:19167335}.P24941CDK2Cyclin-dependent kinase 2SSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus, Cajal body. Cytoplasm. Endosome. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3).&anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; blood coagulation [GO:0007596]; cell division [GO:0051301]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; centrosome duplication [GO:0051298]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; histone phosphorylation [GO:0016572]; lens development in camera-type eye [GO:0002088]; meiotic nuclear division [GO:0007126]; mitotic cell cycle [GO:0000278]; mitotic G1 DNA damage checkpoint [GO:0031571]; mitotic nuclear division [GO:0007067]; organ regeneration [GO:0031100]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA-dependent DNA replication initiation [GO:0032298]; positive regulation of transcription, DNA-templated [GO:0045893]; potassium ion transport [GO:0006813]; Ras protein signal transduction [GO:0007265]; regulation of gene silencing [GO:0060968]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; response to cadmium ion [GO:0046686]; response to cAMP [GO:0051591]; response to drug [GO:0042493]; response to electrical stimulus [GO:0051602]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to toxic substance [GO:0009636]ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]Cajal body [GO:0015030]; centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; condensed chromosome [GO:0000793]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]; X chromosome [GO:0000805]; Y chromosome [GO:0000806] FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). {ECO:0000250|UniProtKB:P97377, ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10995386, ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:18372919, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20079829, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20195506, ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21319273, ECO:0000269|PubMed:21596315}.Q96DE5APC16%Anaphase-promoting complex subunit 16eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20360068}. Nucleus {ECO:0000269|PubMed:20360068}.fcell division [GO:0051301]; mitotic nuclear division [GO:0007067]; protein ubiquitination [GO:0016567]< ?anaphase-promoting complex [GO:0005680]; cytoplasm [GO:0005737]FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:20360068}.P00167CYB5 Cytochrome b5SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.hydrogen ion transmembrane transport [GO:1902600]; L-ascorbic acid metabolic process [GO:0019852]; response to cadmium ion [GO:0046686]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]aldo-keto reductase (NADP) activity [GO:0004033]; cytochrome-c oxidase activity [GO:0004129]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; metal ion binding [GO:0046872]endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.Q6NXE6ARMC6%Armadillo repeat-containing protein 6P05204HMGN2&Non-histone chromosomal protein HMG-17SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10739259}. Cytoplasm {ECO:0000269|PubMed:10739259}. Note=Cytoplasmic enrichment upon phosphorylation.FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity). {ECO:0000250}.O60333KIF1BKinesin-like protein KIF1BSUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:16225668}. Note=Colocalizes with synaptophysin at synaptic cytoplasmic transport vesicles in the neurites of hippocampal neurons. {ECO:0000250}.xanterograde axon cargo transport [GO:0008089]; apoptotic process [GO:0006915]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; mitochondrion transport along microtubule [GO:0047497]; neuromuscular synaptic transmission [GO:0007274]; neuron-neuron synaptic transmission [GO:0007270]; vesicle-mediated transport [GO:0016192]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; kinesin binding [GO:0019894]; microtubule motor activity [GO:0003777]cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis. {ECO:0000269|PubMed:18334619}.P51636CAV2 Caveolin-2SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments. {ECO:0000250}.kcaveola assembly [GO:0070836]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of dopamine receptor signaling pathway [GO:0060161]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of GTPase activity [GO:0043547]; positive regulation of MAPK cascade [GO:0043410]; protein oligomerization [GO:0051259]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; regulation of mitotic nuclear division [GO:0007088]; skeletal muscle fiber development [GO:0048741]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle organization [GO:0016050]YD1 dopamine receptor binding [GO:0031748]; protein homodimerization activity [GO:0042803]acrosomal membrane [GO:0002080]; caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; transport vesicle [GO:0030133]kFUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}.O43933PEX1Peroxisome biogenesis factor 1microtubule-based peroxisome localization [GO:0060152]; peroxisome organization [GO:0007031]; protein import into peroxisome matrix [GO:0016558]; protein targeting to peroxisome [GO:0006625]ATPase activity, coupled [GO:0042623]; ATP binding [GO:0005524]; protein complex binding [GO:0032403]; protein C-terminus binding [GO:0008022]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]FUNCTION: Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.Q8IVG5SAM9L4Sterile alpha motif domain-containing protein 9-likecommon myeloid progenitor cell proliferation [GO:0035726]; endosomal vesicle fusion [GO:0034058]; hematopoietic progenitor cell differentiation [GO:0002244]; regulation of protein catabolic process [GO:0042176]; spleen development [GO:0048536]; stem cell division [GO:0017145]Q9UHL4DPP2Dipeptidyl peptidase 2SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15487984}. Cytoplasmic vesicle {ECO:0000269|PubMed:15487984}. Secreted {ECO:0000269|PubMed:15487984}.cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; vesicle [GO:0031982]jFUNCTION: Plays an important role in the degradation of some oligopeptides. {ECO:0000269|PubMed:15487984}.Q9NWZ5UCKL1Uridine-cytidine kinase-like 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12199906}. Nucleus {ECO:0000269|PubMed:12199906}. Note=EBNA3 induces isoform 1 translocation to the nucleus, w< hereas it does change isoform 3 location.NCTP salvage [GO:0044211]; UMP salvage [GO:0044206]; viral process [GO:0016032]>ATP binding [GO:0005524]; uridine kinase activity [GO:0004849]~FUNCTION: May contribute to UTP accumulation needed for blast transformation and proliferation. {ECO:0000269|PubMed:12199906}.Q15836VAMP3%Vesicle-associated membrane protein 3SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, synapse, synaptosome {ECO:0000250}.Ccalcium ion-dependent exocytosis [GO:0017156]; exocytosis [GO:0006887]; Golgi to plasma membrane protein transport [GO:0043001]; membrane fusion [GO:0061025]; negative regulation of secretion by cell [GO:1903531]; positive regulation of receptor recycling [GO:0001921]; protein complex assembly [GO:0006461]; retrograde transport, endosome to Golgi [GO:0042147]; SNARE complex assembly [GO:0035493]; substrate adhesion-dependent cell spreading [GO:0034446]; vesicle docking involved in exocytosis [GO:0006904]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; cell surface [GO:0009986]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytosol [GO:0005829]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule [GO:0030141]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]Q9NQ66PLCB1@1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250}.activation of meiosis involved in egg activation [GO:0060466]; cerebral cortex development [GO:0021987]; fat cell differentiation [GO:0045444]; G2/M transition of mitotic cell cycle [GO:0000086]; glutamate receptor signaling pathway [GO:0007215]; G-protein coupled acetylcholine receptor signaling pathway [GO:0007213]; inositol phosphate metabolic process [GO:0043647]; insulin-like growth factor receptor signaling pathway [GO:0048009]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-15-mediated signaling pathway [GO:0035723]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; lipid catabolic process [GO:0016042]; memory [GO:0007613]; negative regulation of monocyte extravasation [GO:2000438]; negative regulation of transcription, DNA-templated [GO:0045892]; phosphatidylinositol metabolic process [GO:0046488]; positive regulation of acrosome reaction [GO:2000344]; positive regulation of CD24 biosynthetic process [GO:2000560]; positive regulation of developmental growth [GO:0048639]; positive regulation of embryonic development [GO:0040019]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of GTPase activity [GO:0043547]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of JNK cascade [GO:0046330]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of fertilization [GO:0080154]; regulation of G-protein coupled receptor protein signaling pathway [GO:0008277]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]Wcalcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol phospholipase C activity [GO:0004435]; protein homodimerization activity [GO:0042803]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; nuclear chromatin [GO:0000790]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleus [GO:0005634]Q9Y4F1FARP17FERM, RhoGEF and pleckstrin domain-containing protein 1SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, synapse. Cell junction, synapse, synaptosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell membrane via interaction with CADM1. {ECO:0000250}.dendrite morphogenesis [GO:0048813]; negative regulation of phosphatase activity [GO:0010923]; positive regulation of GTPase activity [GO:0043547]; regulation of Rho protein signal transduction [GO:0035023]; synapse assembly [GO:0007416]xRac guanyl-nucleotide exchange factor activity [GO:0030676]; Rho guanyl-nucleotide exchange factor activity [GO:0005089]cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; filopodium [GO:0030175]; synapse [GO:0045202];FUNCTION: Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}.P08842STSSteryl-sulfatase@cellular protein metabolic process [GO:0044267]; epidermis development [GO:0008544]; female pregnancy [GO:0007565]; glycosphingolipid metabolic process [GO:0006687]; learning or memory [GO:0007611]; positive regulation of cell proliferation [GO:0008284]; post-translational protein modification [GO:0043687]; response to estrogen [GO:0043627]; response to peptide hormone [GO:0043434]; response to pH [GO:0009268]; skin development [GO:0043588]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]; steroid catabolic process [GO:0006706]vmetal ion binding [GO:0046872]; steryl-sulfatase activity [GO:0004773]; sulfuric ester hydrolase activity [GO:0008484]}endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]RFUNCTION: Conversion of sulfated steroid precursors to estrogens during pregnancy.Q96IF1AJUBA#LIM domain-containing protein ajubaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, P-body. Note=Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase. Preferentially co- localizes with cadherin-adhesive complexes at sites of cell-cell contacts. Colocalizes with GFI1 in the nucleus.calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cellular protein localization [GO:0034613]; focal adhesion assembly [GO:0048041]; G2/M transition of mitotic cell cycle [GO:0000086]; gene silencing by miRNA [GO:0035195]; glycerophospholipid biosynthetic process [GO:0046474]; lamellipodium assembly [GO:0030032]; mitotic cell cycle [GO:0000278]; negative regulation of hippo signaling [GO:0035331]; negative regulation of kinase activity [GO:0033673]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cellular biosynthetic process [GO:0031328]; positive regulation of gene silencing by miRNA [GO:2000637]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of protein complex assembly [GO:0031334]; < regulation of cell migration [GO:0030334]; regulation of cellular response to hypoxia [GO:1900037]; regulation of GTPase activity [GO:0043087]; response to hypoxia [GO:0001666]; transcription, DNA-templated [GO:0006351]; wound healing, spreading of epidermal cells [GO:0035313]alpha-catenin binding [GO:0045294]; chromatin binding [GO:0003682]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270](cell-cell junction [GO:0005911]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription factor complex [GO:0005667]$FUNCTION: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. {ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.Q8NG68TTLTubulin--tyrosine ligasecellular protein modification process [GO:0006464]; microtubule cytoskeleton organization [GO:0000226]; regulation of axon extension [GO:0030516]GATP binding [GO:0005524]; tubulin-tyrosine ligase activity [GO:0004835]FUNCTION: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. {ECO:0000250}.Q9BZL4PP12C,Protein phosphatase 1 regulatory subunit 12CSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:12923170}. Note=Along actomyosin filaments and stress fibers. {ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:12923170}.OFUNCTION: Regulates myosin phosphatase activity. {ECO:0000269|PubMed:11399775}.P59768GBG2AGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; blood coagulation [GO:0007596]; cell proliferation [GO:0008283]; cellular response to catecholamine stimulus [GO:0071870]; cellular response to glucagon stimulus [GO:0071377]; cellular response to prostaglandin E stimulus [GO:0071380]; energy reserve metabolic process [GO:0006112]; platelet activation [GO:0030168]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]TG-protein beta-subunit binding [GO:0031681]; signal transducer activity [GO:0004871]6FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction (By similarity). {ECO:0000250}.P49915GUAA$GMP synthase [glutamine-hydrolyzing]Jglutamine metabolic process [GO:0006541]; nucleobase-containing small molecule metabolic process [GO:0055086]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleobase metabolic process [GO:0006144]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; small molecule metabolic process [GO:0044281]ATP binding [GO:0005524]; GMP synthase (glutamine-hydrolyzing) activity [GO:0003922]; GMP synthase activity [GO:0003921]; pyrophosphatase activity [GO:0016462]FUNCTION: Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.Q9Y2W2WBP11WW domain-binding protein 11YSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.mRNA processing [GO:0006397]; positive regulation of protein targeting to mitochondrion [GO:1903955]; regulation of mitochondrion degradation [GO:1903146]; RNA splicing [GO:0008380]; rRNA processing [GO:0006364]poly(A) RNA binding [GO:0044822]; protein phosphatase type 1 regulator activity [GO:0008599]; single-stranded DNA binding [GO:0003697]; WW domain binding [GO:0050699]FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity. {ECO:0000269|PubMed:10593949, ECO:0000269|PubMed:11375989, ECO:0000269|PubMed:14640981}.Q96D96HVCN1 Voltage-gated hydrogen channel 1SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.(cellular response to pH [GO:0071467]; cellular response to zinc ion [GO:0071294]; multicellular organism reproduction [GO:0032504]; proton transport [GO:0015992]; response to pH [GO:0009268]; response to zinc ion [GO:0010043]; single fertilization [GO:0007338]; sperm-egg recognition [GO:0035036]fvoltage-gated cation channel activity [GO:0022843]; voltage-gated proton channel activity [GO:0030171]FUNCTION: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis. {ECO:0000269|PubMed:16554753, ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:22020278}.P19525E2AK2@Interferon-induced, double-stranded RNA-activated protein kinase9SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Note=Nuclear localization is elevated in acute leukemia, myelodysplastic syndrome (MDS), melanoma, breast, colon, prostate and lung cancer patient samples or cell lines as well as neurocytes from advanced Creutzfeldt-Jakob disease patients.lactivation of MAPKK activity [GO:0000186]; defense response to virus [GO:0051607]; endoplasmic reticulum unfolded protein response [GO:0030968]; evasion or tolerance by virus of host immune response [GO:0030683]; innate immune response [GO:0045087]; modulation by virus of host morphology or physiology [GO:0019048]; modulation by virus of host process [GO:0019054]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of translation [GO:0017148]; negative regulation of viral genome replication [GO:0045071]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production [GO:0001819]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of NIK/NF-kappaB signaling [GO:1901224]; positive regulation of stress-activated MAPK cascade [GO:0032874< ]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of hematopoietic progenitor cell differentiation [GO:1901532]; regulation of hematopoietic stem cell differentiation [GO:1902036]; regulation of hematopoietic stem cell proliferation [GO:1902033]; regulation of NLRP3 inflammasome complex assembly [GO:1900225]; regulation of protein phosphatase type 2A activity [GO:0034047]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998]; response to interferon-alpha [GO:0035455]; response to virus [GO:0009615]; transcription, DNA-templated [GO:0006351]; translation [GO:0006412]; viral life cycle [GO:0019058]ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; protein phosphatase type 2A regulator activity [GO:0008601]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribosome [GO:0005840]z FUNCTION: IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Can trigger apoptosis via FADD-mediated activation of CASP8. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin. {ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11836380, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15229216, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:19189853, ECO:0000269|PubMed:19229320, ECO:0000269|PubMed:19507191, ECO:0000269|PubMed:19840259, ECO:0000269|PubMed:20171114, ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:20685959, ECO:0000269|PubMed:21072047, ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:21710204, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:22381929, ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:22948139, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23115276, ECO:0000269|PubMed:23229543, ECO:0000269|PubMed:23372823, ECO:0000269|PubMed:23399035}.Q8N3X1FNBP4Formin-binding protein 4Q6ZW31SYDE1#Rho GTPase-activating protein SYDE1activation of GTPase activity [GO:0090630]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]Q96EB1ELP4Elongator complex protein 42chromatin organization [GO:0006325]; histone H3 acetylation [GO:0043966]; histone H4 acetylation [GO:0043967]; regulation of protein kinase activity [GO:0045859]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription elongation from RNA polymerase II promoter [GO:0006368]4phosphorylase kinase regulator activity [GO:0008607]cytoplasm [GO:0005737]; Elongator holoenzyme complex [GO:0033588]; histone acetyltransferase complex [GO:0000123]; nucleoplasm [GO:0005654]; transcription elongation factor complex [GO:0008023]FUNCTION: Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. {ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576, ECO:0000269|PubMed:16713582}.Q702N8XIRP1-Xin actin-binding repeat-containing protein 1mSUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}. Note=Colocalizes with actin stress fibers.Lactin cytoskeleton organization [GO:0030036]; heart development [GO:0007507]cell junction [GO:0030054]XFUNCTION: Protects actin filaments from depolymerization. {ECO:0000269|PubMed:15454575}.O60293ZC3H1*Zinc finger C3H1 domain-containing proteinP48200IREB2)Iron-responsive element-binding protein 2kcellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; metabolic process [GO:0008152]4 iron, 4 sulfur cluster binding [GO:0051539]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; translation repressor activity [GO:0030371]FUNCTION: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA. {ECO:0000269|PubMed:7983023}.Q8N1S5S39ABZinc transporter ZIP11cellular zinc ion homeostasis [GO:0006882]; zinc II ion transmembrane transport [GO:0071577]; zinc II ion transport [GO:0006829]Ucell [GO:0005623]; integral component of membrane [GO:0016021]; membrane [GO:0016020]>FUNCTION: May act as a zinc-influx transporter. {ECO:0000250}.Q9Y6A5TACC34Transforming acidic coiled-coil-containing protein 3astral microtubule organization [GO:0030953]; cell proliferation [GO:0008283]; cerebral cortex development [GO:0021987]; cytoplasmic sequestering of transcription factor [GO:0042994]; hemopoiesis [GO:0030097]; interkinetic nuclear migration [GO:0022027]; microtubule cytoskeleton organization [GO:0000226]; neurogenesis [GO:0022008]; regulation of cell cycle [GO:0051726]; regulation of microtubule-based process [GO:0032886]; response to hypoxia [GO:0001666]Vcentrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]SFUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May be involved in the control of cell growth and differentiation. May contribute to cancer. {ECO:0000250}.Q8NE00TM104Transmembrane protein 104Q9H7N4SFR19(Splicing factor, arginine/serine-rich 19smRNA processing [GO:0006397]; RNA splicing [GO:0008380]; transcripti< on from RNA polymerase II promoter [GO:0006366];FUNCTION: May function in pre-mRNA splicing. {ECO:0000250}.Q9UN86G3BP2/Ras GTPase-activating protein-binding protein 2}cytoplasmic sequestering of NF-kappaB [GO:0007253]; mRNA transport [GO:0051028]; Ras protein signal transduction [GO:0007265]|nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; receptor signaling complex scaffold activity [GO:0030159]ZFUNCTION: Probable scaffold protein that may be involved in mRNA transport. {ECO:0000305}.Q96RL7VP13A/Vacuolar protein sorting-associated protein 13AGolgi to endosome transport [GO:0006895]; locomotory behavior [GO:0007626]; nervous system development [GO:0007399]; protein localization [GO:0008104]; protein retention in Golgi apparatus [GO:0045053]; protein targeting to vacuole [GO:0006623]; social behavior [GO:0035176]idense core granule [GO:0031045]; extrinsic component of membrane [GO:0019898]; intracellular [GO:0005622]FUNCTION: May play a role in the control of protein cycling through the trans-Golgi network to early and late endosomes, lysosomes and plasma membrane.Q99973TEP1Telomerase protein component 1BSUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere._RNA-dependent DNA replication [GO:0006278]; telomere maintenance via recombination [GO:0000722]2ATP binding [GO:0005524]; RNA binding [GO:0003723]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; ribonucleoprotein complex [GO:0030529]; telomerase holoenzyme complex [GO:0005697]FUNCTION: Component of the telomerase ribonucleoprotein complex that is essential for the replication of chromosome termini. Also component of the ribonucleoprotein vaults particle, a multi-subunit structure involved in nucleo-cytoplasmic transport. Responsible for the localizing and stabilizing vault RNA (vRNA) association in the vault ribonucleoprotein particle. Binds to TERC (By similarity). {ECO:0000250}.Q9BPX3CND3Condensin complex subunit 3tSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.icell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; condensin complex [GO:0000796]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.Q9NUT2ABCB89ATP-binding cassette sub-family B member 8, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16259955}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16259955}.<transmembrane transport [GO:0055085]; transport [GO:0006810]ATPase activity, coupled to transmembrane movement of substances [GO:0042626]; ATP binding [GO:0005524]; transporter activity [GO:0005215]ATP-binding cassette (ABC) transporter complex [GO:0043190]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]P49447CY561Cytochrome b561uelectron transport chain [GO:0022900]; oxidation-reduction process [GO:0055114]; transmembrane transport [GO:0055085]ferric-chelate reductase activity [GO:0000293]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; transmembrane electron transfer carrier [GO:0022865]@FUNCTION: Secretory vesicle-specific electron transport protein.Q96GA3LTV1Protein LTV1 homologQ16610ECM1Extracellular matrix protein 1angiogenesis [GO:0001525]; biomineral tissue development [GO:0031214]; inflammatory response [GO:0006954]; negative regulation of bone mineralization [GO:0030502]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negative regulation of peptidase activity [GO:0010466]; ossification [GO:0001503]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; regulation of T cell migration [GO:2000404]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of type 2 immune response [GO:0002828]; signal transduction [GO:0007165]enzyme binding [GO:0019899]; laminin binding [GO:0043236]; protease binding [GO:0002020]; protein C-terminus binding [GO:0008022]; signal transducer activity [GO:0004871]extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578])FUNCTION: Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity. {ECO:0000269|PubMed:11165938, ECO:0000269|PubMed:11292659, ECO:0000269|PubMed:16512877}.Q9UHI6DDX20)Probable ATP-dependent RNA helicase DDX20SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; oogenesis [GO:0048477]; positive regulation of apoptotic process [GO:0043065]; regulation of steroid biosynthetic process [GO:0050810]; RNA processing [GO:0006396]; RNA secondary structure unwinding [GO:0010501]; spliceosomal snRNP assembly [GO:0000387]; spliceosomal tri-snRNP complex assembly [GO:0000244]ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; DNA binding [GO:0003677]; repressing transcription factor binding [GO:0070491]#cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]; transcriptional repressor complex [GO:0017053]FUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161}.Q15041AR6P1<ADP-ribosylation factor-like protein 6-interacting protein 18SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:10995579}; Multi-pass membrane protein {ECO:0000269|PubMed:10995579}. Endoplasmic r< eticulum membrane {ECO:0000269|PubMed:24076029}; Multi-pass membrane protein {ECO:0000269|PubMed:24076029}. Note=Predominantly localized to intracytoplasmic membranes.:cotranslational protein targeting to membrane [GO:0006613]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; Sec61 translocon complex [GO:0005784]xFUNCTION: May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation.Q96FJ2DYL2!Dynein light chain 2, cytoplasmicantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; apoptotic process [GO:0006915]; intrinsic apoptotic signaling pathway [GO:0097193]; microtubule-based process [GO:0007017]; organelle organization [GO:0006996]; positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [GO:1900740]; programmed cell death [GO:0012501]; synaptic target recognition [GO:0008039]; transport [GO:0006810]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cytosol [GO:0005829]; dynein complex [GO:0030286]; membrane [GO:0016020]; microtubule [GO:0005874]; myosin complex [GO:0016459]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; primary cilium [GO:0072372]FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.Q8N2S1LTBP48Latent-transforming growth factor beta-binding protein 4regulators(26)SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:16157329, ECO:0000269|PubMed:9660815}.extracellular matrix organization [GO:0030198]; growth hormone secretion [GO:0030252]; multicellular organismal development [GO:0007275]; protein folding [GO:0006457]; regulation of cell differentiation [GO:0045595]; regulation of cell growth [GO:0001558]; regulation of proteolysis [GO:0030162]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transforming growth factor beta receptor signaling pathway [GO:0007179]calcium ion binding [GO:0005509]; glycosaminoglycan binding [GO:0005539]; integrin binding [GO:0005178]; transforming growth factor beta-activated receptor activity [GO:0005024]; transforming growth factor beta binding [GO:0050431]cell [GO:0005623]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]&FUNCTION: May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM) (By similarity). {ECO:0000250}.Q9C040TRIM2%Tripartite motif-containing protein 23regulation of neuron apoptotic process [GO:0043523]FUNCTION: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. {ECO:0000250}.Q9UBH6XPR1/Xenotropic and polytropic retrovirus receptor 1YG-protein coupled receptor signaling pathway [GO:0007186]; response to virus [GO:0009615]G-protein coupled receptor activity [GO:0004930]; receptor activity [GO:0004872]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: May function in G-protein coupled signal transduction (By similarity). Potential receptor for xenotropic and polytropic murine leukemia retroviruses. {ECO:0000250, ECO:0000269|PubMed:9988277, ECO:0000269|PubMed:9990033}.Q9NPA8ENY2)Transcription and mRNA export factor ENY2SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03046, ECO:0000269|PubMed:22307388}. Nucleus, nuclear pore complex {ECO:0000255|HAMAP-Rule:MF_03046, ECO:0000269|PubMed:22307388}.chromatin organization [GO:0006325]; histone deubiquitination [GO:0016578]; mRNA export from nucleus [GO:0006406]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; positive regulation of transcription, DNA-templated [GO:0045893]; protein transport [GO:0015031]; transcription elongation from RNA polymerase II promoter [GO:0006368]|DUBm complex [GO:0071819]; nuclear pore [GO:0005643]; SAGA complex [GO:0000124]; transcription export complex 2 [GO:0070390]FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:21746879}.Q9Y605MOFA1!MORF4 family-associated protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}. Note=Colocalizes with MORF4L1 to cell nuclei. {ECO:0000269|PubMed:11500496, ECO:0000269|PubMed:12397079}.\nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]Q6IQ49SDE2Protein SDE2 homologP18846ATF1/Cyclic AMP-dependent transcription factor ATF-1cellular protein complex assembly [GO:0043623]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of DNA replication [GO:0045740]; positive regulation of neuron projection development [GO:0010976]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; response to cobalt ion [GO:0032025]; response to organic cyclic compound [GO:0014070]; stress-activated MAPK cascade [GO:0051403]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:0034162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]cATF1-ATF4 transcription factor complex [GO:1990590]; nucleoplasm [GO:0005654]; nucleu< s [GO:0005634]FUNCTION: This protein binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Binds to the Tax-responsive element (TRE) of HTLV-I. Mediates PKA-induced stimulation of CRE-reporter genes. Represses the expression of FTH1 and other antioxidant detoxification genes. Triggers cell proliferation and transformation. {ECO:0000269|PubMed:18794154, ECO:0000269|PubMed:20980392}.Q9ULE3DEN2A!DENN domain-containing protein 2ArSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20937701}. Note=Associated with actin filaments.positive regulation of GTPase activity [GO:0043547]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]4FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May play a role in late endosomes back to trans-Golgi network/TGN transport. {ECO:0000269|PubMed:20937701}.Q7Z7N9T179BTransmembrane protein 179BQ9HCJ1ANKH%Progressive ankylosis protein homologinorganic diphosphate transport [GO:0030505]; locomotory behavior [GO:0007626]; regulation of bone mineralization [GO:0030500]; skeletal system development [GO:0001501]; transmembrane transport [GO:0055085]inorganic diphosphate transmembrane transporter activity [GO:0030504]; inorganic phosphate transmembrane transporter activity [GO:0005315]; phosphate ion transmembrane transporter activity [GO:0015114]integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; outer membrane [GO:0019867]; plasma membrane [GO:0005886]~FUNCTION: Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter.Q8WVI0SMIM4!Small integral membrane protein 4P42695CNDD3Condensin-2 complex subunit D3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14532007}.cell division [GO:0051301]; chromosome separation [GO:0051304]; meiotic chromosome condensation [GO:0010032]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]Gchromatin binding [GO:0003682]; methylated histone binding [GO:0035064]condensed chromosome, centromeric region [GO:0000779]; germinal vesicle [GO:0042585]; membrane [GO:0016020]; nuclear condensin complex [GO:0000799]; nuclear pericentric heterochromatin [GO:0031618]; nucleoplasm [GO:0005654]FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. {ECO:0000269|PubMed:14532007}.Q8NHG7SVIP!Small VCP/p97-interacting proteinSUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.Unegative regulation of ER-associated ubiquitin-dependent protein catabolic process [GO:1903070]; negative regulation of protein complex assembly [GO:0031333]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; positive regulation of autophagy [GO:0010508]; positive regulation of protein lipidation [GO:1903061]BATPase binding [GO:0051117]; protein self-association [GO:0043621]anchored component of membrane [GO:0031225]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868]Q7Z7F0K0907UPF0469 protein KIAA0907Q86WV6STING&Stimulator of interferon genes protein{SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, perinuclear region. Cytoplasm. Note=In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited.activation of innate immune response [GO:0002218]; apoptotic process [GO:0006915]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to interferon-beta [GO:0035458]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; interferon-beta production [GO:0032608]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of protein binding [GO:0032092]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of type I interferon production [GO:0032481]; regulation of type I interferon production [GO:0032479]cyclic-di-GMP binding [GO:0035438]; cyclic-GMP-AMP binding [GO:0061507]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; transcription factor binding [GO:0008134]1cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Essential for the induction of IFN-beta in response to human herpes simplex virus 1 (HHV-1) infection. {ECO:0000269|PubMed:18724357, ECO:0000269|PubMed:18818105, ECO:0000269|PubMed:19433799, ECO:0000269|PubMed:19776740, ECO:0000269|PubMed:21074459, ECO:0000269|PubMed:21947006, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:23258412, ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722158}.Q14571ITPR2,Inositol 1,4,5-trisphosphate receptor type 2activation of phospholipase C activity [GO:0007202]; blood coagulation [GO:0007596]; cellular response to cAMP [GO:0071320]; cellular response to ethanol [GO:0071361]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; innate immune response [GO:0045087]; inositol phosphate-mediated signaling [GO:0048016]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; regulation of insulin secretion [GO:0050796]; response to hypoxia [GO:0001666]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; transport [GO:0006810]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]calcium ion transmembrane transporter activity [GO:0015085]; inositol 1,4,5-trisphosphate-sensitive calcium-release chann< el activity [GO:0005220]; phosphatidylinositol binding [GO:0035091]*cell cortex [GO:0005938]; endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]; platelet dense tubular network membrane [GO:0031095]; receptor complex [GO:0043235]; sarcoplasmic reticulum membrane [GO:0033017]FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA (By similarity). {ECO:0000250|UniProtKB:Q9Z329}.Q9P2H5UBP35(Ubiquitin carboxyl-terminal hydrolase 35Q9NRD1FBX6F-box only protein 6Protein processing in ER(157)>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19716789}.MDNA damage checkpoint [GO:0000077]; DNA repair [GO:0006281]; ER-associated ubiquitin-dependent protein catabolic process [GO:0030433]; glycoprotein catabolic process [GO:0006516]; proteolysis [GO:0006508]; response to unfolded protein [GO:0006986]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]tcarbohydrate binding [GO:0030246]; glycoprotein binding [GO:0001948]; ubiquitin protein ligase activity [GO:0061630]FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranlocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication. {ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:19716789}.P11047LAMC1Laminin subunit gamma-1axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; endoderm development [GO:0007492]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581]; positive regulation of epithelial cell proliferation [GO:0050679]; protein complex assembly [GO:0006461]; substrate adhesion-dependent cell spreading [GO:0034446] basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-10 complex [GO:0043259]; laminin-11 complex [GO:0043260]; laminin-1 complex [GO:0005606]Q15021CND1Condensin complex subunit 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.<chromatin binding [GO:0003682]; histone binding [GO:0042393]>condensed chromosome [GO:0000793]; condensed chromosome, centromeric region [GO:0000779]; condensin complex [GO:0000796]; condensin core heterodimer [GO:0000797]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear condensin complex [GO:0000799]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain. {ECO:0000269|PubMed:11136719}.P08069IGF1R%Insulin-like growth factor 1 receptorSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17524361}; Single-pass type I membrane protein {ECO:0000269|PubMed:17524361}.jaxonogenesis [GO:0007409]; brain development [GO:0007420]; epidermis development [GO:0008544]; establishment of cell polarity [GO:0030010]; exocrine pancreas development [GO:0031017]; immune response [GO:0006955]; inactivation of MAPKK activity [GO:0051389]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin receptor signaling pathway [GO:0008286]; male sex determination [GO:0030238]; mammary gland development [GO:0030879]; negative regulation of apoptotic process [GO:0043066]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; peptidyl-tyrosine autophosphorylation [GO:0038083]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cytokinesis [GO:0032467]; positive regulation of DNA replication [GO:0045740]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of steroid hormone biosynthetic process [GO:0090031]; prostate gland epithelium morphogenesis [GO:0060740]; protein autophosphorylation [GO:0046777]; protein heterooligomerization [GO:0051291]; protein tetramerization [GO:0051262]; regulation of JNK cascade [GO:0046328]; response to vitamin E [GO:0033197]; signal transduction [GO:0007165]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin-like growth factor-activated receptor activity [GO:0005010]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin receptor binding [GO:0005158]; insulin receptor substrate binding [GO:0043560]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein tyrosine kinase activity [GO:0004713]caveola [GO:0005901]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] FUNCTION: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphoryl< ation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.; FUNCTION: When present in a hybrid receptor with INSR, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.Q96DE0NUD16U8 snoRNA-decapping enzymeSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus. Cytoplasm. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity). {ECO:0000250}.adenosine to inosine editing [GO:0006382]; dephosphorylation [GO:0016311]; dITP catabolic process [GO:0035863]; IDP catabolic process [GO:0046709]; mRNA catabolic process [GO:0006402]; negative regulation of rRNA processing [GO:2000233]; nucleobase-containing small molecule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; positive regulation of cell cycle process [GO:0090068]; positive regulation of cell proliferation [GO:0008284]; positive regulation of double-strand break repair [GO:2000781]; proteolysis [GO:0006508]; small molecule metabolic process [GO:0044281]; snoRNA catabolic process [GO:0016077]; XDP catabolic process [GO:1901639]Dcobalt ion binding [GO:0050897]; dIDP diphosphatase activity [GO:0097383]; dITP diphosphatase activity [GO:0035870]; GTP binding [GO:0005525]; inosine-diphosphatase activity [GO:0090450]; ITP binding [GO:1901641]; m7G(5')pppN diphosphatase activity [GO:0050072]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; metalloexopeptidase activity [GO:0008235]; mRNA binding [GO:0003729]; nucleotide phosphatase activity, acting on free nucleotides [GO:0098519]; protein homodimerization activity [GO:0042803]; snoRNA binding [GO:0030515]; XTP binding [GO:1901640]FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. {ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011}.Q9H0H0INT2Integrator complex subunit 2integral component of membrane [GO:0016021]; integrator complex [GO:0032039]; intracellular [GO:0005622]; membrane [GO:0016020]; nuclear membrane [GO:0031965]Q8WTW4NPRL2*Nitrogen permease regulator 2-like proteincellular response to amino acid starvation [GO:0034198]; negative regulation of kinase activity [GO:0033673]; negative regulation of TOR signaling [GO:0032007]; positive regulation of GTPase activity [GO:0043547]; protein phosphorylation [GO:0006468]LGTPase activator activity [GO:0005096]; protein kinase activity [GO:0004672]Iml1 complex [GO:1990130]FUNCTION: Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling. Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr-9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor. Suppresses cell growth and enhances sensitivity to various anticancer drugs. As a component of the GATOR1 complex, inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. {ECO:0000269|PubMed:18616680, ECO:0000269|PubMed:23723238}.Q9Y5J5PHLA31Pleckstrin homology-like domain family A member 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19203586}. Membrane {ECO:0000269|PubMed:19203586}; Peripheral membrane protein {ECO:0000269|PubMed:19203586}. anatomical structure morphogenesis [GO:0009653]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; negative regulation of protein kinase B signaling [GO:0051898]; positive regulation of apoptotic process [GO:0043065]_phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-5-phosphate binding [GO:0010314]FUNCTION: p53/TP53-regulated repressor of Akt/AKT1 signaling. Represses AKT1 by preventing AKT1-binding to membrane lipids, thereby inhibiting AKT1 translocation to the cellular membrane and activation. Contributes to p53/TP53-dependent apoptosis by repressing AKT1 activity. Its direct transcription regulation by p53/TP53 may explain how p53/TP53 can negatively regulate AKT1. May act as a tumor suppressor. {ECO:0000269|PubMed:19203586}.Q15645PCH2&Pachytene checkpoint protein 2 homologdouble-strand break repair [GO:0006302]; female meiosis I [GO:0007144]; male meiosis I [GO:0007141]; oocyte maturation [GO:0001556]; oogenesis [GO:0048477]; reciprocal meiotic recombination [GO:0007131]; regulation of nucleic acid-templated transcription [GO:1903506]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; transcription from RNA polymerase II promoter [GO:0006366]nATP binding [GO:0005524]; identical protein binding [GO:0042802]; tran< scription cofactor activity [GO:0003712]9male germ cell nucleus [GO:0001673]; nucleus [GO:0005634]%FUNCTION: Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes (By similarity). {ECO:0000250}.Q86SZ2TPC6B/Trafficking protein particle complex subunit 6BdFUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. {ECO:0000250}.Q13151ROA0*Heterogeneous nuclear ribonucleoprotein A03'-UTR-mediated mRNA stabilization [GO:0070935]; gene expression [GO:0010467]; inflammatory response [GO:0006954]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; response to lipopolysaccharide [GO:0032496]; RNA splicing [GO:0008380]AU-rich element binding [GO:0017091]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; RNA binding [GO:0003723]FUNCTION: mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs. {ECO:0000269|PubMed:12456657}.Q8IVF7FMNL3Formin-like protein 3SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}. Cell membrane {ECO:0000269|PubMed:22275430}; Lipid-anchor {ECO:0000255}. Note=Enriched in lamellipodia.actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; regulation of cell shape [GO:0008360]; small GTPase mediated signal transduction [GO:0007264].GTPase activating protein binding [GO:0032794]FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Required for developmental angiogenesis (By similarity). In this process, required for microtubule reorganization and for efficient endothelial cell elongation. In quiescent endothelial cells, triggers rearrangement of the actin cytoskeleton, but does not alter microtubule alignement. {ECO:0000250|UniProtKB:Q6NXC0, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22275430}.Q9UL63MKLN1MuskelinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O89050}. Cell projection, ruffle {ECO:0000250|UniProtKB:O89050}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O89050}. Note=Colocalizes with actin fibers in the cell cortex. {ECO:0000250|UniProtKB:O89050}.actin cytoskeleton reorganization [GO:0031532]; cell-matrix adhesion [GO:0007160]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165]Ccell cortex [GO:0005938]; cytosol [GO:0005829]; ruffle [GO:0001726]FUNCTION: Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1. {ECO:0000250|UniProtKB:O89050}.O75190DNJB6!DnaJ homolog subfamily B member 6fSUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Cytoplasm, myofibril, sarcomere, Z line.actin cytoskeleton organization [GO:0030036]; cellular response to heat [GO:0034605]; chorio-allantoic fusion [GO:0060710]; chorion development [GO:0060717]; extracellular matrix organization [GO:0030198]; intermediate filament organization [GO:0045109]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of inclusion body assembly [GO:0090084]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of ATPase activity [GO:0032781]; protein folding [GO:0006457]; protein localization to nucleus [GO:0034504]; regulation of cellular response to heat [GO:1900034]; syncytiotrophoblast cell differentiation involved in labyrinthine layer development [GO:0060715]ATPase activator activity [GO:0001671]; chaperone binding [GO:0051087]; DNA binding [GO:0003677]; heat shock protein binding [GO:0031072]; unfolded protein binding [GO:0051082]cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]FUNCTION: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity. {ECO:0000269|PubMed:10954706, ECO:0000269|PubMed:11896048, ECO:0000269|PubMed:20159555, ECO:0000269|PubMed:22366786}.P55042RADGTP-binding protein RADgnegative regulation of cell growth [GO:0030308]; small GTPase mediated signal transduction [GO:0007264]FUNCTION: May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents. Regulates voltage-dependent L-type calcium channel subunit alpha-1C trafficking to the cell membrane (By similarity). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D. {ECO:0000250, ECO:0000269|PubMed:18056528}.Q9NUS5AP5S1AP-5 complex subunit sigma-1SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22022230}. Late endosome membrane {ECO:0000305|PubMed:22022230}; Peripheral membrane protein {ECO:0000305|PubMed:22022230}; Cytoplasmic side {ECO:0000305|PubMed:22022230}. Lysosome membrane {ECO:0000305|PubMed:22022230}; Peripheral membrane protein {ECO:0000305|PubMed:22022230}; Cytoplasmic side {ECO:0000305|PubMed:22022230}.double-strand break repair via homologous recombination [GO:0000724]; endosomal transport [GO:0016197]; protein transport [GO:0015031] AP-type membrane coat adaptor complex [GO:0030119]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862, it is required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}.O43520AT8B1#Phospholipid-transporting ATPase IC5SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Apical cell membrane. Cell projection, stereocilium {ECO:0000250}. Endoplasmic reticulum. Golgi apparatus. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. Localizes to apical membranes in epithelial cells.bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; drug transmembrane transport [GO:0006855]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; ion transmembrane transport [GO:0034220]; negative regulation of transcription, DNA-templated [GO:0045892]; phospholipid translocation [GO:0045332]; regulation of microvillus assembly [GO:0032534]; sensory perception of sound [GO:0007605]; transmembrane transport [GO:0055085]; vestibulocochlear nerve formation [GO:0021650]ATP binding [GO:0005524]; cardiolipin binding [GO:1901612]; magnesium ion binding [GO:0000287]; phospholipid-translocating ATPase activity [GO:0004012]apical plasma membrane [GO:0016324]< ; brush border membrane [GO:0031526]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury. {ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20512993}.Q13148TADBPTAR DNA-binding protein 43:SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17023659, ECO:0000269|PubMed:17481916}. Note=In patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis, it is absent from the nucleus of affected neurons but it is the primary component of cytoplasmic ubiquitin-positive inclusion bodies.g3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA processing [GO:0006397]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of gene expression [GO:0010629]; negative regulation of protein phosphorylation [GO:0001933]; nuclear fragmentation involved in apoptotic nuclear change [GO:0030264]; nuclear inner membrane organization [GO:0071765]; positive regulation of insulin secretion [GO:0032024]; regulation of cell cycle [GO:0051726]; response to endoplasmic reticulum stress [GO:0034976]; RNA splicing [GO:0008380]; transcription from RNA polymerase II promoter [GO:0006366]double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; sequence-specific DNA binding transcription factor activity [GO:0003700]cytoplasm [GO:0005737]; interchromatin granule [GO:0035061]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726]FUNCTION: DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR. {ECO:0000269|PubMed:11285240, ECO:0000269|PubMed:17481916}.O76054S14L2SEC14-like protein 2SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.positive regulation of transcription, DNA-templated [GO:0045893]; regulation of cholesterol biosynthetic process [GO:0045540]; transcription, DNA-templated [GO:0006351]dphospholipid binding [GO:0005543]; transporter activity [GO:0005215]; vitamin E binding [GO:0008431]}cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]FUNCTION: Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.Q9UK99FBX3F-box only protein 3^SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with PML at the peripheries of nuclear bodies.FUNCTION: Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. {ECO:0000269|PubMed:18809579}.Q969M3YIPF5 Protein YIPF5!SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle. Note=Enriched at the endoplasmic reticulum exit sites. Incorporated into COPII coated vesicles.protein transport [GO:0015031]; regulation of ER to Golgi vesicle-mediated transport [GO:0060628]; vesicle-mediated transport [GO:0016192]endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle [GO:0030134]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]FUNCTION: Plays a role in transport between endoplasmic reticulum and Golgi. {ECO:0000269|PubMed:11489904, ECO:0000269|PubMed:15611160}.P301542AABPSerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoformapoptotic process involved in morphogenesis [GO:0060561]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; protein complex assembly [GO:0006461]>extracellular exosome [GO:0070062]; membrane raft [GO:0045121]FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.A6NDJ8RB43L,Putative Rab-43-like protein ENSP00000330714P48436SOX9Transcription factor SOX-9astrocyte fate commitment [GO:0060018]; branching involved in ureteric bud morphogenesis [GO:0001658]; bronchus cartilage development [GO:0060532]; cAMP-mediated signaling [GO:0019933]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate specification [GO:0001708]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to heparin [GO:0071504]; cellular response to interleukin-1 [GO:0071347]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation involved in endochondral bone morphogenesis [GO:0003413]; chondrocyte hypertrophy [GO:0003415]; chromatin remodeling [GO:0006338]; cochlea morphogenesis [GO:0090103]; cytoskeleton organization [GO:0007010]; endocardial cushion morphogenesis [GO:0003203]; endocrine pancreas development [GO:0031018]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation involved in prostatic bud elongation [GO:0060517]; epithelial to mesenchymal transition [GO:0001837]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; ERK1 and ERK2 cascade [GO:0070371]; extracellular matrix organization [GO:0030198]; hair follicle development [GO:0001< 942]; Harderian gland development [GO:0070384]; heart valve development [GO:0003170]; heart valve formation [GO:0003188]; heart valve morphogenesis [GO:0003179]; intestinal epithelial structure maintenance [GO:0060729]; intrahepatic bile duct development [GO:0035622]; limb bud formation [GO:0060174]; lung epithelial cell differentiation [GO:0060487]; lung smooth muscle development [GO:0061145]; male germ-line sex determination [GO:0019100]; male gonad development [GO:0008584]; mammary gland development [GO:0030879]; metanephric nephron tubule formation [GO:0072289]; morphogenesis of a branching epithelium [GO:0061138]; negative regulation of apoptotic process [GO:0043066]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of bone mineralization [GO:0030502]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of epithelial cell differentiation [GO:0030857]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of immune system process [GO:0002683]; negative regulation of mesenchymal cell apoptotic process [GO:2001054]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of ossification [GO:0030279]; negative regulation of photoreceptor cell differentiation [GO:0046533]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neural crest cell development [GO:0014032]; notochord development [GO:0030903]; nucleosome assembly [GO:0006334]; oligodendrocyte differentiation [GO:0048709]; ossification [GO:0001503]; otic vesicle formation [GO:0030916]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cell proliferation involved in heart morphogenesis [GO:2000138]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of kidney development [GO:0090184]; positive regulation of male gonad development [GO:2000020]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of mesenchymal stem cell differentiation [GO:2000741]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; prostate gland development [GO:0030850]; protein complex assembly [GO:0006461]; protein kinase B signaling [GO:0043491]; protein localization to nucleus [GO:0034504]; regulation of apoptotic process [GO:0042981]; regulation of branching involved in lung morphogenesis [GO:0061046]; regulation of cell adhesion [GO:0030155]; regulation of cell cycle process [GO:0010564]; regulation of cell proliferation [GO:0042127]; regulation of cell proliferation involved in tissue homeostasis [GO:0060784]; regulation of epithelial cell proliferation involved in lung morphogenesis [GO:2000794]; renal vesicle induction [GO:0072034]; retina development in camera-type eye [GO:0060041]; retinal rod cell differentiation [GO:0060221]; Sertoli cell development [GO:0060009]; Sertoli cell differentiation [GO:0060008]; signal transduction [GO:0007165]; single organismal cell-cell adhesion [GO:0016337]; skeletal system development [GO:0001501]; somatic stem cell maintenance [GO:0035019]; spermatogenesis [GO:0007283]; tissue homeostasis [GO:0001894]; trachea cartilage development [GO:0060534]; transcription from RNA polymerase II promoter [GO:0006366]; ureter morphogenesis [GO:0072197]; ureter smooth muscle cell differentiation [GO:0072193]; ureter urothelium development [GO:0072190]chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; enhancer binding [GO:0035326]; enhancer sequence-specific DNA binding [GO:0001158]; pre-mRNA intronic binding [GO:0097157]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase activity [GO:0004672]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [GO:0003705]; sequence-specific DNA binding transcription factor activity [GO:0003700]nuclear transcription factor complex [GO:0044798]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Plays an important role in the normal skeletal development. May regulate the expression of other genes involved in chondrogenesis by acting as a transcription factor for these genes.P53675CLH2Clathrin heavy chain 2=SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000250}.anatomical structure morphogenesis [GO:0009653]; intracellular protein transport [GO:0006886]; mitotic nuclear division [GO:0007067]; positive regulation of glucose import [GO:0046326]; receptor-mediated endocytosis [GO:0006898]; signal transduction [GO:0007165]Rsignal transducer activity [GO:0004871]; structural molecule activity [GO:0005198]2clathrin-coated vesicle [GO:0030136]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; coated pit [GO:0005905]; coated vesicle [GO:0030135]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; spindle [GO:0005819]; trans-Golgi network [GO:0005802]FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network (By similarity). {ECO:0000250}.Q9UQB8BAIP2<Brain-specific angiogenesis inhibitor 1-associated protein 2SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Note=Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membrane ruffles. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.eactin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; axonogenesis [GO:0007409]; dendrite development [GO:0016358]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; insulin receptor signaling pathway [GO:0008286]; plasma membrane organization [GO:0007009]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of dendritic spine morphogenesis [GO:0061003]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of synaptic plasticity [GO:0048167]; response to bacterium [GO:0009617]; small GTPase mediated signal transduction [GO:0007264]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]cytoskeletal adaptor activity [GO:0008093]; identical protein binding [GO:0042802]; proline-rich region binding [GO:0070064]; protein C-terminus binding [GO:0008022]\cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; neuronal cell b< ody [GO:0043025]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; secretory granule [GO:0030141]FUNCTION: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions. {ECO:0000269|PubMed:11130076, ECO:0000269|PubMed:11696321, ECO:0000269|PubMed:14752106, ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19366662}.Q13825AUHM-Methylglutaconyl-CoA hydratase, mitochondrialbranched-chain amino acid catabolic process [GO:0009083]; cellular nitrogen compound metabolic process [GO:0034641]; leucine catabolic process [GO:0006552]; small molecule metabolic process [GO:0044281]enoyl-CoA hydratase activity [GO:0004300]; methylglutaconyl-CoA hydratase activity [GO:0004490]; mRNA 3'-UTR binding [GO:0003730]eFUNCTION: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs. {ECO:0000269|PubMed:11738050, ECO:0000269|PubMed:12434311, ECO:0000269|PubMed:12655555, ECO:0000269|PubMed:7892223}.P48681NESTNestinIbrain development [GO:0007420]; cell projection morphogenesis [GO:0048858]; central nervous system development [GO:0007417]; embryonic camera-type eye development [GO:0031076]; G2/M transition of mitotic cell cycle [GO:0000086]; negative regulation of catalytic activity [GO:0043086]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein binding [GO:0032091]; positive regulation of intermediate filament depolymerization [GO:0030844]; positive regulation of neural precursor cell proliferation [GO:2000179]; stem cell proliferation [GO:0072089]Uintermediate filament binding [GO:0019215]; structural molecule activity [GO:0005198]kcytoplasm [GO:0005737]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]FUNCTION: Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). {ECO:0000250}.Q6ZSZ5ARHGI)Rho guanine nucleotide exchange factor 18iSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15558029}. Note=Colocalizes with actin stress fibers.&actin cytoskeleton organization [GO:0030036]; apoptotic signaling pathway [GO:0097190]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; regulation of cell shape [GO:0008360]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; transforming growth factor beta receptor signaling pathway [GO:0007179]apical part of cell [GO:0045177]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. Also act as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. {ECO:0000269|PubMed:11085924, ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:15558029}.Q8WWM7ATX2LAtaxin-2-like proteinxSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11784712}; Peripheral membrane protein {ECO:0000269|PubMed:11784712}.jregulation of cytoplasmic mRNA processing body assembly [GO:0010603]; stress granule assembly [GO:0034063]rcytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; membrane [GO:0016020]; nuclear speck [GO:0016607]Q9BSY9DESI2Desumoylating isopeptidase 2ZFUNCTION: Protease which may deconjugate SUMO from some substrate proteins. {ECO:0000250}.Q9P0K7RAI14 AnkycorbinrSUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11042181, ECO:0000269|PubMed:16729964}. Note=Associated with the cortical actin cytoskeleton structures in terminal web and cell-cell adhesion sites and stress fibers (By similarity). Predominantly nuclear in nonconfluent cells. {ECO:0000250}.actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q5TAQ9DCAF8"DDB1- and CUL4-associated factor 8ISUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22500989}. Cytoplasm {ECO:0000269|PubMed:22500989}. Note=It shuttles between the nucleus and the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under the regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm is XPO1 dependent. {ECO:0000269|PubMed:22500989}.`Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; nucleus [GO:0005634]FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.Q9NZ56FMN2Formin-2_SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Cytoplasm, cytosol. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Nucleus, nucleolus. Note=Recruited to the membranes via its interaction with SPIRE1. Colocalizes with the actin cytoskeleton. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity). {ECO:0000250}.cellular response to DNA damage stimulus [GO:0006974]; cellular response to hypoxia [GO:0071456]; establishment of meiotic spindle localization [GO:0051295]; formin-nucleated actin cable assembly [GO:0070649]; homologous chromosome movement towards spindle pole involved in homologous chromosome segregation [GO:0051758]; intracellular signal transduction [GO:0035556]; intracellular transport [GO:0046907]; multicellular organismal development [GO:0007275]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein catabolic process [GO:0042177]; oogenesis [GO:0048477]; polar body extrusion after meiotic divisions [GO:0040038]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]cell cortex [GO:0005938]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; microvillus [GO:0005902]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; spindle [GO:0005819];FUNCTION: Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intrace< llular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation. {ECO:0000250, ECO:0000269|PubMed:22330775, ECO:0000269|PubMed:23375502}.Q9Y5J1UTP184U3 small nucleolar RNA-associated protein 18 homologQ6DRA6H2B2DPutative histone H2B type 2-DO43447PPIH%Peptidyl-prolyl cis-trans isomerase HSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9570313}. Cytoplasm {ECO:0000269|PubMed:9570313}. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.mRNA splicing, via spliceosome [GO:0000398]; positive regulation of viral genome replication [GO:0045070]; protein complex assembly [GO:0006461]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; ribonucleoprotein complex binding [GO:0043021]cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; spliceosomal complex [GO:0005681]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:9570313}.P35749MYH11 Myosin-11SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Thick filaments of the myofibrils.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; axon guidance [GO:0007411]; cardiac muscle fiber development [GO:0048739]; elastic fiber assembly [GO:0048251]; ephrin receptor signaling pathway [GO:0048013]; muscle contraction [GO:0006936]; skeletal muscle myosin thick filament assembly [GO:0030241]; small GTPase mediated signal transduction [GO:0007264]; smooth muscle contraction [GO:0006939]dATP binding [GO:0005524]; motor activity [GO:0003774]; structural constituent of muscle [GO:0008307]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; melanosome [GO:0042470]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]FUNCTION: Muscle contraction.Q15758AAAT#Neutral amino acid transporter B(0)SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.amino acid transport [GO:0006865]; glutamine transport [GO:0006868]; ion transport [GO:0006811]; neutral amino acid transport [GO:0015804]; transmembrane transport [GO:0055085]L-glutamine transmembrane transporter activity [GO:0015186]; neutral amino acid transmembrane transporter activity [GO:0015175]; receptor activity [GO:0004872]; sodium:dicarboxylate symporter activity [GO:0017153]; virus receptor activity [GO:0001618]extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]iFUNCTION: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349). {ECO:0000269|PubMed:10051606, ECO:0000269|PubMed:10196349, ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:23492904}.Q32P41TRM5'tRNA (guanine(37)-N1)-methyltransferaseSUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.?tRNA (guanine(37)-N(1))-methyltransferase activity [GO:0052906]aFUNCTION: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.Q13573SNW1SNW domain-containing protein 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12840015}.cellular response to retinoic acid [GO:0071300]; gene expression [GO:0010467]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of histone H3-K4 methylation [GO:0051571]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of neurogenesis [GO:0050769]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of vitamin D receptor signaling pathway [GO:0070564]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; regulation of vitamin D receptor signaling pathway [GO:0070562]; retinoic acid receptor signaling pathway [GO:0048384]; skeletal muscle cell differentiation [GO:0035914]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]; viral process [GO:0016032]>Notch binding [GO:0005112]; nuclear hormone receptor binding [GO:0035257]; poly(A) RNA binding [GO:0044822]; retinoic acid receptor binding [GO:0042974]; SMAD binding [GO:0046332]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; vitamin D receptor binding [GO:0042809]catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]FUNCTION: Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD. Proposed to be involved in transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed promoters. Is recruited by HIV-1 Tat to Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription by < recruitment of MYC, MEN1 and TRRAP to the HIV promoter. Functions as a splicing factor in pre-mRNA splicing. Is required in the specific splicing of CDKN1A pre-mRNA; the function probbaly involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. {ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:14985122, ECO:0000269|PubMed:15194481, ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:9632709}.Q5W0Z9ZDH20%Probable palmitoyltransferase ZDHHC20endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]Q9NX70MED296Mediator of RNA polymerase II transcription subunit 29<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15555573}.7mediator complex [GO:0016592]; nucleoplasm [GO:0005654]'FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:15555573}.P27986P85A6Phosphatidylinositol 3-kinase regulatory subunit alpha B cell differentiation [GO:0030183]; blood coagulation [GO:0007596]; cellular glucose homeostasis [GO:0001678]; cellular response to insulin stimulus [GO:0032869]; cellular response to UV [GO:0034644]; epidermal growth factor receptor signaling pathway [GO:0007173]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; growth hormone receptor signaling pathway [GO:0060396]; innate immune response [GO:0045087]; insulin-like growth factor receptor signaling pathway [GO:0048009]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; leukocyte migration [GO:0050900]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of osteoclast differentiation [GO:0045671]; neurotrophin TRK receptor signaling pathway [GO:0048011]; NFAT protein import into nucleus [GO:0051531]; phosphatidylinositol 3-kinase signaling [GO:0014065]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; platelet activation [GO:0030168]; positive regulation of cell migration [GO:0030335]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of establishment of protein localization to plasma membrane [GO:0090004]; positive regulation of glucose import [GO:0046326]; positive regulation of glucose import in response to insulin stimulus [GO:2001275]; positive regulation of RNA splicing [GO:0033120]; positive regulation of transcription factor import into nucleus [GO:0042993]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; protein phosphorylation [GO:0006468]; protein stabilization [GO:0050821]; regulation of phosphatidylinositol 3-kinase activity [GO:0043551]; regulation of stress fiber assembly [GO:0051492]; response to endoplasmic reticulum stress [GO:0034976]; small molecule metabolic process [GO:0044281]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral process [GO:0016032]b1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; ErbB-3 class receptor binding [GO:0043125]; insulin binding [GO:0043559]; insulin-like growth factor receptor binding [GO:0005159]; insulin receptor binding [GO:0005158]; insulin receptor substrate binding [GO:0043560]; neurotrophin TRKA receptor binding [GO:0005168]; phosphatidylinositol 3-kinase binding [GO:0043548]; phosphatidylinositol 3-kinase regulator activity [GO:0035014]; protein phosphatase binding [GO:0019903]; transcription factor binding [GO:0008134]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]ccell-cell junction [GO:0005911]; cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum membrane [GO:1990578]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; plasma membrane [GO:0005886]FUNCTION: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed:17626883, PubMed:19805105, PubMed:7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress-and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348923). {ECO:0000269|PubMed:17626883, ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:7518429}.Q9HA77SYCM-Probable cysteine--tRNA ligase, mitochondrialdATP binding [GO:0005524]; cysteine-tRNA ligase activity [GO:0004817]; metal ion binding [GO:0046872]Q9Y625GPC6 Glypican-6SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: Secreted glypican-6: Secreted, extracellular space {ECO:0000250}.carbohydrate metabolic process [GO:0005975]; cell migration [GO:0016477]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; phototransduction, visible light [GO:0007603]; retinoid metabolic process [GO:0001523]; small molecule metabolic process [GO:0044281]anchored component of membrane [GO:0031225]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; integral component of plasma membrane [GO:0005887]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]6FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases (By similarity). Enhances migration and invasion of cancer cells through WNT5A signaling. {ECO:0000250, ECO:0000269|PubMed:21871017}.Q9C0D2K1731Centrosomal protein KIAA1731USUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20844083}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25131205}. Note=Associates with both of the converted centrioles during G1 but becomes more enriched at the newly formed daughter (or unconverted) centrioles during S, G2, and early M phases. Colocalizes with SASS6 and CEP250 proteins (Pub< Med:25131205). Colocalizes with centriolar acetylated tubulin (PubMed:20844083). {ECO:0000269|PubMed:20844083, ECO:0000269|PubMed:25131205}.6positive regulation of organelle assembly [GO:1902117]bcentriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]FUNCTION: Centriole-enriched protein that mediates centriole-to-centrosome conversion at late mitosis, but is dispensable for cartwheel removal or centriole disengagement. {ECO:0000269|PubMed:20844083, ECO:0000269|PubMed:25131205}.Q9H082RB33BRas-related protein Rab-33BSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18448665}.autophagy [GO:0006914]; intra-Golgi vesicle-mediated transport [GO:0006891]; negative regulation of constitutive secretory pathway [GO:1903434]; protein targeting to Golgi [GO:0000042]; Rab protein signal transduction [GO:0032482]; regulation of autophagosome assembly [GO:2000785]; regulation of Golgi organization [GO:1903358]; regulation of retrograde vesicle-mediated transport, Golgi to ER [GO:2000156]; skeletal system morphogenesis [GO:0048705]wextracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]FUNCTION: Protein transport. Acts, in coordination with RAB6A, to regulate intra-Golgi retrograde trafficking. It is involved in autophagy, acting as a modulator of autophagosome formation. {ECO:0000269|PubMed:20163571}.O60566BUB1B<Mitotic checkpoint serine/threonine-protein kinase BUB1 beta$SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic in interphase cells. Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and CASC5.anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031145]; apoptotic process [GO:0006915]; cell division [GO:0051301]; cell proliferation [GO:0008283]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly checkpoint [GO:0007094]; negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051436]; protein localization to kinetochore [GO:0034501]; regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439]; small GTPase mediated signal transduction [GO:0007264]anaphase-promoting complex [GO:0005680]; condensed chromosome kinetochore [GO:0000777]; condensed chromosome outer kinetochore [GO:0000940]; condensed nuclear chromosome kinetochore [GO:0000778]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; microtubule organizing center [GO:0005815]; perinuclear region of cytoplasm [GO:0048471]; spindle midzone [GO:0051233]FUNCTION: Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269|PubMed:10477750, ECO:0000269|PubMed:11702782, ECO:0000269|PubMed:14706340, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:19411850, ECO:0000269|PubMed:19503101}.P42694HELZ)Probable helicase with zinc finger domainzATP binding [GO:0005524]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]FUNCTION: May act as a helicase that plays a role in RNA metabolism in multiple tissues and organs within the developing embryo.Q2KHR3QSER1#Glutamine and serine-rich protein 1Q9UHN6TMEM2Transmembrane protein 2EFUNCTION: May be required for the heart morphogenesis. {ECO:0000250}.Q8NEF3CC112)Coiled-coil domain-containing protein 112Q9UBX5FBLN5 Fibulin-5SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:20599547}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17035250}. Note=co-localizes with ELN in elastic fibers. {ECO:0000269|PubMed:17035250}.$cell-matrix adhesion [GO:0007160]; elastic fiber assembly [GO:0048251]; extracellular matrix organization [GO:0030198]; protein localization to cell surface [GO:0034394]; regulation of cell growth [GO:0001558]; regulation of removal of superoxide radicals [GO:2000121]; secretion [GO:0046903]calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]elastic fiber [GO:0071953]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]?FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (PubMed:18185537). Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity). Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823). {ECO:0000250|UniProtKB:Q9WVH9, ECO:0000269|PubMed:10428823, ECO:0000269|PubMed:18185537}.Q4KMP7TB10BTBC1 domain family member 10BvSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16923811}. Note=In melanocytes, located at the periphery of cells.positive regulation of GTPase activity [GO:0043547]; regulation of GTPase activity [GO:0043087]; retrograde transport, endosome to Golgi [GO:0042147]FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A, RAB27A, AND RAB35. Does not act on RAB2A and RAB6A. {ECO:0000269|PubMed:16923811, ECO:0000269|PubMed:19077034}.P018921A027HLA class I histocompatibility antigen, A-2 alpha chainantibacterial humoral response [GO:0019731]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; interferon-gamma-mediated signaling pathway [GO:0060333]; positive regulation of CD8-positive, alpha-beta T cell activation [GO:2001187]; positive regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000566]; positive regulation of interferon-gamma production [GO:0032729]; positive regulation of memory T cell activation [GO:2000568]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of defense response to virus by virus [GO:0050690]; regulation of immune response [GO:0050776]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; poly(A) RNA binding [GO:0044822];< receptor binding [GO:0005102]; TAP binding [GO:0046977]; T cell receptor binding [GO:0042608]cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]Q9NX24NHP2)H/ACA ribonucleoprotein complex subunit 2)rRNA pseudouridine synthesis [GO:0031118]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small nucleolar ribonucleoprotein complex [GO:0005732]Q2NKX8ERC6L'DNA excision repair protein ERCC-6-likehSUBCELLULAR LOCATION: Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between kinetochores. In metaphase, it localizes to numerous thin threads that stretch between sister kinetochores of the aligned chromosomes and are composed of catenated centromeric DNA. Evolution from inner centromeres to thin threads takes place in response to tension. Resolution of thin threads requires topoisomerase 2-alpha (TOP2A) after anaphase onset.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; small GTPase mediated signal transduction [GO:0007264]centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]zFUNCTION: DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. {ECO:0000269|PubMed:17218258}.Q9P246STIM2Stromal interaction molecule 2SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041}; Single-pass type I membrane protein {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041}. Note=Dynamically translocates from a uniform endoplasmic reticulum distribution to punctual endoplasmic reticulum-plasma membrane junctions in response to decrease in endoplasmic reticulum Ca(2+) concentration.activation of store-operated calcium channel activity [GO:0032237]; calcium ion transmembrane transport [GO:0070588]; cellular calcium ion homeostasis [GO:0006874]; positive regulation of calcium ion transport [GO:0051928]calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; store-operated calcium channel activity [GO:0015279]TFUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx. {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041, ECO:0000269|PubMed:21217057, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:23359669}.Q5K4L6S27A3)Long-chain fatty acid transport protein 3fatty-acyl-CoA synthase activity [GO:0004321]; long-chain fatty acid-CoA ligase activity [GO:0004467]; nucleotide binding [GO:0000166]; very long-chain fatty acid-CoA ligase activity [GO:0031957]gintegral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]FUNCTION: Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids. Does not exhibit fatty acid transport activity (By similarity). {ECO:0000250}.Q96P11NSUN53Probable 28S rRNA (cytosine-C(5))-methyltransferaseFUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3782 in 28S rRNA. {ECO:0000250}.P09132SRP19*Signal recognition particle 19 kDa protein cellular protein metabolic process [GO:0044267]; cotranslational protein targeting to membrane [GO:0006613]; gene expression [GO:0010467]; response to drug [GO:0042493]; SRP-dependent cotranslational protein targeting to membrane [GO:0006614]; translation [GO:0006412]=7S RNA binding [GO:0008312]; poly(A) RNA binding [GO:0044822]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; signal recognition particle, endoplasmic reticulum targeting [GO:0005786]FUNCTION: Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.Q13620CUL4B Cullin-4BYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544}.cell cycle [GO:0007049]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; histone H2A monoubiquitination [GO:0035518]; neuron projection development [GO:0031175]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of protein catabolic process [GO:0045732]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; translesion synthesis [GO:0019985]; UV-damage excision repair [GO:0070914]Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8. {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460}.Q07157ZO1Tight junction protein ZO-13SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, tight junction. Cell junction. Cell junction, gap junction. Note=Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells.apoptotic process [GO:0006915]; blastocyst formation [GO:0001825]; cell-cell junction assembly [GO:0007043]; cell-cell signaling involved in cell-cell junction organization [GO:1901350]; cellular component disassembly< involved in execution phase of apoptosis [GO:0006921]; establishment of endothelial intestinal barrier [GO:0090557]; hippo signaling [GO:0035329]; membrane organization [GO:0061024]; programmed cell death [GO:0012501]; sensory perception of sound [GO:0007605]apical junction complex [GO:0043296]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell adherens junction [GO:0005913]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; gap junction [GO:0005921]; intercalated disc [GO:0014704]; intercellular canaliculus [GO:0046581]; nucleus [GO:0005634]; plasma membrane [GO:0005886]wFUNCTION: The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells. {ECO:0000269|PubMed:21240187}.P09429HMGB1High mobility group protein B1{apoptotic DNA fragmentation [GO:0006309]; apoptotic process [GO:0006915]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; chromatin remodeling [GO:0006338]; dendritic cell chemotaxis [GO:0002407]; DNA geometric change [GO:0032392]; DNA ligation involved in DNA repair [GO:0051103]; DNA recombination [GO:0006310]; DNA topological change [GO:0006265]; inflammatory response [GO:0006954]; inflammatory response to antigenic stimulus [GO:0002437]; innate immune response [GO:0045087]; myeloid dendritic cell activation [GO:0001773]; negative regulation of apoptotic cell clearance [GO:2000426]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of RNA polymerase II transcriptional preinitiation complex assembly [GO:0017055]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; neuron projection development [GO:0031175]; positive chemotaxis [GO:0050918]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA binding [GO:0043388]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; programmed cell death [GO:0012501]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; V(D)J recombination [GO:0033151]bbubble DNA binding [GO:0000405]; chemoattractant activity [GO:0042056]; chromatin binding [GO:0003682]; cytokine activity [GO:0005125]; damaged DNA binding [GO:0003684]; DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; poly(A) RNA binding [GO:0044822]; RAGE receptor binding [GO:0050786]; repressing transcription factor binding [GO:0070491]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]; supercoiled DNA binding [GO:0097100]; transcription factor binding [GO:0008134]cell surface [GO:0009986]; condensed chromosome [GO:0000793]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity). {ECO:0000250}.Q6PJG6BRAT1 BRCA1-associated ATM activator 1_SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16452482, ECO:0000269|PubMed:25631046}. Cytoplasm {ECO:0000269|PubMed:25631046}. Note=Present at double strand breaks (DSBs)following ionizing radiation treatment. The ubiquitinated form localizes in the nucleus in a NDFIP1-dependent manner. {ECO:0000269|PubMed:16452482, ECO:0000269|PubMed:25631046}.FUNCTION: Involved in DNA damage response; activates kinases ATM, SMC1A and PRKDC by modulating their phosphorylation status following ionizing radiation (IR) stress (PubMed:16452482, PubMed:22977523). Plays a role in regulating mitochondrial function and cell proliferation (PubMed:25070371). Required for protein stability of MTOR and MTOR-related proteins, and cell cycle progress by growth factors (PubMed:25657994). {ECO:0000269|PubMed:16452482, ECO:0000269|PubMed:22977523, ECO:0000269|PubMed:25070371, ECO:0000269|PubMed:25657994}.Q9NS93TM7S3$Transmembrane 7 superfamily member 3Q8WV24PHLA11Pleckstrin homology-like domain family A member 1SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle membrane. Nucleus, nucleolus. Note=Colocalizes with intracellular vesicles.apoptotic process [GO:0006915]; FasL biosynthetic process [GO:0045210]; forebrain neuron differentiation [GO:0021879]; positive regulation of apoptotic process [GO:0043065]ycytoplasmic vesicle membrane [GO:0030659]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]UFUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. May be involved in translational regulation. {ECO:0000269|PubMed:11369516, ECO:0000269|PubMed:12738777}.Q8IVH8M4K37Mitogen-activated protein kinase kinase kinase kinase 3xactivation of MAPKKK activity [GO:0000185]; activation of protein kinase activity [GO:0032147]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; response to tumor necrosis factor [GO:0034612]; response to UV [GO:0009411]ATP binding [GO:0005524]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]FUNCTION: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. {ECO:0000269|PubMed:9275185}.Q9BXK1KLF16Krueppel-like factor 16[dopamine receptor signaling pathway [GO:0007212]; transcription, DNA-templated [GO:0006351]%metal ion binding [GO:0046872]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]FUNCTION: Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity). {ECO:0000250}.Q14241ELOA1/Transcription elongation factor B polypeptide 3gene expression [GO:0010467]; positive regulation of viral transcription [GO:0050434]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]cytoplasm [GO:0005737]; elongin complex [GO:0070449]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]rFUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).Q8IZD4DCP1BmRNA-decapping enzyme 1BUSUBCELLULAR L< OCATION: Cytoplasm {ECO:0000269|PubMed:15067023}. Nucleus {ECO:0000250}.deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; deadenylation-independent decapping of nuclear-transcribed mRNA [GO:0031087]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of catalytic activity [GO:0050790]benzyme regulator activity [GO:0030234]; hydrolase activity [GO:0016787]; mRNA binding [GO:0003729]cytoplasm [GO:0005737]; cytoplasmic mRNA processing body [GO:0000932]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity). {ECO:0000250}.Q8NBZ7UXS1#UDP-glucuronic acid decarboxylase 1~SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.Tprotein tetramerization [GO:0051262]; UDP-D-xylose biosynthetic process [GO:0033320]~NAD+ binding [GO:0070403]; protein homodimerization activity [GO:0042803]; UDP-glucuronate decarboxylase activity [GO:0048040]extracellular exosome [GO:0070062]; Golgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]; mitochondrion [GO:0005739]FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.Q9BSY4CHCH5?Coiled-coil-helix-coiled-coil-helix domain-containing protein 5 aerobic respiration [GO:0009060]Q15361TTF1"Transcription termination factor 1@SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}.chromatin remodeling [GO:0006338]; DNA-templated transcription, termination [GO:0006353]; gene expression [GO:0010467]; negative regulation of DNA replication [GO:0008156]; negative regulation of gene expression, epigenetic [GO:0045814]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription, DNA-templated [GO:0006355]; termination of RNA polymerase I transcription [GO:0006363]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]{FUNCTION: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. {ECO:0000269|PubMed:7597036}.Q8NHP8PLBL2Putative phospholipase B-like 2CSUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:17105447}.0FUNCTION: Putative phospholipase. {ECO:0000250}.P51787KCNQ16Potassium voltage-gated channel subfamily KQT member 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18165683}; Multi-pass membrane protein {ECO:0000269|PubMed:18165683}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18165683}; Multi-pass membrane protein {ECO:0000269|PubMed:18165683}.jatrial cardiac muscle cell action potential [GO:0086014]; cardiac muscle contraction [GO:0060048]; cardiovascular system development [GO:0072358]; cellular response to cAMP [GO:0071320]; cellular response to drug [GO:0035690]; cellular response to epinephrine stimulus [GO:0071872]; gene silencing [GO:0016458]; membrane repolarization during action potential [GO:0086011]; membrane repolarization during cardiac muscle cell action potential [GO:0086013]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of heart rate [GO:0010460]; positive regulation of potassium ion transmembrane transport [GO:1901381]; potassium ion export [GO:0071435]; potassium ion export across plasma membrane [GO:0097623]; potassium ion transmembrane transport [GO:0071805]; regulation of atrial cardiac muscle cell membrane repolarization [GO:0060372]; regulation of gene expression by genetic imprinting [GO:0006349]; regulation of heart contraction [GO:0008016]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane repolarization [GO:0060306]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; sensory perception of sound [GO:0007605]; synaptic transmission [GO:0007268]; ventricular cardiac muscle cell action potential [GO:0086005]calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; ion channel binding [GO:0044325]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; protein phosphatase 1 binding [GO:0008157]; scaffold protein binding [GO:0097110]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization [GO:0086089]; voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization [GO:0086008]; voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization [GO:1902282]$basolateral plasma membrane [GO:0016323]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]zFUNCTION: Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.Q03013GSTM4Glutathione S-transferase Mu 4glutathione derivative biosynthetic process [GO:1901687]; glutathione metabolic process [GO:0006749]; nitrobenzene metabolic process [GO:0018916]; small molecule metabolic process [GO:0044281]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805]FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1-chloro-2,4-dinitrobenzene.Q7Z4G4TRM11/tRNA (guanine(10)-N2)-methyltransferase homologBmethyltransferase activity [GO:0008168]; tRNA binding [GO:0000049]FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.Q9BQ24ZFY21-Zinc finger FYVE domain-containing protein 21SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasmic vesicle. Endosome. Note=Within cytoplasmic vesicles, partially colocalizes with EEA1, an endosomal marker.ecytoplasmic membrane-bounded vesicle [GO:0016023]; endosome [GO:0005768]; focal adhesion [GO:0005925]oFUNCTION: Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression. {ECO:0000269|PubMed:20439989, ECO:0000269|PubMed:21768110}.P57772SELB)Selenocysteine-specific elongation< factorGTPase activity [GO:0003924]; GTP binding [GO:0005525]; ribonucleoprotein complex binding [GO:0043021]; selenocysteine insertion sequence binding [GO:0035368]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049]Xmitochondrion [GO:0005739]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.Q86UU0BCL9L"B-cell CLL/lymphoma 9-like proteinYSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17129358, ECO:0000269|PubMed:17309600}.canonical Wnt signaling pathway [GO:0060070]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell morphogenesis [GO:0022604]; skeletal muscle cell differentiation [GO:0035914]; somatic stem cell maintenance [GO:0035019]; transcription, DNA-templated [GO:0006351]Rbeta-catenin binding [GO:0008013]; transcription coactivator activity [GO:0003713]FUNCTION: Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity). {ECO:0000250}.Q7Z412PEX26Peroxisome assembly protein 26SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:12717447}; Single-pass type II membrane protein {ECO:0000269|PubMed:12717447}.hprotein import into peroxisome matrix [GO:0016558]; protein import into peroxisome membrane [GO:0045046]jATPase binding [GO:0051117]; protein complex binding [GO:0032403]; protein C-terminus binding [GO:0008022]Pintegral component of peroxisomal membrane [GO:0005779]; peroxisome [GO:0005777]FUNCTION: Probably required for protein import into peroxisomes. Anchors PEX1 and PEX6 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes. Involved in the import of catalase and proteins containing a PTS2 target sequence, but not in import of proteins with a PTS1 target sequence. {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:12851857}.P47712PA24ACytosolic phospholipase A2|SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle. Note=Translocates to membrane vesicles in a calcium-dependent fashion.arachidonic acid metabolic process [GO:0019369]; arachidonic acid secretion [GO:0050482]; blood coagulation [GO:0007596]; cardiolipin acyl-chain remodeling [GO:0035965]; cellular response to antibiotic [GO:0071236]; glycerophospholipid biosynthetic process [GO:0046474]; icosanoid biosynthetic process [GO:0046456]; icosanoid metabolic process [GO:0006690]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylethanolamine acyl-chain remodeling [GO:0036152]; phosphatidylglycerol acyl-chain remodeling [GO:0036148]; phosphatidylinositol acyl-chain remodeling [GO:0036149]; phosphatidylserine acyl-chain remodeling [GO:0036150]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; platelet activating factor biosynthetic process [GO:0006663]; platelet activation [GO:0030168]; regulation of cell proliferation [GO:0042127]; small molecule metabolic process [GO:0044281]calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; lysophospholipase activity [GO:0004622]; phospholipase A2 activity [GO:0004623]cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; mitochondrial inner membrane [GO:0005743]FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.Q9BXV9CN142!Uncharacterized protein C14orf142Q9UGY1NOL12Nucleolar protein 12.FUNCTION: May bind to 28S rRNA. {ECO:0000250}.P03956MMP1Interstitial collagenasegSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2167156}.lblood coagulation [GO:0007596]; cellular protein metabolic process [GO:0044267]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; leukocyte migration [GO:0050900]; positive regulation of protein oligomerization [GO:0032461]; proteolysis [GO:0006508]; viral process [GO:0016032]calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]Rextracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]/FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. {ECO:0000269|PubMed:1645757}.O75475PSIP1!PC4 and SFRS1-interacting proteinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9885563}. Note=Remains chromatin-associated throughout the cell cycle.establishment of integrated proviral latency [GO:0075713]; mRNA 5'-splice site recognition [GO:0000395]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]activating transcription factor binding [GO:0033613]; chromatin binding [GO:0003682]; poly(A) RNA binding [GO:0044822]; RNA polymerase II transcription coactivator activity [GO:0001105]; supercoiled DNA binding [GO:0097100]cytosol [GO:0005829]; nuclear heterochromatin [GO:0005720]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptionally active chromatin [GO:0035327]-FUNCTION: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. {ECO:0000269|PubMed:15642333}.Q9H9A5CNO10)CCR4-NOT transcription complex subunit 10cgene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; transcription, DNA-templated [GO:0006351]`CCR4-NOT complex [GO:0030014]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is not required for association of CNOT7 to the CCR4-NOT complex. {ECO:0000269|PubMed:23221646}.Q96HQ2C2AIL CDKN2AIP N-terminal-like proteinQ92576PHF3PHD finger protein 3O60711LPXNLeupaxinHSUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region {ECO:000< 0250}. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.cell adhesion [GO:0007155]; negative regulation of B cell receptor signaling pathway [GO:0050859]; negative regulation of cell adhesion [GO:0007162]; protein complex assembly [GO:0006461]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]Ktranscription cofactor activity [GO:0003712]; zinc ion binding [GO:0008270]cell projection [GO:0042995]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; podosome [GO:0002102]_FUNCTION: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}.Q9Y285SYFA(Phenylalanine--tRNA ligase alpha subunitgene expression [GO:0010467]; phenylalanyl-tRNA aminoacylation [GO:0006432]; tRNA aminoacylation for protein translation [GO:0006418]ATP binding [GO:0005524]; phenylalanine-tRNA ligase activity [GO:0004826]; poly(A) RNA binding [GO:0044822]; tRNA binding [GO:0000049]P17706PTN20Tyrosine-protein phosphatase non-receptor type 2oSUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum {ECO:0000269|PubMed:7593185}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:7593185}. Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. {ECO:0000269|PubMed:7593185}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Cell membrane. Note=Predominantly localizes to chromatin (By similarity). Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors (PubMed:9488479). Recruited by activated ITGA1 at the plasma membrane. {ECO:0000250, ECO:0000269|PubMed:9488479}. B cell differentiation [GO:0030183]; cytokine-mediated signaling pathway [GO:0019221]; erythrocyte differentiation [GO:0030218]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of cell proliferation [GO:0008285]; negative regulation of chemotaxis [GO:0050922]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of interferon-gamma-mediated signaling pathway [GO:0060336]; negative regulation of interleukin-2-mediated signaling pathway [GO:1902206]; negative regulation of interleukin-4-mediated signaling pathway [GO:1902215]; negative regulation of interleukin-6-mediated signaling pathway [GO:0070104]; negative regulation of lipid storage [GO:0010888]; negative regulation of macrophage colony-stimulating factor signaling pathway [GO:1902227]; negative regulation of macrophage differentiation [GO:0045650]; negative regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000587]; negative regulation of positive thymic T cell selection [GO:1902233]; negative regulation of prolactin signaling pathway [GO:1902212]; negative regulation of protein tyrosine kinase activity [GO:0061099]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]; negative regulation of tyrosine phosphorylation of Stat1 protein [GO:0042512]; negative regulation of tyrosine phosphorylation of Stat3 protein [GO:0042518]; negative regulation of tyrosine phosphorylation of Stat5 protein [GO:0042524]; negative regulation of tyrosine phosphorylation of Stat6 protein [GO:0042527]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of PERK-mediated unfolded protein response [GO:1903899]; regulation of hepatocyte growth factor receptor signaling pathway [GO:1902202]; regulation of interferon-gamma-mediated signaling pathway [GO:0060334]; T cell differentiation [GO:0030217]integrin binding [GO:0005178]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; receptor tyrosine kinase binding [GO:0030971]; syntaxin binding [GO:0019905]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3, STAT5A, STAT5B and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. Finally, it negatively regulates prolactin-mediated signaling pathway through dephosphorylation of STAT5A and STAT5B. May also bind DNA. {ECO:0000269|PubMed:10734133, ECO:0000269|PubMed:11909529, ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15592458, ECO:0000269|PubMed:18819921, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:9488479}.< P15408FOSL2Fos-related antigen 2 cell death [GO:0008219]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts. {ECO:0000250}.Q9NXG2THUM1!THUMP domain-containing protein 1Q8N556AFAP1#Actin filament-associated protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15485829}. Note=Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles upon their induction.dregulation of cytoskeleton organization [GO:0051493]; regulation of signal transduction [GO:0009966]FUNCTION: Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells. {ECO:0000250, ECO:0000269|PubMed:15485829}.O00622CYR61 Protein CYR61anatomical structure morphogenesis [GO:0009653]; apoptotic process involved in heart morphogenesis [GO:0003278]; atrial septum morphogenesis [GO:0060413]; atrioventricular valve morphogenesis [GO:0003181]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cell proliferation [GO:0008283]; chemotaxis [GO:0006935]; chondroblast differentiation [GO:0060591]; chorio-allantoic fusion [GO:0060710]; extracellular matrix organization [GO:0030198]; intussusceptive angiogenesis [GO:0002041]; labyrinthine layer blood vessel development [GO:0060716]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell death [GO:0060548]; osteoblast differentiation [GO:0001649]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of phospholipase activity [GO:0010518]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; reactive oxygen species metabolic process [GO:0072593]; regulation of cell growth [GO:0001558]; regulation of ERK1 and ERK2 cascade [GO:0070372]; signal transduction [GO:0007165]; ventricular septum development [GO:0003281]; wound healing, spreading of cells [GO:0044319]fextracellular matrix binding [GO:0050840]; heparin binding [GO:0008201]; integrin binding [GO:0005178]Rextracellular matrix [GO:0031012]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CYR61-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3. {ECO:0000269|PubMed:11584015}.Q5JTH9RRP12RRP12-like proteinSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.bintegral component of membrane [GO:0016021]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]Q15434RBMS28RNA-binding motif, single-stranded-interacting protein 2Q9BZF3OSBL6+Oxysterol-binding protein-related protein 6cytosol [GO:0005829]; nuclear membrane [GO:0031965]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]LFUNCTION: Weakly binds 25-hydroxycholesterol. {ECO:0000269|PubMed:17428193}.Q06330SUH2Recombining binding protein suppressor of hairless NCID-CSL(2)SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear, upon interaction with RITA/C12orf52, translocates to the cytoplasm, down-regulating the Notch signaling pathway. angiogenesis [GO:0001525]; arterial endothelial cell fate commitment [GO:0060844]; atrioventricular canal development [GO:0036302]; auditory receptor cell fate commitment [GO:0009912]; B cell differentiation [GO:0030183]; blood vessel endothelial cell fate specification [GO:0097101]; blood vessel lumenization [GO:0072554]; blood vessel remodeling [GO:0001974]; cardiac left ventricle morphogenesis [GO:0003214]; Clara cell differentiation [GO:0060486]; defense response to bacterium [GO:0042742]; DNA recombination [GO:0006310]; dorsal aorta morphogenesis [GO:0035912]; endocardium morphogenesis [GO:0003160]; epidermal cell fate specification [GO:0009957]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; gene expression [GO:0010467]; hair follicle maturation [GO:0048820]; humoral immune response [GO:0006959]; inflammatory response to antigenic stimulus [GO:0002437]; interleukin-4 secretion [GO:0072602]; keratinocyte differentiation [GO:0030216]; labyrinthine layer blood vessel development [GO:0060716]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of cell proliferation [GO:0008285]; negative regulation of ossification [GO:0030279]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling involved in heart development [GO:0061314]; Notch signaling pathway [GO:0007219]; outflow tract morphogenesis [GO:0003151]; pituitary gland development [GO:0021983]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment [GO:1901297]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cell proliferation involved in heart morphogenesis [GO:2000138]; positive regulation of ephrin receptor signaling pathway [GO:1901189]; positive regulation of ERBB signaling pathway [GO:1901186]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter in response to hypoxia [GO:0061419]; positive regulation of transcription of Notch receptor target [GO:0007221]; regulation of timing of cell differentiation [GO:0048505]; regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation [GO:0003256]; sebaceous gland development [GO:0048733]; secondary heart field specification [GO:0003139]; somatic stem cell maintenance [GO:0035019]; transcription initiation from RNA polymerase II promoter [GO:0006367]; ventricular trabecula myocardium morphogenesis [GO:0003222]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; recombinase activity [GO:0000150]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequenc< e-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II repressing transcription factor binding [GO:0001103]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; MAML1-RBP-Jkappa- ICN1 complex [GO:0002193]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen) (PubMed:23303788). {ECO:0000269|PubMed:21991380, ECO:0000269|PubMed:23303788}.Q9BPU6DPYL5%Dihydropyrimidinase-related protein 5hydrolase(PC00121)eaxon guidance [GO:0007411]; nervous system development [GO:0007399]; signal transduction [GO:0007165]Rhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]Lcytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]MFUNCTION: May have a function in neuronal differentiation and/or axon growth.O00300TR11B5Tumor necrosis factor receptor superfamily member 11Bapoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; response to arsenic-containing substance [GO:0046685]; response to drug [GO:0042493]; response to estrogen [GO:0043627]; response to magnesium ion [GO:0032026]; response to nutrient [GO:0007584]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]>cytokine activity [GO:0005125]; receptor activity [GO:0004872]textracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9168977}.Q12913PTPRJ.Receptor-type tyrosine-protein phosphatase etaSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane {ECO:0000250}. Cell junction. Note=After T-cell stimulation, it is temporarily excluded from immunological synapses.Ocontact inhibition [GO:0060242]; heart development [GO:0007507]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of T cell receptor signaling pathway [GO:0050860]; negative regulation of vascular permeability [GO:0043116]; oligodendrocyte differentiation [GO:0048709]; peptidyl-tyrosine dephosphorylation [GO:0035335]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive chemotaxis [GO:0050918]; positive regulation of cell adhesion [GO:0045785]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of protein kinase B signaling [GO:0051897]; regulation of cell adhesion [GO:0030155]; vasculogenesis [GO:0001570]Zbeta-catenin binding [GO:0008013]; delta-catenin binding [GO:0070097]; gamma-catenin binding [GO:0045295]; mitogen-activated protein kinase binding [GO:0051019]; phosphatase activity [GO:0016791]; platelet-derived growth factor receptor binding [GO:0005161]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725](cell-cell junction [GO:0005911]; cell junction [GO:0030054]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; immunological synapse [GO:0001772]; integral component of plasma membrane [GO:0005887]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]FUNCTION: Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. {ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403, ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717, ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:16778204, ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114, ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411, ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.Q9NQZ2SAS10$Something about silencing protein 10brain development [GO:0007420]; chromatin modification [GO:0016568]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]Snucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]FUNCTION: Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity). {ECO:0000250|UniProtKB:Q12136, ECO:0000250|UniProtKB:Q9JI13}.P42857NSG1'Neuron-specific protein family member 1clathrin coat assembly [GO:0048268]; dopamine receptor signaling pathway [GO:0007212]; endosomal transport [GO:0016197]; positive regulation of receptor recycling [GO:0001921]cytoplasm [GO:0005737]; endosome [GO:0005768]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; lateral plasma membrane [GO:0016328]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211]O15230LAMA5Laminin subunit alpha-5angiogenesis [GO:0001525]; branching involved in salivary gland morphogenesis [GO:0060445]; branching involved in urete< ric bud morphogenesis [GO:0001658]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell proliferation [GO:0008283]; cell recognition [GO:0008037]; cilium assembly [GO:0042384]; cytoskeleton organization [GO:0007010]; embryo development [GO:0009790]; endothelial cell differentiation [GO:0045446]; establishment of protein localization to plasma membrane [GO:0090002]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; focal adhesion assembly [GO:0048041]; hair follicle development [GO:0001942]; integrin-mediated signaling pathway [GO:0007229]; lung development [GO:0030324]; morphogenesis of a polarized epithelium [GO:0001738]; morphogenesis of embryonic epithelium [GO:0016331]; muscle organ development [GO:0007517]; neural crest cell migration [GO:0001755]; odontogenesis of dentin-containing tooth [GO:0042475]; regulation of cell adhesion [GO:0030155]; regulation of cell migration [GO:0030334]; regulation of cell proliferation [GO:0042127]; regulation of embryonic development [GO:0045995]; substrate adhesion-dependent cell spreading [GO:0034446]Hintegrin binding [GO:0005178]; structural molecule activity [GO:0005198]=basal lamina [GO:0005605]; basement membrane [GO:0005604]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; laminin-10 complex [GO:0043259]; laminin-11 complex [GO:0043260]; laminin-5 complex [GO:0005610]; nucleus [GO:0005634]P61165TM258Transmembrane protein 258Q86XI2CNDG2Condensin-2 complex subunit G2cell division [GO:0051301]; chromosome condensation [GO:0030261]; inner cell mass cell proliferation [GO:0001833]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]Q9HCK8CHD8+Chromodomain-helicase-DNA-binding protein 8SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:20453063}. Note=Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites.ATP-dependent chromatin remodeling [GO:0043044]; brain development [GO:0007420]; canonical Wnt signaling pathway [GO:0060070]; digestive tract development [GO:0048565]; DNA duplex unwinding [GO:0032508]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase III promoter [GO:0045945]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]&ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-dependent ATPase activity [GO:0008094]; DNA helicase activity [GO:0003678]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; p53 binding [GO:0002039]gMLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. {ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:18378692}.Q9NRZ9HELLSLymphoid-specific helicaseuSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Closely associated with pericentric heterochromatin. {ECO:0000250}.^cell division [GO:0051301]; lymphocyte proliferation [GO:0046651]; maintenance of DNA methylation [GO:0010216]; methylation-dependent chromatin silencing [GO:0006346]; mitotic nuclear division [GO:0007067]; multicellular organismal development [GO:0007275]; pericentric heterochromatin assembly [GO:0031508]; transcription, DNA-templated [GO:0006351]8ATP binding [GO:0005524]; helicase activity [GO:0004386]kchromosome, centromeric region [GO:0000775]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]FUNCTION: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of heterochromatin, implying a functional role in the regulation of transcription and mitosis (By similarity). {ECO:0000250|UniProtKB:Q60848}.P62068UBP46(Ubiquitin carboxyl-terminal hydrolase 465adult feeding behavior [GO:0008343]; behavioral fear response [GO:0001662]; behavioral response to ethanol [GO:0048149]; protein deubiquitination [GO:0016579]; regulation of synaptic transmission, GABAergic [GO:0032228]; righting reflex [GO:0060013]; ubiquitin-dependent protein catabolic process [GO:0006511]mFUNCTION: Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. {ECO:0000269|PubMed:19075014}.O94854K0754 Uncharacterized protein KIAA0754Q8WXD5GEMI6Gem-associated protein 6OSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11748230}. Nucleus, gem {ECO:0000269|PubMed:11748230}. Cytoplasm {ECO:0000269|PubMed:11748230}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]kFUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:11748230, ECO:0000269|PubMed:18984161}.O60716CTND1Catenin delta-1Regulators(10)SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Interaction with GLIS2 promotes nuclear translocation (By similarity). Detected at cell-cell contacts. NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm. Isoforms 4A and 1AB are excluded from the nucleus. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1A: Nucleus.< ; SUBCELLULAR LOCATION: Isoform 2A: Nucleus.; SUBCELLULAR LOCATION: Isoform 3A: Nucleus.adherens junction organization [GO:0034332]; cell adhesion [GO:0007155]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; regulation of transcription, DNA-templated [GO:0006355]; single organismal cell-cell adhesion [GO:0016337]; transcription, DNA-templated [GO:0006351]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; Wnt signaling pathway [GO:0016055]<cadherin binding [GO:0045296]; receptor binding [GO:0005102]cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage. {ECO:0000250, ECO:0000269|PubMed:17344476, ECO:0000269|PubMed:20371349}.Q13740CD166 CD166 antigenCSCSUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000269|PubMed:15496415}.axon guidance [GO:0007411]; cell adhesion [GO:0007155]; motor neuron axon guidance [GO:0008045]; signal transduction [GO:0007165]axon [GO:0030424]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; neuronal cell body [GO:0043025]FUNCTION: Cell adhesion molecule that binds to CD6. Involved in neurite extension by neurons via heterophilic and homophilic interactions. May play a role in the binding of T- and B-cells to activated leukocytes, as well as in interactions between cells of the nervous system.P48307TFPI2!Tissue factor pathway inhibitor 2sextracellular matrix structural constituent [GO:0005201]; serine-type endopeptidase inhibitor activity [GO:0004867]Enucleus [GO:0005634]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: May play a role in the regulation of plasmin-mediated matrix remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and weakly factor Xa. Has no effect on thrombin. {ECO:0000269|PubMed:7872799}.Q96J01THOC3THO complex subunit 3 EJC/TREK(10)Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346]FUNCTION: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:15833825, ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602, ECO:0000269|PubMed:18974867}.O94851MICA2+Protein-methionine sulfoxide oxidase MICAL2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24440334}./actin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; heart development [GO:0007507]; heart looping [GO:0001947]; oxidation-reduction process [GO:0055114]; positive regulation of transcription via serum response element binding [GO:0010735]; sulfur oxidation [GO:0019417]9actin binding [GO:0003779]; FAD binding [GO:0071949]; NADPH:sulfur oxidoreductase activity [GO:0043914]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; zinc ion binding [GO:0008270]FUNCTION: Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin and regulates the SRF signaling. Acts by modifying nuclear actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA. {ECO:0000269|PubMed:23927065, ECO:0000269|PubMed:24440334}.Q9NTJ3SMC4/Structural maintenance of chromosomes protein 4cell division [GO:0051301]; kinetochore organization [GO:0051383]; meiotic chromosome condensation [GO:0010032]; meiotic chromosome segregation [GO:0045132]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]; mitotic sister chromatid segregation [GO:0000070]|condensin complex [GO:0000796]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q86UV5UBP48(Ubiquitin carboxyl-terminal hydrolase 48eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16214042}. Nucleus {ECO:0000269|PubMed:16214042}.Lcytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. {ECO:0000269|PubMed:16214042}.Q12805FBLN3:EGF-containing fibulin-like extracellular matrix protein 1SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Localizes to the lamina propria underneath the olfactory epithelium. {ECO:0000250}.camera-type eye development [GO:0043010]; embryonic eye morphogenesis [GO:0048048]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix organization [GO:0030198]; negative regulation of chondrocyte differentiation [GO:0032331]; peptidyl-tyrosine phosphorylation [GO:0018108]; post-embryonic eye morphogenesis [GO:0048050]; regulation of transcription, DNA-templated [GO:0006355]; visual perception [GO:0007601]calcium ion binding [GO:0005509]; epidermal growth factor-activated receptor activity [GO:0005006]; epidermal growth factor receptor binding [GO:0005154]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. {ECO:0000269|PubMed:19804359, ECO:0000269|PubMed:19887559, ECO:0000269|PubMed:20005202}.P52758UK114Ribonuclease UK114ySUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mostly cytoplasmic but, in less differentiated cells occasionally nuclear.ibrain development [GO:0007420]; G1 to G0 transiti< on [GO:0070314]; kidney development [GO:0001822]; lung development [GO:0030324]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of translation [GO:0017148]; regulation of translational termination [GO:0006449]; response to lipid [GO:0033993]; response to salt [GO:1902074] deaminase activity [GO:0019239]; endoribonuclease activity, producing 3'-phosphomonoesters [GO:0016892]; long-chain fatty acid binding [GO:0036041]; platinum binding [GO:1904012]; poly(A) RNA binding [GO:0044822]; transition metal ion binding [GO:0046914]; xenon atom binding [GO:1904013]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]FUNCTION: Endoribonuclease responsible for the inhibition of the translation by cleaving mRNA. Inhibits cell-free protein synthesis. Cleaves phosphodiester bonds only in single-stranded RNA (By similarity). {ECO:0000250}.P29279CTGFConnective tissue growth factorpSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted {ECO:0000250}.angiogenesis [GO:0001525]; cartilage condensation [GO:0001502]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cell differentiation [GO:0030154]; cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cellular lipid metabolic process [GO:0044255]; chondrocyte proliferation [GO:0035988]; cytosolic calcium ion transport [GO:0060401]; DNA biosynthetic process [GO:0071897]; epidermis development [GO:0008544]; extracellular matrix constituent secretion [GO:0070278]; fibroblast growth factor receptor signaling pathway [GO:0008543]; gene expression [GO:0010467]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; lung development [GO:0030324]; negative regulation of cell death [GO:0060548]; negative regulation of gene expression [GO:0010629]; organ senescence [GO:0010260]; ossification [GO:0001503]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of cell activation [GO:0050867]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G0 to G1 transition [GO:0070318]; positive regulation of gene expression [GO:0010628]; positive regulation of JNK cascade [GO:0046330]; positive regulation of stress fiber assembly [GO:0051496]; reactive oxygen species metabolic process [GO:0072593]; regulation of cell growth [GO:0001558]; regulation of chondrocyte differentiation [GO:0032330]; response to amino acid [GO:0043200]; response to anoxia [GO:0034059]; response to estradiol [GO:0032355]; response to fatty acid [GO:0070542]; response to glucose [GO:0009749]; response to mineralocorticoid [GO:0051385]; response to peptide hormone [GO:0043434]; response to wounding [GO:0009611]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; tissue homeostasis [GO:0001894]; transcription initiation from RNA polymerase II promoter [GO:0006367]heparin binding [GO:0008201]; insulin-like growth factor binding [GO:0005520]; integrin binding [GO:0005178]; protein C-terminus binding [GO:0008022]ecell cortex [GO:0005938]; cis-Golgi network [GO:0005801]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis. {ECO:0000269|PubMed:10614647, ECO:0000269|PubMed:12553878}.Q9BWE0REPI1Replication initiator 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606657}.DNA replication [GO:0006260]; regulation of fatty acid transport [GO:2000191]; regulation of glucose import in response to insulin stimulus [GO:2001273]cytosolic ribosome [GO:0022626]; lipid particle [GO:0005811]; nuclear membrane [GO:0031965]; nuclear origin of replication recognition complex [GO:0005664]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]PFUNCTION: Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending.P58335ANTR2Anthrax toxin receptor 2iSUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein. Note=Expressed at the cell surface.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=Expressed predominantly within the endoplasmic reticulum and not at the plasma membrane.; SUBCELLULAR LOCATION: Isoform 3: Secreted.?reproductive process [GO:0022414]; toxin transport [GO:1901998]>metal ion binding [GO:0046872]; receptor activity [GO:0004872]endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Necessary for cellular interactions with laminin and the extracellular matrix. {ECO:0000269|PubMed:11683410, ECO:0000269|PubMed:12973667}.Q8N3R9MPP5MAGUK p55 subfamily member 5SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Cell junction, tight junction. Note=Localized to the tight junctions of epithelial cells and a subset of intracellular vesicles. In the retina, detected at the outer limiting membrane (OLM), apical to the adherens junction (AJ), where it colocalizes with CRB1. Colocalizes with MPP1 in the retina at the outer limiting membrane (OLM). Localized to the Purkinje cell body and axon.bicellular tight junction assembly [GO:0070830]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; establishment of protein localization to plasma membrane [GO:0090002]; morphogenesis of an epithelial sheet [GO:0002011]; myelin assembly [GO:0032288]; peripheral nervous system myelin maintenance [GO:0032287]; protein localization to myelin sheath abaxonal region [GO:0035750]Jbicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; lateral loop [GO:0043219]; myelin sheath adaxonal region [GO:0035749]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; Schmidt-Lanterman incisure [GO:0043220]vFUNCTION: May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). {ECO:0000250}.Q8IWR1TRI59&Tripartite motif-containing protein 59SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q922Y2}; Single-pass membrane protein {ECO:0000305}.innate immune response [GO:0045087]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of viral entry into host cell [GO:0046597]Mubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]xFUNCTION: May serve as a multifunctional regulator for innate immune signaling pathways. {ECO:0000250|Un< iProtKB:Q922Y2}.Q6EEV4GL1AD<DNA-directed RNA polymerase II subunit GRINL1A, isoforms 4/5Q01469FABP5%Fatty acid-binding protein, epidermalFepidermis development [GO:0008544]; glucose metabolic process [GO:0006006]; glucose transport [GO:0015758]; lipid metabolic process [GO:0006629]; phosphatidylcholine biosynthetic process [GO:0006656]; response to wounding [GO:0009611]; small molecule metabolic process [GO:0044281]; triglyceride catabolic process [GO:0019433]^fatty acid binding [GO:0005504]; lipid binding [GO:0008289]; transporter activity [GO:0005215]FUNCTION: High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.O75914PAK3%Serine/threonine-protein kinase PAK 3jactin cytoskeleton organization [GO:0030036]; activation of MAPK activity [GO:0000187]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cell migration [GO:0016477]; dendrite development [GO:0016358]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; innate immune response [GO:0045087]; MAPK cascade [GO:0000165]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of neuron apoptotic process [GO:0043525]; regulation of actin filament polymerization [GO:0030833]; regulation of apoptotic process [GO:0042981]; regulation of mitotic cell cycle [GO:0007346]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated protein kinase signaling cascade [GO:0031098]; synapse organization [GO:0050808]; T cell costimulation [GO:0031295]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; Rac GTPase binding [GO:0048365]acytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; plasma membrane [GO:0005886]NFUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development. {ECO:0000269|PubMed:21177870}.Q96RN5MED156Mediator of RNA polymerase II transcription subunit 15gene expression [GO:0010467]; stem cell maintenance [GO:0019827]; transcription initiation from RNA polymerase II promoter [GO:0006367]|cytoplasm [GO:0005737]; mediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway. {ECO:0000269|PubMed:12167862, ECO:0000269|PubMed:16630888, ECO:0000269|PubMed:16799563}.Q8NBJ5GT251#Procollagen galactosyltransferase 1SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:20470363}. Note=Colocalized with PLOD3 and mannose binding lectin.7procollagen galactosyltransferase activity [GO:0050211]?endoplasmic reticulum lumen [GO:0005788]; membrane [GO:0016020]FUNCTION: Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen. {ECO:0000269|PubMed:19075007}.Q9H2V7SPNS1Protein spinster homolog 1SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:12815463}; Multi-pass membrane protein {ECO:0000269|PubMed:12815463}. Note=Colocalizes with SDHB.ulocomotion [GO:0040011]; sphingosine-1-phosphate signaling pathway [GO:0003376]; transmembrane transport [GO:0055085].sphingolipid transporter activity [GO:0046624]integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; mitochondrial inner membrane [GO:0005743]; vesicle [GO:0031982]FUNCTION: Sphingolipid transporter (By similarity). May be involved in necrotic or autophagic cell death. {ECO:0000250, ECO:0000269|PubMed:12815463}.Q9NQG7HPS4#Hermansky-Pudlak syndrome 4 proteinFblood coagulation [GO:0007596]; hemostasis [GO:0007599]; lysosome organization [GO:0007040]; melanocyte differentiation [GO:0030318]; positive regulation of eye pigmentation [GO:0048075]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein stabilization [GO:0050821]; protein targeting [GO:0006605]Zprotein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]BLOC-3 complex [GO:0031085]; cytoplasm [GO:0005737]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane [GO:0016020]; platelet dense granule [GO:0042827]>FUNCTION: May function in the pathway of organelle biogenesis.O94856NFASC Neurofascinaxon guidance [GO:0007411]; clustering of voltage-gated sodium channels [GO:0045162]; heterotypic cell-cell adhesion [GO:0034113]; myelination [GO:0042552]; paranodal junction assembly [GO:0030913]; peripheral nervous system development [GO:0007422]; protein localization to juxtaparanode region of axon [GO:0071205]; protein localization to paranode region of axon [GO:0002175]; protein targeting to plasma membrane [GO:0072661]; synapse organization [GO:0050808]; transmission of nerve impulse [GO:0019226]qaxon initial segment [GO:0043194]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; intracellular [GO:0005622]; myelin sheath [GO:0043209]; node of Ranvier [GO:0033268]; paranodal junction [GO:0033010]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schwann cell microvillus [GO:0097454]FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. {ECO:0000250}.P42167LAP2B4Lamina-associated polypeptide 2, isoforms beta/gammaSUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II membrane protein. Note=Tightly associated with the nuclear lamina.; SUBCELLULAR LOCATION: Isoform Zeta: Cytoplasm {ECO:0000269|PubMed:18403046}.cytoplasm [GO:0005737]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]FUNCTION: May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95.; FUNCTION: Thymopoietin (TP) and Thymopentin (TP5) may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.Q9GZN7ROGDIProtein rogdi homologESUBCELLULAR LOCATION: Nucleus envelope {ECO< :0000269|PubMed:22482807}.brain development [GO:0007420]; hemopoiesis [GO:0030097]; neurogenesis [GO:0022008]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of cell proliferation [GO:0008284]9intracellular [GO:0005622]; nuclear envelope [GO:0005635]OFUNCTION: May act as a positive regulator of cell proliferation. {ECO:0000250}.Q14689DIP2A%Disco-interacting protein 2 homolog Amulticellular organismal development [GO:0007275]; negative regulation of gene expression [GO:0010629]; regulation of apoptotic process [GO:0042981]/cell surface [GO:0009986]; nucleus [GO:0005634]hFUNCTION: May provide positional cues for axon pathfinding and patterning in the central nervous system.Q8WVM7STAG1Cohesin subunit SA-1SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.cell division [GO:0051301]; cellular protein metabolic process [GO:0044267]; chromosome segregation [GO:0007059]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]FUNCTION: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.Q9UKK6NXT1NTF2-related export protein 1}SUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000305}. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.Nprotein export from nucleus [GO:0006611]; RNA export from nucleus [GO:0006405]Mcytoplasm [GO:0005737]; nuclear pore [GO:0005643]; nuclear speck [GO:0016607]lFUNCTION: Stimulator of protein export for NES-containing proteins. Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5. {ECO:0000269|PubMed:10567585, ECO:0000269|PubMed:10848583, ECO:0000269|PubMed:11259602, ECO:0000269|PubMed:19165146}.Q7Z3V4UBE3BUbiquitin-protein ligase E3BFUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.Q9P2K6KLH42Kelch-like protein 423SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261606}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19261606}. Note=Predominantly in mitotic cells. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase cells is localized between the two sets of separated chromosomes as well as at the spindle poles. During telophase is localized arround the nuclei of the two daughter cells. Not detected at the midbody region during cytokinesis.cell division [GO:0051301]; mitotic nuclear division [GO:0007067]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of microtubule-based process [GO:0032886]]Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; spindle [GO:0005819]UFUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis. {ECO:0000269|PubMed:19261606}.O60934NBNNibrinSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000269|PubMed:12470659, ECO:0000269|PubMed:15916964}. Chromosome, telomere {ECO:0000250}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. {ECO:0000250}.ablastocyst growth [GO:0001832]; cell cycle arrest [GO:0007050]; cell proliferation [GO:0008283]; DNA damage checkpoint [GO:0000077]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; intrinsic apoptotic signaling pathway [GO:0097193]; isotype switching [GO:0045190]; meiotic cell cycle [GO:0051321]; mitotic cell cycle checkpoint [GO:0007093]; mitotic G2 DNA damage checkpoint [GO:0007095]; neuromuscular process controlling balance [GO:0050885]; positive regulation of kinase activity [GO:0033674]; positive regulation of protein autophosphorylation [GO:0031954]; regulation of DNA-dependent DNA replication initiation [GO:0030174]; telomere maintenance [GO:0000723]tdamaged DNA binding [GO:0003684]; protein N-terminus binding [GO:0047485]; transcription factor binding [GO:0008134]Mre11 complex [GO:0030870]; nuclear chromosome, telomeric region [GO:0000784]; nuclear inclusion body [GO:0042405]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; replication fork [GO:0005657]; site of double-strand break [GO:0035861]FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex. {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:15616588, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:9705271}.P63010AP2B1AP-2 complex subunit betaxSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274}. Membrane, coated pit {ECO:0000269|PubMed:14530274}; Peripheral membrane protein {ECO:0000269|PubMed:14530274}; Cytoplasmic side {ECO:0000269|PubMed:14530274}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.{antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin coat assembly [GO:0048268]; clathrin-mediated endocytosis [GO:0072583]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; neurotrophin TRK receptor si< gnaling pathway [GO:0048011]; regulation of defense response to virus by virus [GO:0050690]; synaptic transmission [GO:0007268]; viral process [GO:0016032]nclathrin binding [GO:0030276]; protein transporter activity [GO:0008565]; signal sequence binding [GO:0005048]'AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387}.P34897GLYM.Serine hydroxymethyltransferase, mitochondrialpSUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid. Mitochondrion inner membrane.glycine biosynthetic process from serine [GO:0019264]; L-serine biosynthetic process [GO:0006564]; one-carbon metabolic process [GO:0006730]; positive regulation of cell proliferation [GO:0008284]; protein homotetramerization [GO:0051289]; tetrahydrofolate interconversion [GO:0035999]amino acid binding [GO:0016597]; chromatin binding [GO:0003682]; glycine hydroxymethyltransferase activity [GO:0004372]; L-allo-threonine aldolase activity [GO:0008732]; pyridoxal phosphate binding [GO:0030170]extracellular exosome [GO:0070062]; microtubule cytoskeleton [GO:0015630]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]FUNCTION: Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA. {ECO:0000269|PubMed:21876188}.P51610HCFC1Host cell factor 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Nuclear in general, but uniquely cytoplasmic in trigeminal ganglia, becoming nuclear upon HSV reactivation from the latent state. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER.cell cycle [GO:0007049]; cellular response to organic cyclic compound [GO:0071407]; chromatin organization [GO:0006325]; histone H4-K16 acetylation [GO:0043984]; histone H4-K5 acetylation [GO:0043981]; histone H4-K8 acetylation [GO:0043982]; mitochondrion organization [GO:0007005]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; organelle organization [GO:0006996]; positive regulation of cell cycle [GO:0045787]; positive regulation of gene expression [GO:0010628]; protein stabilization [GO:0050821]; regulation of protein complex assembly [GO:0043254]; regulation of transcription, DNA-templated [GO:0006355]; release from viral latency [GO:0019046]; transcription from RNA polymerase II promoter [GO:0006366]^chromatin binding [GO:0003682]; identical protein binding [GO:0042802]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription coactivator activity [GO:0003713]Paxon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; histone acetyltransferase complex [GO:0000123]; membrane [GO:0016020]; mitochondrion [GO:0005739]; MLL1 complex [GO:0071339]; MLL5-L complex [GO:0070688]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]FUNCTION: Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes. {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:10779346, ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:12244100, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878, ECO:0000269|PubMed:17578910, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:9990006}.Q9P0S2COX16BCytochrome c oxidase assembly protein COX16 homolog, mitochondrialQ5M775CYTSB Cytospin-B<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15602574}.Q5T011SZT2 Protein SZT2central nervous system development [GO:0007417]; corpus callosum morphogenesis [GO:0021540]; pigmentation [GO:0043473]; post-embryonic development [GO:0009791]; regulation of superoxide dismutase activity [GO:1901668]FUNCTION: Involved in oxidative stress. May be involved in superoxide dismutase activity and in neuroprotective effect of peroxisomes, but has no direct dismutase activity when tested in yeast. May enhance epileptogenesis and confer low seizure threshold (By similarity). {ECO:0000250}.P00519ABL1Tyrosine-protein kinase ABL1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform IB: Nucleus membrane; Lipid-anchor. Note=The myristoylated c-ABL protein is reported to be nuclear.actin cytoskeleton organization [GO:0030036]; actin filament branching [GO:0090135]; activated T cell proliferation [GO:00507< 98]; alpha-beta T cell differentiation [GO:0046632]; autophagy [GO:0006914]; axon guidance [GO:0007411]; B-1 B cell homeostasis [GO:0001922]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; Bergmann glial cell differentiation [GO:0060020]; blood coagulation [GO:0007596]; cell cycle arrest [GO:0007050]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular protein modification process [GO:0006464]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to dopamine [GO:1903351]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to oxidative stress [GO:0034599]; cerebellum morphogenesis [GO:0021587]; collateral sprouting [GO:0048668]; DNA damage induced protein phosphorylation [GO:0006975]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; microspike assembly [GO:0030035]; mismatch repair [GO:0006298]; mitochondrial depolarization [GO:0051882]; mitotic nuclear division [GO:0007067]; muscle cell differentiation [GO:0042692]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cellular senescence [GO:2000773]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of phospholipase C activity [GO:1900275]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of ubiquitin-protein transferase activity [GO:0051444]; neuromuscular process controlling balance [GO:0050885]; peptidyl-tyrosine autophosphorylation [GO:0038083]; peptidyl-tyrosine phosphorylation [GO:0018108]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interferon-gamma secretion [GO:1902715]; positive regulation of interleukin-2 secretion [GO:1900042]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of neuron death [GO:1901216]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of oxidoreductase activity [GO:0051353]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; regulation of actin cytoskeleton reorganization [GO:2000249]; regulation of autophagy [GO:0010506]; regulation of cell adhesion [GO:0030155]; regulation of cell motility [GO:2000145]; regulation of cell proliferation [GO:0042127]; regulation of endocytosis [GO:0030100]; regulation of extracellular matrix organization [GO:1903053]; regulation of response to DNA damage stimulus [GO:2001020]; regulation of transcription, DNA-templated [GO:0006355]; response to oxidative stress [GO:0006979]; signal transduction in response to DNA damage [GO:0042770]; small GTPase mediated signal transduction [GO:0007264]; spleen development [GO:0048536]; substrate adhesion-dependent cell spreading [GO:0034446]; thymus development [GO:0048538]; transitional one stage B cell differentiation [GO:0002333]bactin monomer binding [GO:0003785]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase binding [GO:0051019]; nicotinate-nucleotide adenylyltransferase activity [GO:0004515]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; proline-rich region binding [GO:0070064]; protein C-terminus binding [GO:0008022]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; receptor binding [GO:0005102]; SH3 domain binding [GO:0017124]; syntaxin binding [GO:0019905]gactin cytoskeleton [GO:0015629]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]/FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. {ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, ECO:0000269|PubM< ed:16943190, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:9037071, ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.P0C0L4CO4AComplement C4-Acomplement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of apoptotic cell clearance [GO:2000427]; regulation of complement activation [GO:0030449]\complement component C1q binding [GO:0001849]; endopeptidase inhibitor activity [GO:0004866]/FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.; FUNCTION: Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.Q8N4X5AF1L2*Actin filament-associated protein 1-like 2>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17412687}.inflammatory response [GO:0006954]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of interleukin-6 production [GO:0032675]; regulation of mitotic cell cycle [GO:0007346]protein tyrosine kinase activator activity [GO:0030296]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; signaling adaptor activity [GO:0035591]FUNCTION: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation. {ECO:0000269|PubMed:17412687}.Q9UBT2SAE2 SUMO-activating enzyme subunit 2SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.cellular protein metabolic process [GO:0044267]; positive regulation of catalytic activity [GO:0043085]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]ATP binding [GO:0005524]; enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; SUMO activating enzyme activity [GO:0019948]qcytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SUMO activating enzyme complex [GO:0031510]FUNCTION: The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:11481243, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:17643372, ECO:0000269|PubMed:19443651, ECO:0000269|PubMed:20164921}.Q9Y224CN166UPF0568 protein C14orf166SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=May localize at the centrosome during mitosis. Shuttles between the cytosol and the nucleus: enters into the nucleus in case of active transcription while it accumulates in cytosol when transcription level is low (PubMed:24608264). {ECO:0000269|PubMed:24608264}.positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; RNA transport [GO:0050658]; transcription, DNA-templated [GO:0006351]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]; viral process [GO:0016032]identical protein binding [GO:0042802]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA polymerase II core binding [GO:0000993]cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; tRNA-splicing ligase complex [GO:0072669]FUNCTION: RNA-binding protein involved in modulation of mRNA transcription by Polymerase II. In case of infection by influenza virus A, is involved in viral replication. Component of the tRNA-splicing ligase complex and is required for tRNA ligation (PubMed:24870230). May be required for RNA transport (PubMed:24608264). {ECO:0000269|PubMed:16950395, ECO:0000269|PubMed:24608264, ECO:0000269|PubMed:24870230}.P24821TENATenascincell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]; mesenchymal-epithelial cell signaling involved in prostate gland development [GO:0060739]; neuromuscular junction development [GO:0007528]; osteoblast differentiation [GO:0001649]; peripheral nervous system axon regeneration [GO:0014012]; positive regulation of cell proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; prostate gland epithelium morphogenesis [GO:0060740]; response to wounding [GO:0009611]syndecan binding [GO:0045545]basement membrane [GO:0005604]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; interstitial matrix [GO:0005614]; membrane [GO:0016020]ZFUNCTION: Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.Q96SA4SERC2Serine incorporator 2L-serine transport [GO:0015825]; phosphatidylserine metabolic process [GO:0006658]; positive regulation of transferase activity [GO:0051347]; sphingolipid metabolic process [GO:0006665]Q96BM9ARL8A'ADP-ribosylation factor-like protein 8A@SUBCELLULAR LOCATION: Late endosome membrane. Lysosome membrane.cell division [GO:0051301]; chromosome segregation [GO:0007059]; mitotic nuclear division [GO:0007067]; small GTPase mediated signal transduction [GO:0007264]}alpha-tubulin binding [GO:0043014]; beta-tubulin binding [GO:0048487]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]FUNCTION: May play a role in lysosomes motility. Alternatively, may play a role in chromosome segregation (By similarity). {ECO:0000250}.Q49AJ0F135BProtein FAM135BP15924DESP Desmoplakin"SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000269|PubMed:12802069}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12802069}. Note=Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network.adherens junction organization [GO:0034332]; apoptotic process [GO:0006915]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; desmosome organization [GO:0002934]; epidermis development [GO:0008544]; intermediate filament organization [GO:0045109]; keratinocyte differentiation [GO:0030216]; peptide cross-linking [GO:0018149]; programmed cell death [GO:0012501]; protein localization to adherens junction [GO:0071896]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; ventricular compact myocardium morphogenesis [GO:0003223]; wound healing [GO:0042060]`cell adhesive protein binding involved in bundle of His cel< l-Purkinje myocyte communication [GO:0086083]; poly(A) RNA binding [GO:0044822]; protein binding, bridging [GO:0030674]; protein kinase C binding [GO:0005080]; scaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]3basolateral plasma membrane [GO:0016323]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin-plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.P78356PI42B5Phosphatidylinositol 5-phosphate 4-kinase type-2 beta]SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20583997}. Cytoplasm {ECO:0000269|PubMed:20583997}. Note=Associated with the plasma membrane and the endoplasmic reticulum. {ECO:0000250}.+cell surface receptor signaling pathway [GO:0007166]; intracellular signal transduction [GO:0035556]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphorylation [GO:0046854]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; receptor signaling protein activity [GO:0005057]ycytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]rFUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:9038203}.Q7L7X3TAOK1$Serine/threonine-protein kinase TAO1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:13679851}.activation of MAPKK activity [GO:0000186]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; execution phase of apoptosis [GO:0097194]; G2 DNA damage checkpoint [GO:0031572]; MAPK cascade [GO:0000165]; mitotic cell cycle [GO:0000278]; positive regulation of JNK cascade [GO:0046330]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein phosphorylation [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of cytoskeleton organization [GO:0051493]; regulation of mitotic cell cycle [GO:0007346]; signal transduction by protein phosphorylation [GO:0023014]; small GTPase mediated signal transduction [GO:0007264]; stress-activated protein kinase signaling cascade [GO:0031098]ATP binding [GO:0005524]; kinase activity [GO:0016301]; MAP kinase kinase kinase activity [GO:0004709]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; transferase activity [GO:0016740]FUNCTION: Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. {ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16407310, ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:17900936}.Q9UNA0ATS5@A disintegrin and metalloproteinase with thrombospondin motifs 5ccellular protein metabolic process [GO:0044267]; defense response to bacterium [GO:0042742]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; post-translational protein modification [GO:0043687]; protein O-linked fucosylation [GO:0036066]; protein O-linked glycosylation [GO:0006493]; proteolysis [GO:0006508]integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]|endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.P98175RBM10RNA-binding protein 10SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18315527}. Note=In the extranucleolar nucleoplasm constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, the nuclear bodies enlarge and decrease in number. They occur closely adjacent to nuclear speckles or IGCs (interchromatin granule clusters) but coincide with TIDRs (transcription-inactivation-dependent RNA domains).identical protein binding [GO:0042802]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; protein complex binding [GO:0032403]; zinc ion binding [GO:0008270]FUNCTION: May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) (By similarity). {ECO:0000250}.Q96FS4SIPA11Signal-induced proliferation-associated protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm, perinuclear region. Endomembrane system; Peripheral membrane protein. Note=Mostly localized in the perinuclear membraneous region.cell proliferation [GO:0008283]; cellular response to water deprivation [GO:0042631]; cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; positive regulation of GTPase activity [GO:0043547]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; transport vesicle [GO:0030133]FUNCTION: GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting it to the putatively inactive GDP-bound state. {ECO:0000269|PubMed:9346962}.Q15653IKBBNF-kappa-B inhibitor betaNF-kappa-B inhibitorscellular response to lipopolysaccharide [GO:0071222]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; innate immune response [GO:0045087]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; MyD88-independent toll-like receptor signaling pathway [GO:0002756]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of type I interferon production [GO:0032481]; signal transduction [GO:0007165]; toll-like receptor 10 signaling pathway [GO:0034166]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 3 signaling pathway [GO:0034138]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor 5 signaling pathway [GO:0034146]; toll-like receptor 9 signaling pathway [GO:00< 34162]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]; transcription, DNA-templated [GO:0006351]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]Xsignal transducer activity [GO:0004871]; transcription coactivator activity [GO:0003713]FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.P11532DMD DystrophinSUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Note=In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). {ECO:0000250}.cardiac muscle cell action potential [GO:0086001]; cardiac muscle contraction [GO:0060048]; cellular protein complex assembly [GO:0043623]; cellular protein localization [GO:0034613]; extracellular matrix organization [GO:0030198]; motile cilium assembly [GO:0044458]; muscle attachment [GO:0016203]; muscle cell cellular homeostasis [GO:0046716]; muscle fiber development [GO:0048747]; muscle filament sliding [GO:0030049]; muscle organ development [GO:0007517]; negative regulation of peptidyl-cysteine S-nitrosylation [GO:1902083]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; peptide biosynthetic process [GO:0043043]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of neuron projection development [GO:0010976]; positive regulation of sodium ion transmembrane transporter activity [GO:2000651]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cellular response to growth factor stimulus [GO:0090287]; regulation of heart rate [GO:0002027]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; regulation of skeletal muscle contraction [GO:0014819]; regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014809]; regulation of voltage-gated calcium channel activity [GO:1901385]; response to muscle stretch [GO:0035994](actin binding [GO:0003779]; dystroglycan binding [GO:0002162]; myosin binding [GO:0017022]; nitric-oxide synthase binding [GO:0050998]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270]cell-substrate junction [GO:0030055]; cell surface [GO:0009986]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dystrophin-associated glycoprotein complex [GO:0016010]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; membrane raft [GO:0045121]; neuron projection terminus [GO:0044306]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein complex [GO:0043234]; sarcolemma [GO:0042383]; synapse [GO:0045202]; syntrophin complex [GO:0016013]; Z disc [GO:0030018]FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission. {ECO:0000269|PubMed:16710609}.Q15648MED15Mediator of RNA polymerase II transcription subunit 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15471764, ECO:0000269|PubMed:16314496, ECO:0000269|PubMed:16574658}. Note=A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.v androgen biosynthetic process [GO:0006702]; androgen receptor signaling pathway [GO:0030521]; angiogenesis [GO:0001525]; brain development [GO:0007420]; cell morphogenesis [GO:0000902]; cellular lipid metabolic process [GO:0044255]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to steroid hormone stimulus [GO:0071383]; cellular response to thyroid hormone stimulus [GO:0097067]; embryonic heart tube development [GO:0035050]; embryonic hemopoiesis [GO:0035162]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic placenta development [GO:0001892]; enucleate erythrocyte development [GO:0048822]; epithelial cell proliferation involved in mammary gland duct elongation [GO:0060750]; ERK1 and ERK2 cascade [GO:0070371]; erythrocyte development [GO:0048821]; fat cell differentiation [GO:0045444]; gene expression [GO:0010467]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; keratinocyte differentiation [GO:0030216]; lactation [GO:0007595]; lens development in camera-type eye [GO:0002088]; liver development [GO:0001889]; mammary gland branching involved in pregnancy [GO:0060745]; mammary gland branching involved in thelarche [GO:0060744]; megakaryocyte development [GO:0035855]; monocyte differentiation [GO:0030224]; mRNA transcription from RNA polymerase II promoter [GO:0042789]; negative regulation of apoptotic process [GO:0043066]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; organ regeneration [GO:0031100]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of G0 to G1 transition [GO:0070318]; positive regulation of gene expression [GO:0010628]; positive regulation of hepatocyte proliferation [GO:2000347]; positive regulation of interferon-gamma-mediated signaling pathway [GO:0060335]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of mammary gland epithelial cell proliferation [GO:0033601]; positive regulation of protein import into nucleus, translocation [GO:0033160]; positive regulation of receptor activity [GO:2000273]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of RNA biosynthetic process [GO:2001141]; regulation of transcription from RNA polymerase I promoter [GO:0006356]; regulation of vitamin D receptor signaling pathway [GO:0070562]; retinal pigment epithelium development [GO:0003406]; small molecule metabolic process [GO:0044281]; thyroid hormone generation [GO:0006590]; thyroid hormone mediated signaling pathway [GO:0002154]; transcription initiation from RNA polymerase II promoter [GO:0006367]; ventricular trabecula myocardium morphogenesis [GO:0003222]dchromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; core promoter binding [GO:0001047]; estrogen receptor binding [GO:0030331]; LBD domain binding [GO:0050693]; ligand-dependent nuclear receptor binding [GO:0016922]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; mediator complex binding [GO:0036033]; nuclear hormone receptor binding [GO:0035257]; peroxisome proliferator activated receptor binding [GO:0042975]; receptor activity [GO:0004872]; retinoic acid receptor binding [GO:0042974]; RNA polymerase II core promoter proximal region sequence-specific DNA b< inding [GO:0000978]; RNA polymerase II transcription cofactor activity [GO:0001104]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; thyroid hormone receptor binding [GO:0046966]; thyroid hormone receptor coactivator activity [GO:0030375]; transcription coactivator activity [GO:0003713]; transcription cofactor activity [GO:0003712]; transcription factor binding [GO:0008134]; ubiquitin protein ligase activity [GO:0061630]; vitamin D receptor binding [GO:0042809]chromatin [GO:0000785]; mediator complex [GO:0016592]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; ubiquitin ligase complex [GO:0000151]FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, ECO:0000269|PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). {ECO:0000269|PubMed:10406464, ECO:0000269|PubMed:11867769, ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:12556447, ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15471764, ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16574658, ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:9653119}.P10586PTPRF,Receptor-type tyrosine-protein phosphatase FNcell adhesion [GO:0007155]; cell migration [GO:0016477]; negative regulation of receptor binding [GO:1900121]; neuron projection regeneration [GO:0031102]; peptidyl-tyrosine dephosphorylation [GO:0035335]; regulation of axon regeneration [GO:0048679]; transmembrane receptor protein tyrosine phosphatase signaling pathway [GO:0007185]heparin binding [GO:0008201]; protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001]extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]3FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; FUNCTION: The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.Q5VST6AB17B2Alpha/beta hydrolase domain-containing protein 17BP29016CD1B T-cell surface glycoprotein CD1bSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. Localizes to cell surface lipid rafts.xantigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]beta-2-microglobulin binding [GO:0030881]; endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723]cell surface [GO:0009986]; endosome membrane [GO:0010008]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]FUNCTION: Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:10981968, ECO:0000269|PubMed:14716313}.Q15061WDR43WD repeat-containing protein 43Q6UN15FIP1&Pre-mRNA 3'-end-processing factor FIP1 FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex. {ECO:0000269|PubMed:14749727}.Q96RT8GCP5!Gamma-tubulin complex component 5centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; gamma-tubulin ring complex [GO:0008274]; microtubule [GO:0005874]; nucleoplasm [GO:0005654]; spindle pole [GO:0000922]Q6UUV7CRTC3*CREB-regulated transcription coactivator 3LSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Appears to be mainly nuclear.energy homeostasis [GO:0097009]; macrophage activation [GO:0042116]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of lipid catabolic process [GO:0050995]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein homotetramerization [GO:0051289]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]:cAMP response element binding protein binding [GO:0008140]QFUNCTION: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). {ECO:0000269|PubMed:14506290, ECO:0000269|PubMed:15454081, ECO:0000269|PubMed:15466468, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:16980408, ECO:0000269|PubMed:17210223, ECO:0000269|PubMed:17644518}.O60287NPA1P,Nucleolar pre-ribosomal-associated protein 1dSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16963496}.P14778IL1R1Interleukin-1 receptor type 1 Receptor/ILRSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597}; Single-pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell membrane {ECO:0000305|PubMed:8142597}. Secreted {ECO:0000269|PubMed:8142597}.cell surface receptor signaling pathway [GO:0007166]; cellular response to glucose stimulus [GO:0071333]; heat acclimation [GO:0010286]; immune response [GO:0006955]; interleukin-1-mediated signaling pathway [GO:0070498]; ovulation [GO:0030728]; regulation of inflammatory response [GO:0050727]; response to epidermal growth factor [GO:0070849]; response to interleukin-1 [GO:0070555]; response to nitric oxide [GO:0071731]; response to radiation [GO:0009314]; response to transforming growth factor beta [GO:0071559] interleukin-1, Type I, activating receptor activity [GO:0004909]; interleukin-1 receptor activity [GO:0004908]; platelet-derived growth factor receptor binding [GO:0005161]; signal transducer activity [GO:0004871]; transmembrane signaling receptor activity [GO:0004888]axon [GO:0030424]; cell surface [GO:0009986]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; protein complex [GO:0043234]MFUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitme< nt of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. {ECO:0000269|PubMed:10671496}.Q96NT0CC115)Coiled-coil domain-containing protein 115ESUBCELLULAR LOCATION: Endosome {ECO:0000250}. Lysosome {ECO:0000250}.Cendosome [GO:0005768]; lysosome [GO:0005764]; membrane [GO:0016020]Q9C004SPY4Protein sprouty homolog 4SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12027893}. Cell projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.lmulticellular organismal development [GO:0007275]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]ocytoplasm [GO:0005737]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; ruffle membrane [GO:0032587]0FUNCTION: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras. Inhibits Ras-independent, but not Ras-dependent, activation of RAF1. {ECO:0000269|PubMed:12717443}.Q6NZY4ZCHC8,Zinc finger CCHC domain-containing protein 8gSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:21855801}. Note=Excluded from nucleolus.Q9Y3B2EXOS1Exosome complex component CSL4SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11812149}. Nucleus {ECO:0000305|PubMed:11812149}. Cytoplasm {ECO:0000305|PubMed:11812149}.cytoplasm [GO:0005737]; cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.O43760SNG2Synaptogyrin-2_SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cytoplasmic vesicle {ECO:0000250}.extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; neuromuscular junction [GO:0031594]; synaptic vesicle membrane [GO:0030672]Q9H3E2SNX25Sorting nexin-25SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:14975938}; Peripheral membrane protein {ECO:0000269|PubMed:14975938}. Note=Detected in endosome-derived secreted vesicles (exosomes) from malignant pleural effusions.Fnegative regulation of pathway-restricted SMAD protein phosphorylation [GO:0060394]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; protein transport [GO:0015031]; receptor catabolic process [GO:0032801]; termination of G-protein coupled receptor signaling pathway [GO:0038032]endosome membrane [GO:0010008]P40425PBX2*Pre-B-cell leukemia transcription factor 2embryonic limb morphogenesis [GO:0030326]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proximal/distal pattern formation [GO:0009954]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1. {ECO:0000269|PubMed:12609849}.Q6UXH9PAMR1Inactive serine protease PAMR1LFUNCTION: May play a role in regeneration of skeletal muscle. {ECO:0000250}.Q9NYB0TE2IP7Telomeric repeat-binding factor 2-interacting protein 1SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Chromosome. Chromosome, telomere. Note=Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex (By similarity). {ECO:0000250}.`negative regulation of DNA recombination at telomere [GO:0048239]; negative regulation of telomere maintenance [GO:0032205]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein acetylation [GO:1901985]; protection from non-homologous end joining at telomere [GO:0031848]; protein localization to chromosome, telomeric region [GO:0070198]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of transcription, DNA-templated [GO:0006355]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]; telomere maintenance via telomere lengthening [GO:0010833]; transcription, DNA-templated [GO:0006351]&chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nuclear chromosome [GO:0000228]; nuclear chromosome, telomeric region [GO:0000784]; nuclear envelope [GO:0005635]; nuclear telomere cap complex [GO:0000783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; telosome [GO:0070187]FUNCTION: Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes. {ECO:0000269|PubMed:16166375, ECO:0000269|PubMed:19763083}.Q14126DSG2 Desmoglein-2cSUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome.apoptotic process [GO:0006915]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell adhesion [GO:0007155]; cellular component disassembly involved in execution phase of apoptosis [GO:0006921]; desmosome organization [GO:0002934]; homophilic cell adhesion via< plasma membrane adhesion molecules [GO:0007156]; maternal process involved in female pregnancy [GO:0060135]; programmed cell death [GO:0012501]; Purkinje myocyte development [GO:0003165]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; response to progesterone [GO:0032570]calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication [GO:0086083],apical plasma membrane [GO:0016324]; cell-cell junction [GO:0005911]; cell surface [GO:0009986]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.O14757CHK1$Serine/threonine-protein kinase Chk1OSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B.cellular response to DNA damage stimulus [GO:0006974]; cellular response to mechanical stimulus [GO:0071260]; chromatin-mediated maintenance of transcription [GO:0048096]; DNA damage checkpoint [GO:0000077]; DNA damage induced protein phosphorylation [GO:0006975]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; G2/M transition of mitotic cell cycle [GO:0000086]; G2 DNA damage checkpoint [GO:0031572]; histone H3-T11 phosphorylation [GO:0035407]; negative regulation of mitotic nuclear division [GO:0045839]; peptidyl-threonine phosphorylation [GO:0018107]; regulation of cell proliferation [GO:0042127]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of histone H3-K9 acetylation [GO:2000615]; regulation of mitotic centrosome separation [GO:0046602]; regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage [GO:0010767]; replicative senescence [GO:0090399]ATP binding [GO:0005524]; histone kinase activity (H3-T11 specific) [GO:0035402]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]centrosome [GO:0005813]; chromatin [GO:0000785]; condensed nuclear chromosome [GO:0000794]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]m FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest.; FUNCTION: Isoform 2: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition.Q96P16RPR1A;Regulation of nuclear pre-mRNA domain-containing protein 1AEdephosphorylation of RNA polymerase II C-terminal domain [GO:0070940]2FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle. {ECO:0000269|PubMed:22231121}.O95801TTC4"Tetratricopeptide repeat protein 4O14773TPP1Tripeptidyl-peptidase 1SUBCELLULAR LOCATION: Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.5bone resorption [GO:0045453]; cellular protein metabolic process [GO:0044267]; central nervous system development [GO:0007417]; endoplasmic reticulum unfolded protein response [GO:0030968]; epithelial cell differentiation [GO:0030855]; IRE1-mediated unfolded protein response [GO:0036498]; lipid metabolic process [GO:0006629]; lysosome organization [GO:0007040]; nervous system development [GO:0007399]; neuromuscular process controlling balance [GO:0050885]; peptide catabolic process [GO:0043171]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508] endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; tripeptidyl-peptidase activity [GO:0008240]extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; melanosome [GO:0042470]; mitochondrion [GO:0005739](FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity). {ECO:0000250}.Q86V88MGDP1!Magnesium-dependent phosphatase 1Rmetal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]aFUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine phosphatase. {ECO:0000250}.A5PLN9TPC13/Trafficking protein particle complex subunit 13Q8WWI5CTL1"Choline transporter-like protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein {ECO:0000269|PubMed:19357133}. Mitochondrion outer membrane {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein {ECO:0000269|PubMed:19357133}.choline transport [GO:0015871]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]7choline transmembrane transporter activity [GO:0015220]extracellular exosome [GO:0070062]; integral component of membrane [GO< :0016021]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886]zFUNCTION: Choline transporter. May be involved in membrane synthesis and myelin production. {ECO:0000269|PubMed:19357133}.Q86U86PB1Protein polybromo-1'chromatin remodeling [GO:0006338]; heart development [GO:0007507]; mitotic nuclear division [GO:0007067]; negative regulation of cell proliferation [GO:0008285]; placenta development [GO:0001890]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]XBAF-type complex [GO:0090544]; kinetochore [GO:0000776]; nuclear chromosome [GO:0000228]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752}.Q9Y3Z3SAMH17Deoxynucleoside triphosphate triphosphohydrolase SAMHD1YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:23092512}.Ocytokine-mediated signaling pathway [GO:0019221]; dATP catabolic process [GO:0046061]; defense response to virus [GO:0051607]; dGTP catabolic process [GO:0006203]; immune response [GO:0006955]; protein homotetramerization [GO:0051289]; regulation of innate immune response [GO:0045088]; type I interferon signaling pathway [GO:0060337]dGTPase activity [GO:0008832]; dGTP binding [GO:0032567]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]hintracellular [GO:0005622]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Host restriction nuclease that blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May function by reducing the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. May play a role in mediating proinflammatory responses to TNF-alpha signaling. {ECO:0000269|PubMed:18546154, ECO:0000269|PubMed:19525956, ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:24336198}.Q9Y2B9IPKG-cAMP-dependent protein kinase inhibitor gammanegative regulation of cAMP-dependent protein kinase activity [GO:2000480]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; signal transduction [GO:0007165]=cAMP-dependent protein kinase inhibitor activity [GO:0004862]FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. {ECO:0000250}.Q02880TOP2BDNA topoisomerase 2-betaSaxonogenesis [GO:0007409]; DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]; forebrain development [GO:0030900]; mitotic DNA integrity checkpoint [GO:0044774]; neuron migration [GO:0001764]; resolution of meiotic recombination intermediates [GO:0000712]; sister chromatid segregation [GO:0000819]ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding, bending [GO:0008301]; DNA topoisomerase type II (ATP-hydrolyzing) activity [GO:0003918]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; protein C-terminus binding [GO:0008022]; protein heterodimerization activity [GO:0046982]; protein kinase C binding [GO:0005080]cytoplasm [GO:0005737]; cytosol [GO:0005829]; DNA topoisomerase complex (ATP-hydrolyzing) [GO:0009330]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. {ECO:0000269|PubMed:10684600}.Q9UMY1NOL7Nucleolar protein 7SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16205646}.Q9H840GEMI7Gem-associated protein 7OSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:12065586}. Nucleus, gem {ECO:0000269|PubMed:12065586}. Cytoplasm {ECO:0000269|PubMed:12065586}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; spliceosomal snRNP assembly [GO:0000387]cytoplasm [GO:0005737]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]kFUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. {ECO:0000269|PubMed:12065586, ECO:0000269|PubMed:18984161}.Q9ULX3NOB1RNA-binding protein NOB1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16172919}.visual perception [GO:0007601].FUNCTION: May play a role in mRNA degradation.Q8NBT2SPC24Kinetochore protein Spc24SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores from late prophase to anaphase. Localizes specifically to the outer plate of the kinetochore.condensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; Ndc80 complex [GO:0031262]; nucleolus [GO:0005730]; nucleus [GO:0005634]DFUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. {ECO:0000269|PubMed:14738735}.Q86Y37CACL16CDK2-associated and cullin domain-containing protein 1G1/S transition of mitotic cell cycle [GO:0000082]; positive regulation of cell proliferation [GO:0008284]; positive regulation of protein kinase activity [GO:0045860]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]'anaphase-promoting complex [GO:0005680]FUNCTION: Cell cycle associated protein capable of promoting cell proliferation through the activation of CDK2 at the G1/S phase transition. {ECO:0000269|PubMed:19829063}.Q96I51WBS166Williams-Beuren syndrome chromosomal region 16 proteinQ14746COG2,Conserved oligomeric Golgi complex subunit 2SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; oligosaccharide biosynthetic process [GO:0009312]; protein glycosylation [GO:0006486]qcytosol [GO:0005829]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; Golgi transport complex [GO:0017119]<FUNCTION: Required for normal Golgi morphology and function.Q9Y580RBM7RNA-binding protein 7meiotic cell cycle [GO:0051321]DFUNCTION: Possible involved in germ cell RNA processing and meiosis.Q8N5J2FA63AProtein FAM63ARextracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]P00736C1RComplement C1r subcomponentcomplement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; immune< response [GO:0006955]; innate immune response [GO:0045087]~calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.P51178PLCD1A1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1gangiogenesis [GO:0001525]; inositol phosphate metabolic process [GO:0043647]; intracellular signal transduction [GO:0035556]; labyrinthine layer blood vessel development [GO:0060716]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; regulation of cell proliferation [GO:0042127]; small molecule metabolic process [GO:0044281];calcium ion binding [GO:0005509]; GTPase activating protein binding [GO:0032794]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylinositol phospholipase C activity [GO:0004435]; phosphatidylserine binding [GO:0001786]; signal transducer activity [GO:0004871]FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.O00291HIP1 Huntingtin-interacting protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cell differentiation [GO:0030154]; clathrin coat assembly [GO:0048268]; clathrin-mediated endocytosis [GO:0072583]; positive regulation of receptor-mediated endocytosis [GO:0048260]; regulation of apoptotic process [GO:0042981]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]}clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]; structural constituent of cytoskeleton [GO:0005200]clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]FUNCTION: Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors. {ECO:0000269|PubMed:11007801, ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:11577110, ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:12163454, ECO:0000269|PubMed:14732715, ECO:0000269|PubMed:16027218, ECO:0000269|PubMed:9147654}.Q01105SET Protein SETSUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus, nucleoplasm. Note=In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium.DNA replication [GO:0006260]; gene expression [GO:0010467]; mitotic cell cycle [GO:0000278]; negative regulation of catalytic activity [GO:0043086]; negative regulation of histone acetylation [GO:0035067]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleocytoplasmic transport [GO:0006913]; nucleosome assembly [GO:0006334]; nucleosome disassembly [GO:0006337]; regulation of protein phosphatase type 2A activity [GO:0034047]; viral process [GO:0016032]DNA binding [GO:0003677]; histone binding [GO:0042393]; protein phosphatase inhibitor activity [GO:0004864]; protein phosphatase type 2A regulator activity [GO:0008601]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]FUNCTION: Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher. {ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12628186}.Q53TN4CYBR1Cytochrome b reductase 1xSUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12949720}; Multi-pass membrane protein {ECO:0000269|PubMed:12949720}.cellular iron ion homeostasis [GO:0006879]; oxidation-reduction process [GO:0055114]; response to iron ion [GO:0010039]; transmembrane transport [GO:0055085]ferric-chelate reductase activity [GO:0000293]; metal ion binding [GO:0046872]; oxidoreductase activity, oxidizing metal ions [GO:0016722]brush border membrane [GO:0031526]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). Present at the brush border of duodenal enterocytes where it probably reduces dietary Fe(3+) thereby facilitating its transport into the mucosal cells. Uses ascorbate as electron donor. May be involved in extracellular ascorbate recycling in erythrocyte membranes. May also act as a ferrireductase in airway epithelial cells. {ECO:0000269|PubMed:16521311, ECO:0000269|PubMed:16521312, ECO:0000269|PubMed:17068337, ECO:0000269|PubMed:19673882}.O75691UTP20-Small subunit processome component 20 homologSUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16458307}. Note=Colocalizes with NCL in the nucleolus.endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000472]; negative regulation of cell proliferation [GO:0008285]; rRNA processing [GO:0006364]90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; preribosome, small subunit precursor [GO:0030688]; small-subunit processome [GO:0032040]hFUNCTION: Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. {ECO:0000269|PubMed:17498821}.P36956SRBP1+Sterol regulatory element-binding protein 1ySUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pas< s membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols.; SUBCELLULAR LOCATION: Processed sterol regulatory element-binding protein 1: Nucleus.; SUBCELLULAR LOCATION: Isoform SREBP-1aDelta: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:18267114}.; SUBCELLULAR LOCATION: Isoform SREBP-1cDelta: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:18267114}.}aging [GO:0007568]; cellular response to fatty acid [GO:0071398]; cellular response to starvation [GO:0009267]; cholesterol metabolic process [GO:0008203]; circadian rhythm [GO:0007623]; insulin receptor signaling pathway [GO:0008286]; lipid biosynthetic process [GO:0008610]; lipid metabolic process [GO:0006629]; lung development [GO:0030324]; negative regulation of insulin secretion [GO:0046676]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of histone deacetylation [GO:0031065]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of fatty acid metabolic process [GO:0019217]; regulation of heart rate by chemical signal [GO:0003062]; regulation of mitochondrion degradation [GO:1903146]; regulation of protein stability [GO:0031647]; regulation of protein targeting to mitochondrion [GO:1903214]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to cAMP [GO:0051591]; response to drug [GO:0042493]; response to food [GO:0032094]; response to glucagon [GO:0033762]; response to glucose [GO:0009749]; response to progesterone [GO:0032570]; response to retinoic acid [GO:0032526]; small molecule metabolic process [GO:0044281]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; sequence-specific DNA binding transcription factor activity [GO:0003700]; sterol response element binding [GO:0032810]icytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the fatty acid and to a lesser degree the cholesterol synthesis pathway (By similarity). Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). {ECO:0000250|UniProtKB:Q9WTN3}.Q96AT1K1143 Uncharacterized protein KIAA1143Q5T6V5CI064UPF0553 protein C9orf64P52732KIF11Kinesin-like protein KIF11SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19001501}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19001501}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; microtubule-based movement [GO:0007018]; mitotic centrosome separation [GO:0007100]; mitotic nuclear division [GO:0007067]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; regulation of mitotic centrosome separation [GO:0046602]; spindle organization [GO:0007051]ATP binding [GO:0005524]; ATP-dependent microtubule motor activity, plus-end-directed [GO:0008574]; microtubule motor activity [GO:0003777]; protein complex binding [GO:0032403]; protein kinase binding [GO:0019901]cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; spindle [GO:0005819]; spindle pole [GO:0000922]FUNCTION: Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays. {ECO:0000269|PubMed:19001501}.P58397ATS12AA disintegrin and metalloproteinase with thrombospondin motifs 12cell-matrix adhesion [GO:0007160]; cell migration [GO:0016477]; cellular response to BMP stimulus [GO:0071773]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; negative regulation of cellular response to hepatocyte growth factor stimulus [GO:2001113]; negative regulation of cellular response to vascular endothelial growth factor stimulus [GO:1902548]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of hepatocyte growth factor receptor signaling pathway [GO:1902203]; proteoglycan catabolic process [GO:0030167]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of endothelial tube morphogenesis [GO:1901509]; regulation of inflammatory response [GO:0050727]FUNCTION: Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties. {ECO:0000269|PubMed:16611630, ECO:0000269|PubMed:17895370, ECO:0000269|PubMed:18485748}.Q9NRK6ABCBA:ATP-binding cassette sub-family B member 10, mitochondrialdintegral component of mitochondrial membrane [GO:0032592]; mitochondrial inner membrane [GO:0005743]mFUNCTION: May mediate critical mitochondrial transport functions related to heme biosynthesis. {ECO:0000250}.O75554WBP4WW domain-binding protein 4SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}./mRNA cis splicing, via spliceosome [GO:0045292]jnucleic acid binding [GO:0003676]; proline-rich region binding [GO:0070064]; zinc ion binding [GO:0008270]unuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; spliceosomal complex [GO:0005681]FUNCTION: Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex. {ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}.O43396TXNL1Thioredoxin-like protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349277}. Nucleus {ECO:0000269|PubMed:19349277}. Note=At least 85% of the cellular TXNL1 is proteasome-associated.cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glycerol ether metabolic process [GO:0006662]; oxidation-reduction process [GO:0055114]; protein folding [GO:0006457]; sulfate assimilation [GO:0000103]disulfide oxidoreductase activity [GO:0015036]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671]; protein disulfide oxidoreductase activity [GO:0015035]qcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; proteasome complex [GO:0000502]dFUNCTION: Active thioredoxin with a redox potential of about -250 mV. {ECO:0000269|PubMed:19349277}.Q96LB3IFT74+Intraflagellar transport protein 74 homologSUBCELLULAR LOCATION: Cell projection, cilium. Cytoplasmic vesicle. Note=Localizes along primary cilia at interphase and around the basal body/centriole at interphase and mitosis.cilium assembly [GO:0042384]; intraciliary transport involved in cilium morphogenesis [GO:0035735]; keratinocyte development [GO:0003334]; negative regulation of epithelial cell proliferation [GO:0050680]; Notch signaling pathway [GO:0007219]; organelle organization [GO:0006996]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]Abeta-tubulin bindi< ng [GO:0048487]; chromatin binding [GO:0003682]centrosome [GO:0005813]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytoplasmic membrane-bounded vesicle [GO:0016023]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514]; nucleus [GO:0005634]; primary cilium [GO:0072372]FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT81, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds beta-tubulin via its basic region. Required for ciliogenesis. {ECO:0000269|PubMed:23990561}.P16671CD36Platelet glycoprotein 4SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Note=Upon ligand-binding, internalized through dynamin-dependent endocytosis. {ECO:0000269|PubMed:20037584}. antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; apoptotic cell clearance [GO:0043277]; blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular lipid metabolic process [GO:0044255]; cellular response to bacterial lipopeptide [GO:0071221]; cellular response to hydroperoxide [GO:0071447]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO:0071223]; cGMP-mediated signaling [GO:0019934]; cholesterol transport [GO:0030301]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; lipoprotein transport [GO:0042953]; long-chain fatty acid import [GO:0044539]; low-density lipoprotein particle clearance [GO:0034383]; low-density lipoprotein particle mediated signaling [GO:0055096]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of growth of symbiont in host [GO:0044130]; negative regulation of transcription factor import into nucleus [GO:0042992]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nitric oxide mediated signal transduction [GO:0007263]; phagocytosis, recognition [GO:0006910]; plasma lipoprotein particle clearance [GO:0034381]; plasma membrane long-chain fatty acid transport [GO:0015911]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive regulation of blood coagulation [GO:0030194]; positive regulation of blood microparticle formation [GO:2000334]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of tumor necrosis factor production [GO:0032760]; receptor-mediated endocytosis [GO:0006898]; regulation of removal of superoxide radicals [GO:2000121]; response to stilbenoid [GO:0035634]; small molecule metabolic process [GO:0044281]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; toll-like receptor TLR1:TLR2 signaling pathway [GO:0038123]; toll-like receptor TLR6:TLR2 signaling pathway [GO:0038124]high-density lipoprotein particle binding [GO:0008035]; lipid binding [GO:0008289]; lipoprotein particle binding [GO:0071813]; lipoteichoic acid receptor activity [GO:0070892]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein receptor activity [GO:0005041]; thrombospondin receptor activity [GO:0070053]; transforming growth factor beta binding [GO:0050431]cell surface [GO:0009986]; endocytic vesicle membrane [GO:0030666]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; membrane raft [GO:0045121]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]FUNCTION: Binds to collagen, thrombospondin, anionic phospholipids and oxidized low-density lipoprotein (oxLDL). May function as a cell adhesion molecule. Directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes. Binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Receptor for thombospondins, THBS1 AND THBS2, mediating their antiangiogenic effects. As a coreceptor for TLR4-TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, rapidly induces the formation of a heterodimer of TLR4 and TLR6, which is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. {ECO:0000269|PubMed:10890433, ECO:0000269|PubMed:12506336, ECO:0000269|PubMed:20037584}.P12004PCNA"Proliferating cell nuclear antigenProliferating regulatorSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24939902}. Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. {ECO:0000269|PubMed:24939902}.base-excision repair [GO:0006284]; cell proliferation [GO:0008283]; cellular response to UV [GO:0034644]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; epithelial cell differentiation [GO:0030855]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; G1/S transition of mitotic cell cycle [GO:0000082]; heart development [GO:0007507]; leading strand elongation [GO:0006272]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; positive regulation of deoxyribonuclease activity [GO:0032077]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; response to cadmium ion [GO:0046686]; response to lipid [GO:0033993]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; dinucleotide insertion or deletion binding [GO:0032139]; DNA polymerase binding [GO:0070182]; DNA polymerase processivity factor activity [GO:0030337]; histone acetyltransferase binding [GO:0035035]; identical protein binding [GO:0042802]; MutLalpha complex binding [GO:0032405]; purine-specific mismatch base pair DNA N-glycosylase activity [GO:0000701]; receptor tyrosine kinase binding [GO:0030971]centrosome [GO:0005813]; cytoplasm [GO:0005737]; DNA replication factor C complex [GO:0005663]; extracellular exosome [GO:0070062]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PCNA complex [GO:0043626]; PCNA-p21 complex [GO:0070557]>FUNCTION: Auxiliary protein of< DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed:24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion. {ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:24939902}.P39210MPV17 Protein Mpv17SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16582907, ECO:0000269|PubMed:16582910}; Multi-pass membrane protein {ECO:0000269|PubMed:16582907, ECO:0000269|PubMed:16582910}.+cellular response to reactive oxygen species [GO:0034614]; glomerular basement membrane development [GO:0032836]; homeostatic process [GO:0042592]; inner ear development [GO:0048839]; mitochondrial genome maintenance [GO:0000002]; regulation of reactive oxygen species metabolic process [GO:2000377]integral component of membrane [GO:0016021]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]FUNCTION: Involved in mitochondria homeostasis. May be involved in the metabolism of reactive oxygen species and control of oxidative phosphorylation and mitochondrial DNA (mtDNA) maintenance.Q8IVB5LIX1LLIX1-like proteinQ99933BAG1*BAG family molecular chaperone regulator 1SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm. Note=Isoform 1 localizes predominantly to the nucleus.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Note=Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.; SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus. Note=Isoform 4 localizes predominantly to the cytoplasm. The cellular background in which it is expressed can influence whether it resides primarily in the cytoplasm or is also found in the nucleus. In the presence of BCL2, localizes to intracellular membranes (what appears to be the nuclear envelope and perinuclear membranes) as well as punctate cytosolic structures suggestive of mitochondria.Vapoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular response to heat [GO:0034605]; chaperone cofactor-dependent protein refolding [GO:0070389]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; regulation of cellular response to heat [GO:1900034]UFUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli. {ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9873016}.P28347TEAD1%Transcriptional enhancer factor TEF-1YAP/proproliferationgene expression [GO:0010467]; hippo signaling [GO:0035329]; transcription initiation from RNA polymerase II promoter [GO:0006367]FUNCTION: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.P09874PARP1Poly [ADP-ribose] polymerase 1YSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=Localizes at sites of DNA damage.!base-excision repair [GO:0006284]; behavioral response to cocaine [GO:0048148]; cellular protein metabolic process [GO:0044267]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxidative stress [GO:0034599]; cellular response to superoxide [GO:0071451]; DNA damage response, detection of DNA damage [GO:0042769]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; gene expression [GO:0010467]; macrophage differentiation [GO:0030225]; mitochondrial DNA metabolic process [GO:0032042]; mitochondrial DNA repair [GO:0043504]; mitochondrion organization [GO:0007005]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of SMAD protein import into nucleus [GO:0060391]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; post-translational protein modification [GO:0043687]; protein ADP-ribosylation [GO:0006471]; protein autoprocessing [GO:0016540]; protein modification process [GO:0036211]; protein poly-ADP-ribosylation [GO:0070212]; protein sumoylation [GO:0016925]; regulation of growth rate [GO:0040009]; signal transduction involved in regulation of gene expression [GO:0023019]; telomere maintenance [GO:0000723]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD binding [GO:0051287]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]; transcription factor binding [GO:0008134]; zinc ion binding [GO:0008270]membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]; transcription factor complex [GO:0005667]dFUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:23230272}.Q12884SEPRProlyl endopeptidase FAP` SUBCELLULAR LOCATION: Prolyl endopeptid< ase FAP: Cell surface {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242}. Cell membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:2172980}; Single-pass type II membrane protein {ECO:0000255}. Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}.; SUBCELLULAR LOCATION: Antiplasmin-cleaving enzyme FAP, soluble form: Secreted {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}. Note=Found in blood plasma and serum. {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000303|PubMed:10644713}.angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; endothelial cell migration [GO:0043542]; melanocyte apoptotic process [GO:1902362]; melanocyte proliferation [GO:0097325]; mitotic cell cycle arrest [GO:0071850]; negative regulation of cell proliferation involved in contact inhibition [GO:0060244]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of extracellular matrix organization [GO:1903054]; positive regulation of cell cycle arrest [GO:0071158]; positive regulation of execution phase of apoptosis [GO:1900119]; proteolysis [GO:0006508]; proteolysis involved in cellular protein catabolic process [GO:0051603]; regulation of collagen catabolic process [GO:0010710]; regulation of fibrinolysis [GO:0051917]dipeptidyl-peptidase activity [GO:0008239]; endopeptidase activity [GO:0004175]; integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; protease binding [GO:0002020]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]apical part of cell [GO:0045177]; basal part of cell [GO:0045178]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; invadopodium membrane [GO:0071438]; lamellipodium [GO:0030027]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] FUNCTION: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16480718, PubMed:16410248, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219, PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. {ECO:0000250|UniProtKB:P97321, ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:21288888, ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413}.Q96F44TRI11"E3 ubiquitin-protein ligase TRIM11defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of neurogenesis [GO:0050768]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral release from host cell [GO:1902187]; negative regulation of viral transcription [GO:0032897]; positive regulation of viral entry into host cell [GO:0046598]VFUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation p< athway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. {ECO:0000269|PubMed:18248090}.P60953CDC42(Cell division control protein 42 homologpSUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Note=Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells. Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome., actin cytoskeleton organization [GO:0030036]; actin filament branching [GO:0090135]; actin filament bundle assembly [GO:0051017]; adherens junction organization [GO:0034332]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; canonical Wnt signaling pathway [GO:0060070]; cardiac conduction system development [GO:0003161]; cellular protein localization [GO:0034613]; dendritic cell migration [GO:0036336]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell-cell adhesion [GO:0090136]; epithelial-mesenchymal cell signaling [GO:0060684]; establishment of Golgi localization [GO:0051683]; establishment or maintenance of apical/basal cell polarity [GO:0035088]; establishment or maintenance of cell polarity [GO:0007163]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; filopodium assembly [GO:0046847]; Golgi organization [GO:0007030]; hair follicle morphogenesis [GO:0031069]; hair follicle placode formation [GO:0060789]; heart contraction [GO:0060047]; innate immune response [GO:0045087]; keratinization [GO:0031424]; keratinocyte development [GO:0003334]; macrophage differentiation [GO:0030225]; multicellular organism growth [GO:0035264]; muscle cell differentiation [GO:0042692]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of gene expression [GO:0010629]; negative regulation of protein complex assembly [GO:0031333]; neuron fate determination [GO:0048664]; nuclear migration [GO:0007097]; organelle transport along microtubule [GO:0072384]; positive regulation of cytokinesis [GO:0032467]; positive regulation of DNA replication [GO:0045740]; positive regulation of epithelial cell proliferation involved in lung morphogenesis [GO:0060501]; positive regulation of gene expression [GO:0010628]; positive regulation of hair follicle cell proliferation [GO:0071338]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of JNK cascade [GO:0046330]; positive regulation of metalloenzyme activity [GO:0048554]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552]; positive regulation of pseudopodium assembly [GO:0031274]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of synapse structural plasticity [GO:0051835]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; regulation of filopodium assembly [GO:0051489]; regulation of mitotic nuclear division [GO:0007088]; regulation of protein catabolic process [GO:0042176]; regulation of protein heterodimerization activity [GO:0043497]; regulation of protein kinase activity [GO:0045859]; regulation of protein stability [GO:0031647]; regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase mediated signal transduction [GO:0007264]; sprouting angiogenesis [GO:0002040]; submandibular salivary gland formation [GO:0060661]; substantia nigra development [GO:0021762]; T cell costimulation [GO:0031295]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]apolipoprotein A-I receptor binding [GO:0034191]; GTPase activity [GO:0003924]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; thioesterase binding [GO:0031996]apical part of cell [GO:0045177]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; leading edge membrane [GO:0031256]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; spindle midzone [GO:0051233]wFUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration. {ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:17038317}.O15446RPA34+DNA-directed RNA polymerase I subunit RPA34SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9426281}. Chromosome {ECO:0000269|PubMed:9426281}. Note=Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes.gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; regulation of gene expression, epigenetic [GO:0040029]; rRNA transcription [GO:0009303]; termination of RNA polymerase I transcription [GO:0006363]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase I promoter [GO:0006361]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]SDNA-directed RNA polymerase activity [GO:0003899]; poly(A) RNA binding [GO:0044822]chromosome [GO:0005694]; cytoplasm [GO:0005737]; DNA-directed RNA polymerase I complex [GO:0005736]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I transcription factor complex [GO:0000120]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.; FUNCTION: Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex.P46736BRCC3%Lys-63-specific deubiquitinase BRCC36SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).bdouble-strand break repair [GO:0006302]; G2 DNA damage checkpoint [GO:0031572]; histone H2A K63-linked deubiquitination [GO:0070537]; positive regulation of DNA repair [GO:0045739]; prot< ein K63-linked deubiquitination [GO:0070536]; regulation of catalytic activity [GO:0050790]; response to ionizing radiation [GO:0010212]; response to X-ray [GO:0010165]enzyme regulator activity [GO:0030234]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; polyubiquitin binding [GO:0031593]; ubiquitin-specific protease activity [GO:0004843]BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; nuclear ubiquitin ligase complex [GO:0000152]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]hFUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. {ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:16707425, ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:19202061, ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}.Q8TBZ6TM10A#tRNA methyltransferase 10 homolog AnSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24204302}. Nucleus, nucleolus {ECO:0000269|PubMed:24204302}.dmethyltransferase activity [GO:0008168]; poly(A) RNA binding [GO:0044822]; tRNA binding [GO:0000049]Pextracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]?FUNCTION: RNA methyltransferase. {ECO:0000269|PubMed:25053765}.O15120PLCB31-acyl-sn-glycerol-3-phosphate acyltransferase betaCDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; epidermis development [GO:0008544]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of cytokine production [GO:0001819]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711}.Q00613HSF1Heat shock factor protein 1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules.cellular response to heat [GO:0034605]; defense response [GO:0006952]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; female meiotic division [GO:0007143]; mRNA transcription [GO:0009299]; negative regulation of cell proliferation [GO:0008285]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of cellular response to heat [GO:1900034]; response to lipopolysaccharide [GO:0032496]; spermatogenesis [GO:0007283]chromatin binding [GO:0003682]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001078]; RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding [GO:0001162]; sequence-specific DNA binding transcription factor activity [GO:0003700]}cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; pronucleus [GO:0045120]; protein complex [GO:0043234]FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. {ECO:0000269|PubMed:11447121, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12659875, ECO:0000269|PubMed:12665592, ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:8946918, ECO:0000269|PubMed:9121459, ECO:0000269|PubMed:9535852}.Q14657LAGE3EKC/KEOPS complex subunit LAGE3FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. LAGE3 functions as a dimerization module for the complex (By similarity). {ECO:0000250}.Q8NFA0UBP32(Ubiquitin carboxyl-terminal hydrolase 32xSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:20549504}.calcium ion binding [GO:0005509]; cysteine-type endopeptidase activity [GO:0004197]; ubiquitin-specific protease activity [GO:0004843]Kcytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]Q8WWI1LMO7LIM domain only protein 7sprotein ubiquitination [GO:0016567]; regulation of cell adhesion [GO:0030155]; regulation of signaling [GO:0023051]pcytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]Q12899TRI26&Tripartite motif-containing protein 26rcytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral release from host cell [GO:1902187]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]WDNA binding [GO:0003677]; metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]O14929HAT12Histone acetyltransferase type B catalytic subunitISUBCELLULAR LOCATION: Isoform A: Nucleus matrix.; SUBCELLULAR LOCATION: Isoform B: Cytoplasm. Nucleus. Nucleus matrix. Nucleus, nucleoplasm. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein.echromatin organization [GO:0006325]; chromatin silencing at telomere [GO:0006348]; DNA packaging [GO:0006323]; DNA replication-dependent nucleosome assembly [GO:0006335]; DNA replication-independent nucleosome assembly [GO:0006336]; histone H4 acetylation [GO:0043967]; internal protein amino acid acetylation [GO:0006475]; response to nutrient [GO:0007584]H4 histone acetyltransferase activity [GO:0010485]; histone acetyltransferase activity [GO:0004402]; histone binding [GO:0042393]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear chromatin [GO:0000790]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]5FUNCTION: Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical dam< age. {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644}.P51884LUMLumicancarbohydrate metabolic process [GO:0005975]; cartilage development [GO:0051216]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate biosynthetic process [GO:0018146]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; positive regulation of transforming growth factor beta1 production [GO:0032914]; response to growth factor [GO:0070848]; response to organic cyclic compound [GO:0014070]; small molecule metabolic process [GO:0044281]; visual perception [GO:0007601]Wcollagen binding [GO:0005518]; extracellular matrix structural constituent [GO:0005201]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrillar collagen trimer [GO:0005583]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; proteinaceous extracellular matrix [GO:0005578]Q04724TLE1"Transducin-like enhancer protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12397081}. Note=Nuclear and chromatin-associated, depending on isoforms and phosphorylation status. Hyperphosphorylation decreases the affinity for nuclear components.multicellular organismal development [GO:0007275]; negative regulation of anoikis [GO:2000811]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of Wnt signaling pathway [GO:0030178]; Notch signaling pathway [GO:0007219]; organ morphogenesis [GO:0009887]; positive regulation of gene expression [GO:0010628]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]chromatin binding [GO:0003682]; identical protein binding [GO:0042802]; RNA polymerase II transcription corepressor activity [GO:0001106]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]FUNCTION: Transcriptional corepressor that binds to a number of transcription factors. Inhibits NF-kappa-B-regulated gene expression. Inhibits the transcriptional activation mediated by FOXA2, and by CTNNB1 and TCF family members in Wnt signaling. The effects of full-length TLE family members may be modulated by association with dominant-negative AES. Unusual function as coactivator for ESRRG. {ECO:0000269|PubMed:10660609}.P58107EPIPL EpiplakinQ9P2Q2FRM4A!FERM domain-containing protein 4A6establishment of epithelial cell polarity [GO:0090162]Ybicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]P34059GALNS!N-acetylgalactosamine-6-sulfatasecarbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; small molecule metabolic process [GO:0044281]metal ion binding [GO:0046872]; N-acetylgalactosamine-4-sulfatase activity [GO:0003943]; N-acetylgalactosamine-6-sulfatase activity [GO:0043890]; sulfuric ester hydrolase activity [GO:0008484]P15144AMPNAminopeptidase NSUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Cytoplasm, cytosol {ECO:0000305}. Note=A soluble form has also been detected.angiogenesis [GO:0001525]; angiotensin maturation [GO:0002003]; cell differentiation [GO:0030154]; cellular protein metabolic process [GO:0044267]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; metallopeptidase activity [GO:0008237]; peptide binding [GO:0042277]; receptor activity [GO:0004872]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270]!cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; lysosomal membrane [GO:0005765]|FUNCTION: Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection. {ECO:0000269|PubMed:10605003, ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645, ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:9056417}.Q9Y426CU025C2 domain-containing protein 2Mcytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]Q9NZD8SPG21 Maspardin=SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11113139}. Membrane {ECO:0000269|PubMed:11113139}; Peripheral membrane protein {ECO:0000269|PubMed:11113139}. Endosome membrane {ECO:0000269|PubMed:11113139}; Peripheral membrane protein {ECO:0000269|PubMed:11113139}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11113139}; Peripheral membrane protein {ECO:0000269|PubMed:11113139}. Note=Partially localized in the cytosol but also accumulated on an intracellular vesicular compartment. Colocalizes with CD4 on endosomal/trans-Golgi network.8antigen receptor-mediated signaling pathway [GO:0050851]!CD4 receptor binding [GO:0042609]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; trans-Golgi network transport vesicle [GO:0030140]|FUNCTION: May play a role as a negative regulatory factor in CD4-dependent T-cell activation. {ECO:0000269|PubMed:11113139}.P30559OXYROxytocin receptorcell surface receptor signaling pathway [GO:0007166]; cellular response to hormone stimulus [GO:0032870]; digestive tract development [GO:0048565]; eating behavior [GO:0042755]; ERK1 and ERK2 cascade [GO:0070371]; estrous cycle [GO:0044849]; female pregnancy [GO:0007565]; G-protein coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; lactation [GO:0007595]; maternal behavior [GO:0042711]; maternal process involved in parturition [GO:0060137]; memory [GO:0007613]; muscle contraction [GO:0006936]; negative regulation of gastric acid secretion [GO:0060455]; positive regulation of blood pressure [GO:0045777]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of norepinephrine secretion [GO:0010701]; positive regulation of penile erection [GO:0060406]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of uterine smooth muscle contraction [GO:0070474]; positive regulation of vasoconstriction [GO:0045907]; regulation of systemic arterial blood pressure by vasopressin [GO:0001992]; response to amphetamine [GO:0001975]; response to anoxia [GO:0034059]; response to cocaine [GO:0042220]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to estradiol [GO:0032355]; response to peptide [< GO:1901652]; response to peptide hormone [GO:0043434]; response to progesterone [GO:0032570]; sleep [GO:0030431]; social behavior [GO:0035176]; sperm ejaculation [GO:0042713]; suckling behavior [GO:0001967]; telencephalon development [GO:0021537]oxytocin receptor activity [GO:0004990]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]; vasopressin receptor activity [GO:0005000]apical plasma membrane [GO:0016324]; cell-cell adherens junction [GO:0005913]; cytosol [GO:0005829]; integral component of plasma membrane [GO:0005887]; microvillus [GO:0005902]; plasma membrane [GO:0005886]FUNCTION: Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.Q9BQ67GRWD1-Glutamate-rich WD repeat-containing protein 1Q9Y546LRC42)Leucine-rich repeat-containing protein 42P54920SNAA$Alpha-soluble NSF attachment proteinapical protein localization [GO:0045176]; brain development [GO:0007420]; intracellular protein transport [GO:0006886]; intra-Golgi vesicle-mediated transport [GO:0006891]; membrane fusion [GO:0061025]; membrane organization [GO:0061024]; neuron differentiation [GO:0030182]; post-Golgi vesicle-mediated transport [GO:0006892]; regulation of synaptic vesicle priming [GO:0010807]; SNARE complex disassembly [GO:0035494]; synaptic transmission, glutamatergic [GO:0035249]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; myelin sheath [GO:0043209]; SNARE complex [GO:0031201]; synaptobrevin 2-SNAP-25-syntaxin-1a complex [GO:0070044]; terminal bouton [GO:0043195]; vacuolar membrane [GO:0005774]O43157PLXB1 Plexin-B1axon guidance [GO:0007411]; cell migration [GO:0016477]; intracellular signal transduction [GO:0035556]; negative regulation of cell adhesion [GO:0007162]; negative regulation of osteoblast proliferation [GO:0033689]; neuron projection morphogenesis [GO:0048812]; ossification involved in bone maturation [GO:0043931]; positive regulation of axonogenesis [GO:0050772]; positive regulation of GTPase activity [GO:0043547]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; regulation of cell shape [GO:0008360]; regulation of cytoskeleton organization [GO:0051493]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis [GO:1900220]; signal transduction [GO:0007165]GTPase activating protein binding [GO:0032794]; receptor activity [GO:0004872]; semaphorin receptor activity [GO:0017154]; semaphorin receptor binding [GO:0030215]; transmembrane signaling receptor activity [GO:0004888]extracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]cFUNCTION: Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. {ECO:0000269|PubMed:12196628, ECO:0000269|PubMed:12198496, ECO:0000269|PubMed:15210733, ECO:0000269|PubMed:19843518, ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:21912513}.P51798CLCN7!H(+)/Cl(-) exchange transporter 7SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}.chloride transmembrane transport [GO:1902476]; ion transmembrane transport [GO:0034220]; response to pH [GO:0009268]; transmembrane transport [GO:0055085]; transport [GO:0006810]cytoplasmic vesicle [GO:0031410]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]FUNCTION: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen. {ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}.O00592PODXL PodocalyxinSUBCELLULAR LOCATION: Apical cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus {ECO:0000250}. Membrane raft {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells (By similarity). Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). {ECO:0000250}.cell adhesion [GO:0007155]; cell migration [GO:0016477]; epithelial tube formation [GO:0072175]; glomerular visceral epithelial cell development [GO:0072015]; leukocyte migration [GO:0050900]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell-cell adhesion [GO:0022408]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of cell migration [GO:0030335]; regulation of microvillus assembly [GO:0032534]apical plasma membrane [GO:0016324]; cell body [GO:0044297]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; integral component of plasma membrane [GO:0005887]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; slit diaphragm [GO:0036057]FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up inital epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells. {ECO:0000269|PubMed:17616675, ECO:0000269|PubMed:18456258}.Q8IYB1M21D2Protein MB21D2P42331RHG25 Rho GTPase-activating protein 25P28702RXRBRetinoic acid receptor RXR-beta}cardiac muscle cell proliferation [GO:0060038]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; maternal placenta development [GO:0001893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription initiation from RNA polymerase II promoter [GO:0006367]; ventricular cardiac muscle cell differentiation [GO:0055012]9-cis retinoic acid receptor activity [GO:0004886]; ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity < [GO:0004879]; RNA polymerase II distal enhancer sequence-specific DNA binding [GO:0000980]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001228]; sequence-specific DNA binding transcription factor activity [GO:0003700]; steroid hormone receptor activity [GO:0003707]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Specifically binds 9-cis retinoic acid (9C-RA). {ECO:0000250}.Q13112CAF1B%Chromatin assembly factor 1 subunit BSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9614144}. Cytoplasm {ECO:0000269|PubMed:9614144}. Note=DNA replication foci. Cytoplasmic in M phase.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; cell cycle [GO:0007049]; chromatin assembly [GO:0031497]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent nucleosome assembly [GO:0006335]; positive regulation of defense response to virus by host [GO:0002230]; protein complex assembly [GO:0006461]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]cchromatin binding [GO:0003682]; histone binding [GO:0042393]; unfolded protein binding [GO:0051082]CAF-1 complex [GO:0033186]; cytoplasm [GO:0005737]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein complex [GO:0043234]FUNCTION: Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. {ECO:0000269|PubMed:9813080}.Q96PE1GP124G-protein coupled receptor 124central nervous system development [GO:0007417]; endothelial cell migration [GO:0043542]; G-protein coupled receptor signaling pathway [GO:0007186]; negative regulation of vascular endothelial growth factor signaling pathway [GO:1900747]; positive regulation of endothelial cell migration [GO:0010595]; regulation of angiogenesis [GO:0045765]; regulation of chemotaxis [GO:0050920]; regulation of establishment of blood-brain barrier [GO:0090210]; sprouting angiogenesis [GO:0002040]dcell surface [GO:0009986]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Endothelial receptor that acts as an essential regulator of CNS angiogenesis. Required for normal endothelial cell sprouting and migration in the forebrain and neural tube (By similarity). {ECO:0000250}.Q8N3F8MILK1MICAL-like protein 1SUBCELLULAR LOCATION: Recycling endosome membrane; Peripheral membrane protein. Late endosome membrane. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6.cellular response to nerve growth factor stimulus [GO:1990090]; endocytosis [GO:0006897]; membrane tubulation [GO:0097320]; neuron projection development [GO:0031175]; protein localization to endosome [GO:0036010]; protein targeting to membrane [GO:0006612]; receptor-mediated endocytosis [GO:0006898]; retrograde transport, endosome to plasma membrane [GO:1990126]; slow endocytic recycling [GO:0032458]identical protein binding [GO:0042802]; phosphatidic acid binding [GO:0070300]; Rab GTPase binding [GO:0017137]; zinc ion binding [GO:0008270]extrinsic component of membrane [GO:0019898]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; recycling endosome membrane [GO:0055038]FUNCTION: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth. {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20801876, ECO:0000269|PubMed:21795389, ECO:0000269|PubMed:23596323}.Q9BXJ0C1QT56Complement C1q tumor necrosis factor-related protein 5@collagen trimer [GO:0005581]; extracellular exosome [GO:0070062]P0CG39POTEJ#POTE ankyrin domain family member JQ69YN2C19L1CWF19-like protein 1Q9UK45LSM7(U6 snRNA-associated Sm-like protein LSm7exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]U6 snRNA binding [GO:0017070]ocytosol [GO:0005829]; small nucleolar ribonucleoprotein complex [GO:0005732]; spliceosomal complex [GO:0005681]Q9Y530OARD1!O-acetyl-ADP-ribose deacetylase 10purine nucleoside metabolic process [GO:0042278]Ideacetylase activity [GO:0019213]; purine nucleoside binding [GO:0001883]IFUNCTION: Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.Q8WUQ7CATINCactinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829348}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with NFKBIL1 in the nucleus.`cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to tumor necrosis factor [GO:0071356]; innate immune response [GO:0045087]; mRNA splicing, via spliceosome [GO:0000398]; multicellular organismal development [GO:0007275]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of lipopolysaccharide-mediated signaling pathway [GO:0031665]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of toll-like receptor signaling pathway [GO:0034122]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type I interferon-mediated signaling pathway [GO:0060339]catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli. May play a role during early embryonic development. Probably involved in pre-mRNA splicing. {ECO:0000269|PubMed:20829348}.P12235ADT1ADP/ATP translocase 1adenine transport [GO:0015853]; apoptotic mitochondrial changes [GO:0008637]; energy reserve metabolic process [GO:0006112]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial genome maintenance [GO:0000002]; negative regulation of necroptotic process [GO:0060546]; regulation of insulin secretion [GO:0050796]; small molecule metabolic process [GO:0044281]; transport [GO:000< 6810]; viral process [GO:0016032]7adenine transmembrane transporter activity [GO:0015207]integral component of plasma membrane [GO:0005887]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]sFUNCTION: Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane.Q8TEW8PAR3L"Partitioning defective 3 homolog BSUBCELLULAR LOCATION: Endomembrane system. Cell junction. Cell junction, tight junction. Note=Partially localized along the cell-cell contact region. Colocalizes with TJP1 to epithelial tight junctions._bicellular tight junction [GO:0005923]; endomembrane system [GO:0012505]; membrane [GO:0016020]FUNCTION: Putative adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions.Q53GT1KLH22Kelch-like protein 22WSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23455478}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23455478}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23455478}. Note=Mainly. cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase.cell division [GO:0051301]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint [GO:0007094]; protein monoubiquitination [GO:0006513]centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; polar microtubule [GO:0005827]*FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. {ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:23455478}.P51688SPHM#N-sulphoglucosamine sulphohydrolasecarbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; proteoglycan metabolic process [GO:0006029]; small molecule metabolic process [GO:0044281]catalytic activity [GO:0003824]; metal ion binding [GO:0046872]; N-sulfoglucosamine sulfohydrolase activity [GO:0016250]; sulfuric ester hydrolase activity [GO:0008484]Q4KWH8PLCH1?1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1fSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15702972}. Membrane {ECO:0000269|PubMed:15702972}.inositol phosphate metabolic process [GO:0043647]; lipid catabolic process [GO:0016042]; phosphatidylinositol-mediated signaling [GO:0048015]; small molecule metabolic process [GO:0044281]calcium-dependent phospholipase C activity [GO:0050429]; calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]; signal transducer activity [GO:0004871]cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by calcium-activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000269|PubMed:15702972}.Q9Y6B7AP4B1AP-4 complex subunit beta-1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:22472443}. Membrane, coated pit {ECO:0000250}. Note=Associated with the trans-Golgi network. Found in soma and dendritic shafts of neuronal cells.clathrin adaptor complex [GO:0030131]; coated pit [GO:0005905]; endosome lumen [GO:0031904]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]Q9NPI1BRD7 Bromodomain-containing protein 7)SUBCELLULAR LOCATION: Isoform 2: Nucleus.cell cycle [GO:0007049]; negative regulation of cell proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of histone acetylation [GO:0035066]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]; Wnt signaling pathway [GO:0016055]-histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]KBAF-type complex [GO:0090544]; cytoplasm [GO:0005737]; nucleus [GO:0005634]UFUNCTION: Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. {ECO:0000250, ECO:0000269|PubMed:16265664, ECO:0000269|PubMed:16475162, ECO:0000269|PubMed:20215511, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:20660729}.Q9BRJ7SDOSProtein syndesmos^hydrolase activity [GO:0016787]; poly(A) RNA binding [GO:0044822]; snoRNA binding [GO:0030515]FUNCTION: Probable adapter protein, which may link syndecan-4 (SDC4) and paxilin (TGFB1I1 and PXN) receptors (By similarity). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. {ECO:0000250}.Q8IYB3SRRM1+Serine/arginine repetitive matrix protein 16SUBCELLULAR LOCATION: Nucleus matrix. Nucleus speckle.ggene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]LFUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates. {ECO:0000269|PubMed:10339552, ECO:0000269|PubMed:10668804, ECO:0000269|PubMed:11739730, ECO:0000269|PubMed:12600940, ECO:0000269|PubMed:12944400, ECO:0000269|PubMed< :9531537}.Q5BJF2TMM97Transmembrane protein 97tSUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:19583955}. Rough endoplasmic reticulum {ECO:0000269|PubMed:19583955}. Cell membrane {ECO:0000269|PubMed:19583955}. Lysosome {ECO:0000269|PubMed:19583955}. Membrane; Multi-pass membrane protein {ECO:0000305}. Note=Localized in sterol-depleted cells at cell membrane and in lysosomes. {ECO:0000269|PubMed:19583955}.Lcholesterol homeostasis [GO:0042632]; regulation of cell growth [GO:0001558]integral component of membrane [GO:0016021]; lysosome [GO:0005764]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Plays a role as a regulator of cellular cholesterol homeostasis (PubMed:19583955). May function as sterol isomerase (PubMed:25566323). {ECO:0000269|PubMed:19583955, ECO:0000303|PubMed:25566323}.Q6NUK4REEP3'Receptor expression-enhancing protein 3rendoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; microtubule [GO:0005874]P29558RBMS18RNA-binding motif, single-stranded-interacting protein 19DNA replication [GO:0006260]; RNA processing [GO:0006396]double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]FUNCTION: Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.P02461CO3A1Collagen alpha-1(III) chainaging [GO:0007568]; aorta smooth muscle tissue morphogenesis [GO:0060414]; axon guidance [GO:0007411]; cell-matrix adhesion [GO:0007160]; cellular response to amino acid stimulus [GO:0071230]; cerebral cortex development [GO:0021987]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; digestive tract development [GO:0048565]; extracellular fibril organization [GO:0043206]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; heart development [GO:0007507]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of immune response [GO:0050777]; negative regulation of neuron migration [GO:2001223]; peptide cross-linking [GO:0018149]; platelet activation [GO:0030168]; positive regulation of Rho protein signal transduction [GO:0035025]; receptor-mediated endocytosis [GO:0006898]; response to cytokine [GO:0034097]; response to mechanical stimulus [GO:0009612]; response to radiation [GO:0009314]; skeletal system development [GO:0001501]; skin development [GO:0043588]; transforming growth factor beta receptor signaling pathway [GO:0007179]; wound healing [GO:0042060]extracellular matrix structural constituent [GO:0005201]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]collagen type III trimer [GO:0005586]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]BFUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12.P15848ARSBArylsulfatase BLSUBCELLULAR LOCATION: Lysosome. Cell surface {ECO:0000250|UniProtKB:P50429}.{autophagy [GO:0006914]; carbohydrate metabolic process [GO:0005975]; cellular protein metabolic process [GO:0044267]; central nervous system development [GO:0007417]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; colon epithelial cell migration [GO:0061580]; glycosaminoglycan metabolic process [GO:0030203]; glycosphingolipid metabolic process [GO:0006687]; lysosomal transport [GO:0007041]; lysosome organization [GO:0007040]; positive regulation of neuron projection development [GO:0010976]; post-translational protein modification [GO:0043687]; regulation of epithelial cell migration [GO:0010632]; response to estrogen [GO:0043627]; response to methylmercury [GO:0051597]; response to nutrient [GO:0007584]; response to pH [GO:0009268]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]|arylsulfatase activity [GO:0004065]; metal ion binding [GO:0046872]; N-acetylgalactosamine-4-sulfatase activity [GO:0003943]cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; rough endoplasmic reticulum [GO:0005791]FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity). {ECO:0000250|UniProtKB:P50430, ECO:0000269|PubMed:19306108}.P35244RFA3$Replication protein A 14 kDa subunitbase-excision repair [GO:0006284]; cellular response to heat [GO:0034605]; DNA damage response, detection of DNA damage [GO:0042769]; DNA recombinase assembly [GO:0000730]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; G1/S transition of mitotic cell cycle [GO:0000082]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; nucleotide-excision repair, DNA gap filling [GO:0006297]; regulation of cell proliferation [GO:0042127]; regulation of cellular response to heat [GO:1900034]; regulation of mitotic cell cycle [GO:0007346]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription-coupled nucleotide-excision repair [GO:0006283]; translesion synthesis [GO:0019985]Jdamaged DNA binding [GO:0003684]; single-stranded DNA binding [GO:0003697]GDNA replication factor A complex [GO:0005662]; nucleoplasm [GO:0005654]FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Plays also a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279). Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). As pa< rt of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). {ECO:0000269|PubMed:19010961, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279, ECO:0000303|PubMed:24332808}.P24386RAE14Rab proteins geranylgeranyltransferase component A 1FSUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7957092}.blood vessel development [GO:0001568]; protein geranylgeranylation [GO:0018344]; protein targeting to membrane [GO:0006612]; response to stimulus [GO:0050896]; visual perception [GO:0007601]|GTPase activator activity [GO:0005096]; Rab geranylgeranyltransferase activity [GO:0004663]; Rab GTPase binding [GO:0017137]Pcytosol [GO:0005829]; Rab-protein geranylgeranyltransferase complex [GO:0005968]FUNCTION: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation. {ECO:0000269|PubMed:18532927, ECO:0000269|PubMed:7957092}.Q9NQS3PVRL3Nectin-3SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}.adherens junction organization [GO:0034332]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell recognition [GO:0008037]; fertilization [GO:0009566]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; lens morphogenesis in camera-type eye [GO:0002089]; retina morphogenesis in camera-type eye [GO:0060042]; single organismal cell-cell adhesion [GO:0016337]apical junction complex [GO:0043296]; cell-cell adherens junction [GO:0005913]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]FUNCTION: Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body. {ECO:0000269|PubMed:16216929}.Q9BQ52RNZ2%Zinc phosphodiesterase ELAC protein 2SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21593607}. Nucleus {ECO:0000269|PubMed:21593607}. Note=Mainly mitochondrial.Dmitochondrial tRNA 3'-trailer cleavage, endonucleolytic [GO:0072684]{3'-tRNA processing endoribonuclease activity [GO:0042781]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. {ECO:0000269|PubMed:21593607}.Q8N584TT39C$Tetratricopeptide repeat protein 39CP04920B3A2Anion exchange protein 2anion transport [GO:0006820]; bicarbonate transport [GO:0015701]; chloride transmembrane transport [GO:1902476]; ion transport [GO:0006811]; regulation of intracellular pH [GO:0051453]; transmembrane transport [GO:0055085]fanion transmembrane transporter activity [GO:0008509]; inorganic anion exchanger activity [GO:0005452]basolateral plasma membrane [GO:0016323]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FFUNCTION: Plasma membrane anion exchange protein of wide distribution.Q49A26GLYR1Putative oxidoreductase GLYR1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16352664}.DNA binding [GO:0003677]; methylated histone binding [GO:0035064]; NAD binding [GO:0051287]; phosphogluconate dehydrogenase (decarboxylating) activity [GO:0004616]FUNCTION: May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). {ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:20850016}.Q09328MGT5AGAlpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase Acellular protein metabolic process [GO:0044267]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279][alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity [GO:0030144] FUNCTION: Catalyzes the addition of N-acetylglucosamine in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.Q9H900ZWILCProtein zwilch homologXSUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20462495}.cell division [GO:0051301]; mitotic cell cycle [GO:0000278]; mitotic cell cycle checkpoint [GO:0007093]; mitotic nuclear division [GO:0007067]; small GTPase mediated signal transduction [GO:0007264]wcondensed chromosome kinetochore [GO:0000777]; cytosol [GO:0005829]; kinetochore [GO:0000776]; RZZ complex [GO:1990423]xFUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:15824131). {ECO:0000269|PubMed:15824131}.Q9NTN3S35D19UDP-glucuronic acid/UDP-N-acetylgalactosamine transporteranion transmembrane transport [GO:0098656]; carbohydrate transport [GO:0008643]; cellular glucuronidation [GO:0052695]; chondroitin sulfate biosynthetic process [GO:0030206]; embryonic skeletal system development [GO:0048706]; pyrimidine nucleotide-sugar transmembrane transport [GO:0090481]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]; UDP-glucuronate biosynthetic process [GO:0006065]; UDP-glucuronic acid transport [GO:0015787]; xenobiotic metabolic process [GO:0006805]antiporter activity [GO:0015297]; pyrimidine nucleotide-sugar transmembrane transporter activity [GO:0015165]; UDP-glucuronic acid transmembrane transporter activity [GO:0005461]FUNCTION: Transports both UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylgalactosamine (UDP-GalNAc) from the cytoplasm to into the endoplasmic reticulum lumen. May participate in glucuronidation and/or chondroitin sulfate biosynthesis.Q15014MO4L2!Mortality factor 4-like protein 2chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; chromatin silencing [GO:0006< 342]; DNA repair [GO:0006281]; histone deacetylation [GO:0016575]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; positive regulation of striated muscle cell differentiation [GO:0051155]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of growth [GO:0040008]; transcription, DNA-templated [GO:0006351]eNuA4 histone acetyltransferase complex [GO:0035267]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones.P04062GLCMGlucosylceramidaseSUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Peripheral membrane protein {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Lumenal side {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C promotes membrane association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. carbohydrate metabolic process [GO:0005975]; cellular response to tumor necrosis factor [GO:0071356]; ceramide biosynthetic process [GO:0046513]; glucosylceramide catabolic process [GO:0006680]; glycosphingolipid metabolic process [GO:0006687]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of MAP kinase activity [GO:0043407]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of proteolysis involved in cellular protein catabolic process [GO:1903052]; regulation of water loss via skin [GO:0033561]; response to estrogen [GO:0043627]; response to glucocorticoid [GO:0051384]; response to pH [GO:0009268]; response to testosterone [GO:0033574]; response to thyroid hormone [GO:0097066]; skin morphogenesis [GO:0043589]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]; sphingosine biosynthetic process [GO:0046512]; termination of signal transduction [GO:0023021]Gglucosylceramidase activity [GO:0004348]; receptor binding [GO:0005102]aextracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]P13591NCAM1Neural cell adhesion molecule 1SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 5: Secreted.; SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}.axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cytokine-mediated signaling pathway [GO:0019221]; extracellular matrix organization [GO:0030198]; interferon-gamma-mediated signaling pathway [GO:0060333]anchored component of membrane [GO:0031225]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.Q9Y619ORNT1%Mitochondrial ornithine transporter 1cellular amino acid metabolic process [GO:0006520]; cellular nitrogen compound metabolic process [GO:0034641]; L-ornithine transmembrane transport [GO:1903352]; mitochondrial ornithine transport [GO:0000066]; small molecule metabolic process [GO:0044281]; urea cycle [GO:0000050];L-ornithine transmembrane transporter activity [GO:0000064]dFUNCTION: Ornithine transport across inner mitochondrial membrane, from the cytoplasm to the matrix.Q9GZU1MCLN1 Mucolipin-1SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.-calcium ion transmembrane transport [GO:0070588]; cation transport [GO:0006812]; cellular iron ion homeostasis [GO:0006879]; ion transmembrane transport [GO:0034220]; release of sequestered calcium ion into cytosol [GO:0051209]; transferrin transport [GO:0033572]; transmembrane transport [GO:0055085]ccation channel activity [GO:0005261]; NAADP-sensitive calcium-release channel activity [GO:0072345]cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; integral component of membrane [GO:0016021]; integral component of plasma membrane [GO:0005887]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]FUNCTION: Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca(2+) transport regulating lysosomal exocytosis. {ECO:0000269|PubMed:12459486, ECO:0000269|PubMed:14749347}.Q15831STK11%Serine/threonine-protein kinase STK11SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane {ECO:0000250}. Mitochondrion. Note=A small fraction localizes at membranes (By similarity). Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). Translocates to the mitochondrion during apoptosis. Translocates to the cytoplasm in response to metformin or peroxynitrite treatment. PTEN promotes cytoplasmic localization. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000269|PubMed:23612973}. Cytoplasm {ECO:0000269|PubMed:23612973}. Note=Predominantly nuclear, but translocates to the cytoplasm in response to metformin or peroxynitrite treatment.activation of protein kinase activity [GO:0032147]; anoikis [GO:0043276]; autophagy [GO:0006914]; axonogenesis [GO:0007409]; canonical Wnt signaling pathway [GO:0060070]; cell cycle arrest [GO:0007050]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to UV-B [GO:0071493]; dendrite extension [GO:0097484]; energy reserve metabolic process [GO:0006112]; establishment of cell polarity [GO:0030010]; glucose homeostasis [GO:0042593]; Golgi localization [GO:0051645]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of epithelial cell proliferation involved in prostate gland development [GO:0060770]; positive regulation of axonogenesis [GO:0050772]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive thymic T cell selection [GO:0045059]; protein autophosphorylation [GO:0046777]; protein heterooligomerization [GO:0051291]; protein phosphorylation [GO:0006468]; regulation of cell growth [GO:0001558]; regulation of dendrite morphogenesis [GO:0048814]; regulation of fatty acid biosynthetic process [< GO:0042304]; regulation of protein kinase B signaling [GO:0051896]; regulation of Wnt signaling pathway [GO:0030111]; response to glucagon [GO:0033762]; response to ionizing radiation [GO:0010212]; response to lipid [GO:0033993]; small molecule metabolic process [GO:0044281]; spermatid development [GO:0007286]; T cell receptor signaling pathway [GO:0050852]; TCR signalosome assembly [GO:0036399]; tissue homeostasis [GO:0001894]; vasculature development [GO:0001944]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; p53 binding [GO:0002039]; protein kinase activator activity [GO:0030295]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; TCR signalosome [GO:0036398] FUNCTION: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316). {ECO:0000269|PubMed:11430832, ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15016379, ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:15987703, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:18321849, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.; FUNCTION: Isoform 2: Has a role in spermiogenesis. {ECO:0000250}.Q13884SNTB1Beta-1-syntrophincytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystrophin-associated glycoprotein complex [GO:0016010]; focal adhesion [GO:0005925]; protein complex [GO:0043234]; sarcolemma [GO:0042383]; synapse [GO:0045202]FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex.Q5JYT7K1755 Uncharacterized protein KIAA1755Q9H6F5CCD86(Coiled-coil domain-containing protein 86Q9NS00C1GLTAGlycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1%angiogenesis [GO:0001525]; cellular protein metabolic process [GO:0044267]; intestinal epithelial cell development [GO:0060576]; kidney development [GO:0001822]; O-glycan processing [GO:0016266]; post-translational protein modification [GO:0043687]; protein O-linked glycosylation [GO:0006493]uglycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity [GO:0016263]; metal ion binding [GO:0046872]"FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.P42785PCP Lysosomal Pro-X carboxypeptidaseangiogenesis involved in wound healing [GO:0060055]; blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; energy homeostasis [GO:0097009]; glucose homeostasis [GO:0042593]; negative regulation of systemic arterial blood pressure [GO:0003085]; plasma kallikrein-kinin cascade [GO:0002353]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of thyroid hormone mediated signaling pathway [GO:0002155]2serine-type carboxypeptidase activity [GO:0004185]xbasal part of cell [GO:0045178]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; plasma membrane [GO:0005886]FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.P10253LYAGLysosomal alpha-glucosidasenSUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:17897319}. Lysosome membrane {ECO:0000269|PubMed:17897319}.carbohydrate metabolic process [GO:0005975]; cardiac muscle contraction [GO:0060048]; diaphragm contraction [GO:0002086]; glucose metabolic process [GO:0006006]; glycogen catabolic process [GO:0005980]; heart morphogenesis [GO:0003007]; locomotory behavior [GO:0007626]; lysosome organization [GO:0007040]; maltose metabolic process [GO:0000023]; muscle cell cellular homeostasis [GO:0046716]; neuromuscular process controlling balance [GO:0050885]; neuromuscular process controlling posture [GO:0050884]; regulation of the force of heart contraction [GO:0002026]; small molecule metabolic process [GO:0044281]; sucrose metabolic process [GO:0005985]; tissue development [GO:0009888]; vacuolar sequestering [GO:0043181]alpha-1,4-glucosidase activity [GO:0004558]; carbohydrate binding [GO:0030246]; maltose alpha-glucosidase activity [GO:0032450]extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]LFUNCTION: Essential for the degradation of glygogen to glucose in lysosomes.Q9NVQ4FAIM1#Fas apoptotic inhibitory molecule 1apoptotic process [GO:0006915]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]FUNCTION: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. {ECO:0000250}.Q96EA4SPDLYProtein SpindlySUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes to the mitotic spindle pole before metaphase and is subsequently lost from the spindle poles after chromosome congression is completed. Removal of this protein from the kinetochore requires the dynein/dynactin complex.3cell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; mitotic cell cycle [GO:0000278]; mitotic metaphase plate congression [GO:0007080]; protein localization to kinetochore [GO:0034501]; small GTPase mediated signal transduction [GO:0007264]; spindle checkpoint [GO:0031577]=enzyme binding [GO:0019899]; kinetochore binding [GO:0043515]condensed chromosome outer kinetochore [GO:0000940]< ; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle pole [GO:0000922]_FUNCTION: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041, ECO:0000269|PubMed:17576797, ECO:0000269|PubMed:19468067}.Q6PCB7S27A1)Long-chain fatty acid transport protein 1SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12235169}; Single-pass membrane protein {ECO:0000269|PubMed:12235169}. Endomembrane system {ECO:0000269|PubMed:12235169}; Single-pass membrane protein {ECO:0000269|PubMed:12235169}. Cytoplasm {ECO:0000250}. Note=Plasma membrane and intracellular membranes, at least in adipocytes. Predominantly cytoplasmic in myocytes (By similarity). {ECO:0000250}.adiponectin-activated signaling pathway [GO:0033211]; cardiolipin biosynthetic process [GO:0032049]; cellular lipid metabolic process [GO:0044255]; long-chain fatty acid transport [GO:0015909]; medium-chain fatty acid transport [GO:0001579]; negative regulation of phospholipid biosynthetic process [GO:0071072]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylglycerol biosynthetic process [GO:0006655]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylserine biosynthetic process [GO:0006659]; positive regulation of heat generation [GO:0031652]; positive regulation of protein serine/threonine kinase activity [GO:0071902]; response to cold [GO:0009409]; response to insulin [GO:0032868]; small molecule metabolic process [GO:0044281]; transmembrane transport [GO:0055085]caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]WFUNCTION: Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids (By similarity). {ECO:0000250}.P61962DCAF7"DDB1- and CUL4-associated factor 7SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Overexpression of DIAHP1 or active RHOA causes translocation from the nucleus to cytoplasm.Vmulticellular organismal development [GO:0007275]; protein ubiquitination [GO:0016567]Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]+FUNCTION: Involved in craniofacial development. Acts upstream of the EDN1 pathway and is required for formation of the upper jaw equivalent, the palatoquadrate. The activity required for EDN1 pathway function differs between the first and second arches (By similarity). Associates with DIAPH1 and controls GLI1 transcriptional activity. Could be involved in normal and disease skin development. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250, ECO:0000269|PubMed:16887337, ECO:0000269|PubMed:16949367}.P58215LOXL3Lysyl oxidase homolog 3SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000269|PubMed:17018530}. Secreted, extracellular space {ECO:0000269|PubMed:17018530}.sepithelial to mesenchymal transition [GO:0001837]; negative regulation of transcription, DNA-templated [GO:0045892]ycopper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720]; scavenger receptor activity [GO:0005044]cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] FUNCTION: Both isoforms function as amine oxidases toward elastin and different types of collagens. Isoform 1 shows the highest activity toward collagen type VIII, while Isoform 2 presents the highest activity toward collagen type IV. {ECO:0000269|PubMed:17018530}.Q9UPN4CP131Centrosomal protein of 131 kDa|SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=Colocalized with pericentriolar material protein PCM1 at centriolar satellites. During spermiogenesis, becomes enriched with nephrocystin NPHP1 at the transition zone, a structure at the base of the ciliary axoneme important for regulating traffic into the ciliary compartment. Traffics towards and away from the centrosome/basal body and the transition zone of the ciliary axoneme in a microtubule-dependent manner. Localized at the Golgi-derived acrosome and the centrosome-containing head-tail coupling apparatus (HTCA) (By similarity). Ubiquitinated form is sequestred and colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites in proliferating cells. Colocalized with the pericentriolar material protein PCM1 at centrosome. Traffics towards and away from centriolar satellites and centrosome in a microtubule- and dynein-dependent manner in interphase cells. Displaced from centriolar satellites but still remained associated with centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAPK signaling. {ECO:0000250}.cell differentiation [GO:0030154]; G2/M transition of mitotic cell cycle [GO:0000086]; intraciliary transport involved in cilium morphogenesis [GO:0035735]; mitotic cell cycle [GO:0000278]; multicellular organismal development [GO:0007275]; organelle organization [GO:0006996]; positive regulation of cell proliferation [GO:0008284]; positive regulation of intracellular protein transport [GO:0090316]; regulation of centrosome duplication [GO:0010824]; spermatogenesis [GO:0007283]Tprotein complex binding [GO:0032403]; protein homodimerization activity [GO:0042803]acrosomal vesicle [GO:0001669]; centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cilium [GO:0005929]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of centriolar satellites contributing to build a complex and dynamic network required to regulate cilia/flagellum formation. In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation. In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner. Acts also as a negative regulator of BBSome ciliary trafficking. Plays a role in sperm flagellar formation; may be involved< in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail. Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability and centriole duplication in non-ciliogenic cells. {ECO:0000269|PubMed:17954613, ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:24185901, ECO:0000269|PubMed:24550735}.Q86YV9HPS6#Hermansky-Pudlak syndrome 6 proteinVSUBCELLULAR LOCATION: Microsome membrane. Cytoplasm, cytosol. Early endosome membrane.blood coagulation [GO:0007596]; melanocyte differentiation [GO:0030318]; organelle organization [GO:0006996]; protein localization to membrane [GO:0072657]KGTP-dependent protein binding [GO:0030742]; Rab GTPase binding [GO:0017137]|BLOC-2 complex [GO:0031084]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]FUNCTION: May regulate the synthesis and function of lysosomes and of highly specialized organelles, such as melanosomes and platelet dense granules. {ECO:0000269|PubMed:17041891}.P07686HEXB Beta-hexosaminidase subunit betaastrocyte cell migration [GO:0043615]; carbohydrate metabolic process [GO:0005975]; cellular calcium ion homeostasis [GO:0006874]; cellular protein metabolic process [GO:0044267]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; ganglioside catabolic process [GO:0006689]; glycosaminoglycan metabolic process [GO:0030203]; glycosphingolipid metabolic process [GO:0006687]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; lipid storage [GO:0019915]; locomotory behavior [GO:0007626]; lysosome organization [GO:0007040]; male courtship behavior [GO:0008049]; myelination [GO:0042552]; neuromuscular process controlling balance [GO:0050885]; oligosaccharide catabolic process [GO:0009313]; oogenesis [GO:0048477]; penetration of zona pellucida [GO:0007341]; phospholipid biosynthetic process [GO:0008654]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]beta-N-acetylhexosaminidase activity [GO:0004563]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]wacrosomal vesicle [GO:0001669]; extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]FUNCTION: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.Q5VT52RPRD2:Regulation of nuclear pre-mRNA domain-containing protein 2Q9NRR8C42S1CDC42 small effector protein 1SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Lipid-anchor. Note=Recruited to the activated TCR prior actin polymerization.negative regulation of GTPase activity [GO:0034260]; phagocytosis [GO:0006909]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165]QGTPase inhibitor activity [GO:0005095]; structural molecule activity [GO:0005198]Ocytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]FUNCTION: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly. Alters CDC42-induced cell shape changes. In activated T-cells, may play a role in CDC42-mediated F-actin accumulation at the immunological synapse. May play a role in early contractile events in phagocytosis in macrophages. {ECO:0000269|PubMed:10816584, ECO:0000269|PubMed:15840583, ECO:0000269|PubMed:17045588}.Q14145KEAP1#Kelch-like ECH-associated protein 1VSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between cytoplasm and nucleus.balkanesulfonate metabolic process [GO:0019694]; cellular response to interleukin-4 [GO:0071353]; cellular response to organic cyclic compound [GO:0071407]; cytoplasmic sequestering of transcription factor [GO:0042994]; flavonoid metabolic process [GO:0009812]; in utero embryonic development [GO:0001701]; malate metabolic process [GO:0006108]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; proteasomal ubiquitin-independent protein catabolic process [GO:0010499]; protein oligomerization [GO:0051259]; protein ubiquitination [GO:0016567]; regulation of epidermal cell differentiation [GO:0045604]; release of cytochrome c from mitochondria [GO:0001836]; response to immobilization stress [GO:0035902]; response to metal ion [GO:0010038]; response to thyroid hormone [GO:0097066]; selenium compound metabolic process [GO:0001887]; transcription, DNA-templated [GO:0006351]]actin filament [GO:0005884]; cell-cell adherens junction [GO:0005913]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]mFUNCTION: Acts as a substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1 and targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. Retains NFE2L2/NRF2 and may also retain BPTF in the cytosol. Targets PGAM5 for ubiquitination and degradation by the proteasome. {ECO:0000269|PubMed:14585973, ECO:0000269|PubMed:15379550, ECO:0000269|PubMed:15572695, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:17046835}.Q9BRX5PSF3)DNA replication complex GINS protein PSF3DNA replication [GO:0006260]FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA. {ECO:0000269|PubMed:17417653}.O15347HMGB3High mobility group protein B3_SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000250}.Nchromatin remodeling [GO:0006338]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; multicellular organismal development [GO:0007275]; negative regulation of B cell differentiation [GO:0045578]; negative regulation of myeloid cell differentiation [GO:0045638]; regulation of transcription, DNA-templated [GO:0006355]chromatin binding [GO:0003682]; DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; poly(A) RNA binding [GO:0044822]-chromosome [GO:0005694]; nucleus [GO:0005634]bFUNCTION: Binds preferentially single-stranded DNA and unwinds double-stranded DNA. {ECO:0000250}.O43681ASNA ATPase ASNA1KSUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus, nucleolus.cellular protein metabolic process [GO:0044267]; endoplasmic reticulum unfolded protein response [GO:0030968]; inorganic anion transport [GO:0015698]; IRE1-mediated unfolded protein response [GO:0036498]; protein insertion into ER membrane [GO:0045048]; transport [GO:0006810]arsenite transmembrane transporter activity [GO:0015105]; ATPase activity [GO:0016887]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; transporter activity [GO:0005215]cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) pro< teins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). May be involved in insulin signaling. {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:18477612}.Q8TDN4CABL1 CDK5 and ABL1 enzyme substrate 1ESUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Located in the cell body and proximal region of the developing axonal shaft of immature neurons. Located in axonal growth cone, but not in the distal part of the axon shaft or in dendritic growth cone of mature neurons (By similarity). {ECO:0000250}.zblood coagulation [GO:0007596]; cell cycle [GO:0007049]; cell division [GO:0051301]; regulation of cell cycle [GO:0051726]FUNCTION: Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity). {ECO:0000250}.Q8NEY8PPHLN Periphilin-1&SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12853457, ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:26022416}. Cytoplasm {ECO:0000269|PubMed:12853457}. Chromosome {ECO:0000269|PubMed:26022416}. Note=In undifferentiated keratinocytes expressed in speckle-type nuclear granules and at the nuclear membrane, but in the differentiated keratinocytes colocalized with periplakin at the cell periphery and at cell-cell junctions (PubMed:12853457). Localizes to chromatin (PubMed:26022416). {ECO:0000269|PubMed:12853457, ECO:0000269|PubMed:26022416}.keratinization [GO:0031424]cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]$FUNCTION: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin (PubMed:26022416). Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex (PubMed:15474462, PubMed:17963697). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (Probable). {ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:26022416, ECO:0000305|PubMed:12853457}.Q9BUP3HTAI2Oxidoreductase HTATIP2nSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15282309}. Nucleus envelope {ECO:0000269|PubMed:15282309}.?angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; negative regulation of apoptotic process [GO:0043066]; nuclear import [GO:0051170]; regulation of angiogenesis [GO:0045765]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; viral process [GO:0016032]Uoxidoreductase activity [GO:0016491]; transcription coactivator activity [GO:0003713]bcytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]FUNCTION: Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic as well as antiangiogenic properties. Isoform 2 has an antiapoptotic effect. {ECO:0000269|PubMed:10611237, ECO:0000269|PubMed:11313954, ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:9174052}.Q9UIF9BAZ2A5Bromodomain adjacent to zinc finger domain protein 2ASUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus. {ECO:0000250}.Gchromatin remodeling [GO:0006338]; chromatin silencing at rDNA [GO:0000183]; DNA methylation [GO:0006306]; gene expression [GO:0010467]; heterochromatin assembly involved in chromatin silencing [GO:0070869]; histone deacetylation [GO:0016575]; histone H3-K9 methylation [GO:0051567]; histone H4 deacetylation [GO:0070933]; histone H4-K20 methylation [GO:0034770]; negative regulation of gene expression, epigenetic [GO:0045814]; regulation of gene expression, epigenetic [GO:0040029]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; ligand-dependent nuclear receptor binding [GO:0016922]; lysine-acetylated histone binding [GO:0070577]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]cchromatin silencing complex [GO:0005677]; nucleolus [GO:0005730]; rDNA heterochromatin [GO:0033553]`FUNCTION: Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity). {ECO:0000250}.Q5TZA2CROCC RootletinySUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:14654843}. Note=In ciliated cells, associated with ciliary rootlets. In non-ciliated cells, localized between, around and at the proximal ends of the centrioles. Dissociates from the centrioles at the onset of mitosis and reassociates with them at anaphase.cell cycle [GO:0007049]; cell projection organization [GO:0030030]; centriole-centriole cohesion [GO:0010457]; centrosome organization [GO:0051297]; ciliary basal body organization [GO:0032053]; epithelial structure maintenance [GO:0010669]; establishment of organelle localization [GO:0051656]; photoreceptor cell maintenance [GO:0045494]; protein localization [GO:0008104]; protein localization to organelle [GO:0033365]Gkinesin binding [GO:0019894]; structural molecule activity [GO:0005198]actin cytoskeleton [GO:0015629]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary rootlet [GO:0035253]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; photoreceptor inner segment [GO:0001917]; plasma membrane [GO:0005886]QFUNCTION: Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus. Contributes to centrosome cohesion before mitosis. {ECO:0000250|UniProtKB:Q8CJ40, ECO:0000269|PubMed:16203858}.Q9H981ARP8Actin-related protein 8SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163988}. Chromosome {ECO:0000269|PubMed:18163988}. Note=Specifical< ly localizes to mitotic chromosomes.cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; mitotic nuclear division [GO:0007067]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]0Ino80 complex [GO:0031011]; nucleus [GO:0005634]/FUNCTION: Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize.; FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA reoplication and probably DNA repair. Required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex.Q9HAS3S28A3!Solute carrier family 28 member 3SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Multi-pass membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane; Multi-pass membrane protein.spyrimidine nucleoside transport [GO:0015864]; retina homeostasis [GO:0001895]; transmembrane transport [GO:0055085]nucleoside binding [GO:0001882]; purine-specific nucleoside:sodium symporter activity [GO:0015390]; pyrimidine- and adenine-specific:sodium symporter activity [GO:0015389]}endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]FUNCTION: Sodium-dependent, pyrimidine- and purine-selective. Involved in the homeostasis of endogenous nucleosides. Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine). Employs a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine. {ECO:0000269|PubMed:11032837, ECO:0000269|PubMed:16446384, ECO:0000269|PubMed:17140564}.O95425SVIL SupervillinFSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, invadopodium. Cell projection, podosome. Midbody {ECO:0000250|UniProtKB:O46385}. Cleavage furrow {ECO:0000250|UniProtKB:O46385}. Note=Tightly associated with both actin filaments and plasma membranes.cytoskeleton organization [GO:0007010]; positive regulation of cytokinesis [GO:0032467]; skeletal muscle tissue development [GO:0007519]*actin cytoskeleton [GO:0015629]; cleavage furrow [GO:0032154]; costamere [GO:0043034]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; invadopodium [GO:0071437]; microtubule minus-end [GO:0036449]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; podosome [GO:0002102]FUNCTION: Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O46385}.Q8WU79SMAP2%Stromal membrane-associated protein 2SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci throughout the cytoplasm and in juxtanuclear structures. {ECO:0000250}.FUNCTION: GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity). {ECO:0000250}.P02794FRIHFerritin heavy chaincellular iron ion homeostasis [GO:0006879]; immune response [GO:0006955]; intracellular sequestering of iron ion [GO:0006880]; iron ion transport [GO:0006826]; membrane organization [GO:0061024]; negative regulation of cell proliferation [GO:0008285]; negative regulation of fibroblast proliferation [GO:0048147]; post-Golgi vesicle-mediated transport [GO:0006892]; receptor-mediated endocytosis [GO:0006898]; transmembrane transport [GO:0055085]bferric iron binding [GO:0008199]; ferroxidase activity [GO:0004322]; iron ion binding [GO:0005506]{cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular ferritin complex [GO:0008043]; nucleus [GO:0005634]hFUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250}.Q68DK2ZFY26-Zinc finger FYVE domain-containing protein 26SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20208530}. Midbody {ECO:0000269|PubMed:20208530}. Note=Localizes to the centrosome during all stages of the cell cycle. Recruited to the midbody during cytokinesis by KIF13A.^cytokinesis [GO:0000910]; double-strand break repair via homologous recombination [GO:0000724]Umetal ion binding [GO:0046872]; phosphatidylinositol-3-phosphate binding [GO:0032266]Ncentrosome [GO:0005813]; lysosomal membrane [GO:0005765]; midbody [GO:0030496]7FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20208530}.Q96JG8MAGD4Melanoma-associated antigen D4 FUNCTION: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. {ECO:0000269|PubMed:20864041}.P35711SOX5Transcription factor SOX-5cartilage development [GO:0051216]; cell fate commitment [GO:0045165]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system neuron differentiation [GO:0021953]; in utero embryonic development [GO:0001701]; negative regulation of transcription, DNA-templated [GO:0045892]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cartilage development [GO:0061036]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of mesenchymal stem cell differentiation [GO:2000741]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of timing of neuron differentiation [GO:0060164]; transcription from RNA polymerase II promoter [GO:0006366]sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription regulatory region DNA binding [GO:0044212]1nuclear transcription factor complex [GO:0044798]sFUNCTION: Binds specifically to the DNA sequence 5'-AACAAT-3'. Activates transcription of COL2A1 and AGC1 in vitro.Q15392DHC24Delta(24)-sterol reductaseSUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein.Pamyloid precursor protein catabolic process [GO:0042987]; apoptotic process [GO:0006915]; cell cycle arrest [GO:0007050]; cholesterol biosynthetic process [GO:0006695]; male genitalia development [GO:0030539]; membrane organization [GO:0061024]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell proliferation [GO:0008285]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; oxidation-reduction process [GO:0055114]; plasmin< ogen activation [GO:0031639]; protein localization [GO:0008104]; Ras protein signal transduction [GO:0007265]; regulation of neuron death [GO:1901214]; response to hormone [GO:0009725]; response to oxidative stress [GO:0006979]; skin development [GO:0043588]; small molecule metabolic process [GO:0044281]; tissue development [GO:0009888]wdelta24(24-1) sterol reductase activity [GO:0000246]; delta24-sterol reductase activity [GO:0050614]; enzyme binding [GO:0019899]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; peptide antigen binding [GO:0042605]; UDP-N-acetylmuramate dehydrogenase activity [GO:0008762]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; nucleus [GO:0005634]_FUNCTION: Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis. {ECO:0000269|PubMed:11007892, ECO:0000269|PubMed:11519011, ECO:0000269|PubMed:22010141}.Q14693LPIN1Phosphatidate phosphatase LPIN1SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}.cellular lipid metabolic process [GO:0044255]; cellular response to insulin stimulus [GO:0032869]; dephosphorylation [GO:0016311]; fatty acid catabolic process [GO:0009062]; glycerophospholipid biosynthetic process [GO:0046474]; mitotic cell cycle [GO:0000278]; mitotic nuclear envelope disassembly [GO:0007077]; organ regeneration [GO:0031100]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phospholipid metabolic process [GO:0006644]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; triglyceride biosynthetic process [GO:0019432]; triglyceride mobilization [GO:0006642]cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A/PPARA to modulate lipid metabolism gene expression (By similarity). Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}.Q9HBL0TENS1Tensin-1bSUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21768292}. Cell junction, focal adhesion {ECO:0000269|PubMed:21768292}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21768292}. Note=Localized at cell periphery preferentially to fibrillar adhesions than focal adhesions. Translocates from the cell edge to cell center in an ITGB1BP1-dependent manner.Pcell-substrate junction assembly [GO:0007044]; fibroblast migration [GO:0010761]icell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]FUNCTION: Involved in fibrillar adhesion formation. May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. {ECO:0000269|PubMed:21768292}.Q9UKZ1CNO11)CCR4-NOT transcription complex subunit 11cell proliferation [GO:0008283]; gene expression [GO:0010467]; gene silencing by RNA [GO:0031047]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of transcription, DNA-templated [GO:0006355]; regulation of translation [GO:0006417]; transcription, DNA-templated [GO:0006351]ICCR4-NOT complex [GO:0030014]; cytosol [GO:0005829]; nucleus [GO:0005634]FUNCTION: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is required for the association of CNOT10 with the CCR4-NOT complex. Seems not to be required for complex deadenylase function.Q9UGU0TCF20Transcription factor 20DNA binding [GO:0003677]; poly(A) RNA binding [GO:0044822]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]FUNCTION: Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.Q92626PXDNPeroxidasin homologSUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:19590037, ECO:0000269|Ref.8}. Note=Enriched in the peritubular space of fibrotic kidneys.extracellular matrix organization [GO:0030198]; hydrogen peroxide catabolic process [GO:0042744]; immune response [GO:0006955]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; oxidation-reduction process [GO:0055114]; response to oxidative stress [GO:0006979]extracellular matrix structural constituent [GO:0005201]; heme binding [GO:0020037]; interleukin-1 receptor antagonist activity [GO:0005152]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; proteinaceous extracellular matrix [GO:0005578]FUNCTION: Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation. {ECO:0000269|PubMed:18929642, ECO:0000269|PubMed:19590037}.P13612ITA4Integrin alpha-4B cell differentiation [GO:0030183]; blood coagulation [GO:0007596]; blood vessel remodeling [GO:0001974]; cell-matrix adhesion [GO:0007160]; cell-matrix adhesion involved in ameboidal cell migration [GO:0003366]; cellular response to cytokine stimulus [GO:0071345]; chorio-allantoic fusion [GO:0060710]; diapedesis [GO:0050904]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; face development [GO:0060324]; heart development [GO:0007507]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; heterotypic cell-cell adhesion [GO:0034113]; import into cell [GO:0098657]; integrin-mediated signaling pathway [GO:0007229]; leukocyte cell-cell adhesion [GO:0007159]; leukocyte migration [GO:0050900]; leukocyte tethering or rolling [GO:0050901]; negative regulation of protein homodimerization activity [GO:0090074]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of T cell migration [GO:2000406]; receptor clustering [GO:0043113]; regulation of immune response [GO:0050776]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell migration [GO:0072678]Kcell adhesion molecule binding [GO:0050839]; metal ion binding [GO:0046872] cell-cell junction [GO:0005911]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integrin alpha4-beta7 complex [GO:0034669]; membrane [GO:0016020]; plasma membrane [GO:0005886]< vFUNCTION: Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. {ECO:0000269|PubMed:19064666}.Q9BQ95ECSITNEvolutionarily conserved signaling intermediate in Toll pathway, mitochondrialSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17344420}. Nucleus {ECO:0000269|PubMed:17344420}. Mitochondrion {ECO:0000269|PubMed:17344420}.innate immune response [GO:0045087]; oxidation-reduction process [GO:0055114]; regulation of oxidoreductase activity [GO:0051341]7oxidoreductase activity, acting on NAD(P)H [GO:0016651]FUNCTION: Adapter protein of the Toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development (By similarity). {ECO:0000250}.; FUNCTION: Required for efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase.Q9BV73CP250$Centrosome-associated protein CEP250SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:9647649}. Note=Component of the core centrosome. In interphase cells, it specifically associates with the proximal ends of both mother and daughter centrioles. Associates with the centrosome in interphase cells. In mitotic cells, it dissociates from the mitotic spindle poles. At the end of cell division, it reaccumulates at centrosomes. In photoreceptors, found at the proximal ends of basal bodies._centriole-centriole cohesion [GO:0010457]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; nonmotile primary cilium assembly [GO:0035058]; organelle organization [GO:0006996]; protein localization [GO:0008104]; protein localization to organelle [GO:0033365]; regulation of centriole-centriole cohesion [GO:0030997]zprotein C-terminus binding [GO:0008022]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]centriole [GO:0005814]; centrosome [GO:0005813]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815]; perinuclear region of cytoplasm [GO:0048471]; protein complex [GO:0043234]; spindle pole centrosome [GO:0031616]TFUNCTION: Probably plays an important role in centrosome cohesion during interphase.P17096HMGA1'High mobility group protein HMG-I/HMG-Ybase-excision repair [GO:0006284]; DNA unwinding involved in DNA replication [GO:0006268]; establishment of integrated proviral latency [GO:0075713]; negative regulation of cell proliferation [GO:0008285]; negative regulation of chromatin silencing [GO:0031936]; negative regulation of transcription, DNA-templated [GO:0045892]; nucleosome disassembly [GO:0006337]; oncogene-induced cell senescence [GO:0090402]; positive regulation of cellular senescence [GO:2000774]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein complex assembly [GO:0006461]; regulation of transcription, DNA-templated [GO:0006355]; response to virus [GO:0009615]; senescence-associated heterochromatin focus assembly [GO:0035986]; transcription from RNA polymerase II promoter [GO:0006366]; viral process [GO:0016032]5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; AT DNA binding [GO:0003680]; chromatin binding [GO:0003682]; DNA-(apurinic or apyrimidinic site) lyase activity [GO:0003906]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; ligand-dependent nuclear receptor transcription coactivator activity [GO:0030374]; peroxisome proliferator activated receptor binding [GO:0042975]; retinoic acid receptor binding [GO:0042974]; retinoid X receptor binding [GO:0046965]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; sequence-specific DNA binding transcription factor activity [GO:0003700]; transcription factor binding [GO:0008134]cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription factor complex [GO:0090575]; senescence-associated heterochromatin focus [GO:0035985]; transcription factor complex [GO:0005667]WFUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.Q9Y6X9MORC2)MORC family CW-type zinc finger protein 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20225202}. Cytoplasm, cytosol {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:24286864}. Note=Mainly located in the nucleus.;FUNCTION: Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation. May act as a transcriptional repressor. Down-regulates CA9 expression. {ECO:0000269|PubMed:20110259, ECO:0000269|PubMed:20225202}.P17535JUNDTranscription factor jun-Daging [GO:0007568]; cellular response to calcium ion [GO:0071277]; cellular response to hormone stimulus [GO:0032870]; circadian rhythm [GO:0007623]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; osteoblast development [GO:0002076]; positive regulation of cell differentiation [GO:0045597]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cell death [GO:0010941]; regulation of cell proliferation [GO:0042127]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; response to cAMP [GO:0051591]; response to cytokine [GO:0034097]; response to drug [GO:0042493]; response to light stimulus [GO:0009416]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; response to peptide hormone [GO:0043434]; response to radiation [GO:0009314]; transcription from RNA polymerase II promoter [GO:0006366]double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding RNA polymerase II transcription factor activity [GO:0000981]; transcription coactivator activity [GO:0003713]; transcription factor binding [GO:0008134]; transcription regulatory region DNA binding [GO:0044212]chromatin [GO:0000785]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription factor complex [GO:0005667]PFUNCTION: Transcription factor binding AP-1 sites. {ECO:0000269|PubMed:9989505}.O76080ZFAN5AN1-type zinc finger protein 5_face development [GO:0060324]; fibroblast migration [GO:0010761]; in utero embryonic development [GO:0001701]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; respiratory system process [GO:0003016]; skeletal system morphogenesis [GO:0048705]; smooth muscle tissue development [GO:0048745]; vasculature development [GO:0001944]FUNCTION: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in u< biquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. {ECO:0000269|PubMed:14754897}.P16989YBOX3Y-box-binding protein 33'-UTR-mediated mRNA stabilization [GO:0070935]; cellular hyperosmotic response [GO:0071474]; cellular response to tumor necrosis factor [GO:0071356]; fertilization [GO:0009566]; in utero embryonic development [GO:0001701]; male gonad development [GO:0008584]; negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902219]; negative regulation of necroptotic process [GO:0060546]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of organ growth [GO:0046622]; response to cold [GO:0009409]; spermatogenesis [GO:0007283]; transcription, DNA-templated [GO:0006351]/double-stranded DNA binding [GO:0003690]; mRNA 3'-UTR binding [GO:0003730]; poly(A) RNA binding [GO:0044822]; Rho GTPase binding [GO:0017048]; RNA polymerase II regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription [GO:0001227]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]; transcription corepressor activity [GO:0003714]bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; polysome [GO:0005844]FUNCTION: Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression (By similarity). {ECO:0000250}.P30530UFO$Tyrosine-protein kinase receptor UFOSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7896447}; Single-pass type I membrane protein {ECO:0000269|PubMed:7896447}.Napoptotic cell clearance [GO:0043277]; blood vessel remodeling [GO:0001974]; cell maturation [GO:0048469]; cellular response to extracellular stimulus [GO:0031668]; cellular response to interferon-alpha [GO:0035457]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell differentiation [GO:0097028]; erythrocyte homeostasis [GO:0034101]; forebrain cell migration [GO:0021885]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; natural killer cell differentiation [GO:0001779]; negative regulation of dendritic cell apoptotic process [GO:2000669]; negative regulation of interferon-gamma production [GO:0032689]; negative regulation of lymphocyte activation [GO:0051250]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of tumor necrosis factor production [GO:0032720]; neuron migration [GO:0001764]; ovulation cycle [GO:0042698]; peptidyl-tyrosine phosphorylation [GO:0018108]; phagocytosis [GO:0006909]; platelet activation [GO:0030168]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of pinocytosis [GO:0048549]; positive regulation of protein kinase B signaling [GO:0051897]; protein kinase B signaling [GO:0043491]; secretion by cell [GO:0032940]; signal transduction [GO:0007165]; spermatogenesis [GO:0007283]; substrate adhesion-dependent cell spreading [GO:0034446]; vagina development [GO:0060068]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; viral entry into host cell [GO:0046718]ATP binding [GO:0005524]; phosphatidylserine binding [GO:0001786]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; host cell surface [GO:0044228]; integral component of plasma membrane [GO:0005887]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. In case of filovirus infection, seems to function as a cell entry factor. {ECO:0000269|PubMed:10403904, ECO:0000269|PubMed:11484958, ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:12490074, ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:15733062, ECO:0000269|PubMed:1656220, ECO:0000269|PubMed:17005688, ECO:0000269|PubMed:18840707}.Q8N357S35F6"Solute carrier family 35 member F6TSUBCELLULAR LOCATION: Mitochondrion. Lysosome membrane; Multi-pass membrane protein.negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; positive regulation of cell proliferation [GO:0008284]; transport [GO:0006810]extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739] FUNCTION: Involved in the maintenance of mitochondrial membrane potential in pancreatic ductal adenocarcinoma (PDAC) cells. Promotes pancreatic ductal adenocarcinoma (PDAC) cell growth. May play a role as a nucleotide-sugar transporter. {ECO:0000269|PubMed:19154410}.P52747ZN143Zinc finger protein 143gene expression [GO:0010467]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription from RNA polymerase III promoter [GO:0006359]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription from RNA polymerase III promoter [GO:0006383]; transcription from RNA polymerase II promoter [GO:0006366]6FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8. {ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:9776743}.P08236BGLRBeta-glucuronidasecarbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; hyaluronan catabolic process [GO:0030214]; hyaluronan metabolic process [GO:0030212]; small molecule metabolic process [GO:0044281]ubeta-glucuronidase activity [GO:0004566]; protein domain specific binding [GO:0019904]; receptor binding [GO:0005102]extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]VFUNCTION: Pla< ys an important role in the degradation of dermatan and keratan sulfates.Q86U28ISCA25Iron-sulfur cluster assembly 2 homolog, mitochondrialBSUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22323289}.FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. May be involved in the binding of an intermediate of Fe/S cluster assembly. {ECO:0000269|PubMed:22323289}.Q9Y3I1FBX7F-box only protein 7SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Cytoplasm, cytosol. Note=Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria.mitochondrion degradation [GO:0000422]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of lymphocyte differentiation [GO:0045620]; protein targeting to mitochondrion [GO:0006626]; protein ubiquitination [GO:0016567]; regulation of protein stability [GO:0031647]; ubiquitin-dependent protein catabolic process [GO:0006511]cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein complex [GO:0043234]; ubiquitin ligase complex [GO:0000151] FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PARK2 to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination. {ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:16510124, ECO:0000269|PubMed:23933751}.Q99496RING2!E3 ubiquitin-protein ligase RING2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Chromosome {ECO:0000250}. Note=Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells (By similarity). {ECO:0000250}.santerior/posterior axis specification [GO:0009948]; cellular protein metabolic process [GO:0044267]; gastrulation with mouth forming second [GO:0001702]; germ cell development [GO:0007281]; histone H2A-K119 monoubiquitination [GO:0036353]; histone H2A monoubiquitination [GO:0035518]; mitotic cell cycle [GO:0000278]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; transcription, DNA-templated [GO:0006351]chromatin binding [GO:0003682]; ligase activity [GO:0016874]; RING-like zinc finger domain binding [GO:0071535]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]euchromatin [GO:0000791]; MLL1 complex [GO:0071339]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]; sex chromatin [GO:0001739]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. {ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:20696397}.Q9Y618NCOR2Nuclear receptor corepressor 2Ycellular lipid metabolic process [GO:0044255]; chromatin organization [GO:0006325]; gene expression [GO:0010467]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; Notch signaling pathway [GO:0007219]; regulation of cellular ketone metabolic process by negative regulation of transcription from RNA polymerase II promoter [GO:0072365]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transforming growth factor beta receptor signaling pathway [GO:0007179]DNA binding [GO:0003677]; histone deacetylase binding [GO:0042826]; Notch binding [GO:0005112]; protein N-terminus binding [GO:0047485]; transcription corepressor activity [GO:0003714]membrane [GO:0016020]; nuclear body [GO:0016604]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcriptional repressor complex [GO:0017053]FUNCTION: Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival. {ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:23911289}.Q96MY1NOL4LNucleolar protein 4-likeQ13444ADA15>Disintegrin and metalloproteinase domain-containing protein 15 ADAMs(16)mSUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein {ECO:0000269|PubMed:12243749}. Cell junction, adherens junction {ECO:0000269|PubMed:12243749}. Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity). {ECO:0000250}.vangiogenesis [GO:0001525]; cardiac epithelial to mesenchymal transition [GO:0060317]; cell-matrix adhesion [GO:0007160]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of cell growth [GO:0030308]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cell migration [GO:0030336]; negative regulation of receptor binding [GO:1900121]; protein kinase C signaling [GO:0070528]; tissue regeneration [GO:0042246]integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270]acrosomal vesicle [GO:0001669]; adherens junction [GO:0005912]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta< -1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.Q9UBW7ZMYM2Zinc finger MYM-type protein 2Pubiquitin conjugating enzyme binding [GO:0031624]; zinc ion binding [GO:0008270]+cytosol [GO:0005829]; PML body [GO:0016605]1FUNCTION: May function as a transcription factor.Q96IV0NGLY1;Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15358861}.+glycoprotein catabolic process [GO:0006516]ometal ion binding [GO:0046872]; peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity [GO:0000224]FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. {ECO:0000269|PubMed:14749736, ECO:0000269|PubMed:15358861}.P13284GILT4Gamma-interferon-inducible lysosomal thiol reductase)SUBCELLULAR LOCATION: Secreted. Lysosome.antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; cytokine-mediated signaling pathway [GO:0019221]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of fibroblast proliferation [GO:0048147]; protein stabilization [GO:0050821]Hoxidoreductase activity, acting on a sulfur group of donors [GO:0016667]cell junction [GO:0030054]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; plasma membrane [GO:0005886] FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds (By similarity). Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation (By similarity). {ECO:0000250}.Q9NV92NFIP2"NEDD4 family-interacting protein 2SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane. Endosome, multivesicular body membrane.Knegative regulation of gene expression [GO:0010629]; negative regulation of protein transport [GO:0051224]; negative regulation of transporter activity [GO:0032410]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of protein ubiquitination [GO:0031398]; signal transduction [GO:0007165]Gsignal transducer activity [GO:0004871]; WW domain binding [GO:0050699]Ncytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; multivesicular body membrane [GO:0032585]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. May modulate EGFR signaling. {ECO:0000269|PubMed:12761501, ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:20534535}.Q9BWF3RBM4RNA-binding protein 4LSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus speckle. Cytoplasm. Cytoplasmic granule. Note=Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation.cap-independent translational initiation [GO:0002190]; cell differentiation [GO:0030154]; circadian regulation of translation [GO:0097167]; entrainment of circadian clock by photoperiod [GO:0043153]; IRES-dependent translational initiation [GO:0002192]; mRNA processing [GO:0006397]; negative regulation of translation [GO:0017148]; negative regulation of translational initiation [GO:0045947]; negative regulation of translation in response to stress [GO:0032055]; negative regulation of translation involved in gene silencing by miRNA [GO:0035278]; positive regulation of muscle cell differentiation [GO:0051149]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of nucleocytoplasmic transport [GO:0046822]; response to arsenic-containing substance [GO:0046685]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; stress-activated MAPK cascade [GO:0051403]3miRNA binding [GO:0035198]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; pre-mRNA intronic binding [GO:0097157]; pre-mRNA intronic pyrimidine-rich binding [GO:0097158]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]NFUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. {ECO:0000269|PubMed:12628928, ECO:0000269|PubMed:16260624, ECO:0000269|PubMed:16777< 844, ECO:0000269|PubMed:16934801, ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:19801630, ECO:0000269|PubMed:21343338, ECO:0000269|PubMed:21518792}.Q15147PLCB4@1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4inositol phosphate metabolic process [GO:0043647]; intracellular signal transduction [GO:0035556]; lipid catabolic process [GO:0016042]; negative regulation of potassium ion transport [GO:0043267]; small molecule metabolic process [GO:0044281]calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; signal transducer activity [GO:0004871]cytosol [GO:0005829]; dendrite [GO:0030425]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; smooth endoplasmic reticulum [GO:0005790]FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction.P61769B2MGBeta-2-microglobulinzSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1336137, ECO:0000269|PubMed:7554280}. Note=Detected in serum and urine.>antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent [GO:0002481]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cytokine-mediated signaling pathway [GO:0019221]; innate immune response [GO:0045087]; interferon-gamma-mediated signaling pathway [GO:0060333]; iron ion homeostasis [GO:0055072]; negative regulation of receptor binding [GO:1900121]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; protein refolding [GO:0042026]; regulation of defense response to virus by virus [GO:0050690]; regulation of immune response [GO:0050776]; response to cadmium ion [GO:0046686]; response to drug [GO:0042493]; response to molecule of bacterial origin [GO:0002237]; retina homeostasis [GO:0001895]; T cell differentiation in thymus [GO:0033077]; viral process [GO:0016032]Iglycoprotein binding [GO:0001948]; identical protein binding [GO:0042802]fcytoplasm [GO:0005737]; early endosome lumen [GO:0031905]; early endosome membrane [GO:0031901]; endoplasmic reticulum lumen [GO:0005788]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; HFE-transferrin receptor complex [GO:1990712]; membrane [GO:0016020]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.Q5VZL5ZMYM4Zinc finger MYM-type protein 4O95166GBRAP3Gamma-aminobutyric acid receptor-associated protein%SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (By similarity). Localizes also to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250}.Jautophagosome assembly [GO:0000045]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; membrane fusion [GO:0061025]; microtubule cytoskeleton organization [GO:0000226]; mitochondrion degradation [GO:0000422]; nucleophagy [GO:0044804]; protein targeting [GO:0006605]; synaptic transmission [GO:0007268]gbeta-tubulin binding [GO:0048487]; GABA receptor binding [GO:0050811]; microtubule binding [GO:0008017]actin cytoskeleton [GO:0015629]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; axoneme [GO:0005930]; cell body [GO:0044297]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; pre-autophagosomal structure [GO:0000407]; smooth endoplasmic reticulum [GO:0005790]yFUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. {ECO:0000269|PubMed:15977068}.Q6DN90IQEC1-IQ motif and SEC7 domain-containing protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11226253}. Nucleus {ECO:0000269|PubMed:11226253}. Note=At steady state, may be preferentially cytosolic.hactin cytoskeleton organization [GO:0030036]; regulation of ARF protein signal transduction [GO:0032012]FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6 (PubMed:24058294). Guanine nucleotide exchange factor activity is enhanced by lipid binding (PubMed:24058294). Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin. {ECO:0000269|PubMed:11226253, ECO:0000269|PubMed:16461286, ECO:0000269|PubMed:24058294}.Q96G46DUS3L1tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-likeflavin adenine dinucleotide binding [GO:0050660]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; tRNA dihydrouridine synthase activity [GO:0017150]vFUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.Q96QD9UIFUAP56-interacting factorxSUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:19836239}. Nucleus speckle {ECO:0000269|PubMed:19836239}.%mRNA export from nucleus [GO:0006406]1FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4. {ECO:0000269|PubMed:19836239}.O14782KIF3CKinesin-like protein KIF3C=antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; organelle organization [GO:0006996]; organelle transport along microtubule [GO:0072384]ciliary tip [GO:0097542]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; primary cilium [GO:0072372]^FUNCTION: Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.Q96LU7MRFL%Myelin regulatory factor-like proteinQ9Y3Y2CHTOP!Chromatin target of PRMT1 protein6SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle. Note=Mostly associated with facultative heterochromatin (By similarity). Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. {ECO:0000250}.mRNA export from nucleus [GO:0006406]; positive regulation of ATPase activity [GO:0032781]; positive regulation of helicase activi< ty [GO:0051096]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; transcription export complex [GO:0000346]UFUNCTION: Plays an important role in the ligand-dependent activation of estrogen receptor target genes. May play a role in the silencing of fetal globin genes. Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.; FUNCTION: Required for effective mRNA nuclear export and is a component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Stimulates DDX39B ATPase and helicase activities. In cooperation with ALYREF/THOC4 enhances NXF1 RNA binding activity.Q96EB6SIR1+NAD-dependent protein deacetylase sirtuin-1SUBCELLULAR LOCATION: Nucleus, PML body. Cytoplasm. Nucleus {ECO:0000269|PubMed:20955178}. Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane. Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (PubMed:20955178). {ECO:0000250|UniProtKB:Q923E4, ECO:0000269|PubMed:20955178}.; SUBCELLULAR LOCATION: SirtT1 75 kDa fragment: Cytoplasm. Mitochondrion.angiogenesis [GO:0001525]; behavioral response to starvation [GO:0042595]; cell aging [GO:0007569]; cellular glucose homeostasis [GO:0001678]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to heat [GO:0034605]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to ionizing radiation [GO:0071479]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; cellular triglyceride homeostasis [GO:0035356]; cholesterol homeostasis [GO:0042632]; chromatin organization [GO:0006325]; chromatin silencing [GO:0006342]; chromatin silencing at rDNA [GO:0000183]; circadian regulation of gene expression [GO:0032922]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA synthesis involved in DNA repair [GO:0000731]; establishment of chromatin silencing [GO:0006343]; fatty acid homeostasis [GO:0055089]; gene expression [GO:0010467]; histone deacetylation [GO:0016575]; histone H3 deacetylation [GO:0070932]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; maintenance of chromatin silencing [GO:0006344]; methylation-dependent chromatin silencing [GO:0006346]; muscle organ development [GO:0007517]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; negative regulation of cell growth [GO:0030308]; negative regulation of cellular response to testosterone stimulus [GO:2000655]; negative regulation of cellular senescence [GO:2000773]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of helicase activity [GO:0051097]; negative regulation of histone H3-K14 acetylation [GO:0071441]; negative regulation of histone H4-K16 acetylation [GO:2000619]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of neuron death [GO:1901215]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; negative regulation of phosphorylation [GO:0042326]; negative regulation of prostaglandin biosynthetic process [GO:0031393]; negative regulation of protein acetylation [GO:1901984]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of sequence-specific DNA binding transcription factor activity [GO:0043433]; negative regulation of TOR signaling [GO:0032007]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; ovulation from ovarian follicle [GO:0001542]; peptidyl-lysine acetylation [GO:0018394]; peptidyl-lysine deacetylation [GO:0034983]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular senescence [GO:2000774]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of chromatin silencing [GO:0031937]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA repair [GO:0045739]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of histone H3-K9 methylation [GO:0051574]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of macroautophagy [GO:0016239]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deacetylation [GO:0006476]; protein destabilization [GO:0031648]; protein ubiquitination [GO:0016567]; pyrimidine dimer repair by nucleotide-excision repair [GO:0000720]; regulation of bile acid biosynthetic process [GO:0070857]; regulation of cell proliferation [GO:0042127]; regulation of cellular response to heat [GO:1900034]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of gene expression, epigenetic [GO:0040029]; regulation of glucose metabolic process [GO:0010906]; regulation of mitotic cell cycle [GO:0007346]; regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035358]; regulation of protein import into nucleus, translocation [GO:0033158]; regulation of smooth muscle cell apoptotic process [GO:0034391]; response to hydrogen peroxide [GO:0042542]; response to insulin [GO:0032868]; response to oxidative stress [GO:0006979]; rRNA processing [GO:0006364]; single strand break repair [GO:0000012]; spermatogenesis [GO:0007283]; stress-induced premature senescence [GO:0090400]; transcription, DNA-templated [GO:0006351]; triglyceride mobilization [GO:0006642]; UV-damage excision repair [GO:0070914]; viral process [GO:0016032]; white fat cell differentiation [GO:0050872]bHLH transcription factor binding [GO:0043425]; core promoter sequence-specific DNA binding [GO:0001046]; deacetylase activity [GO:0019213]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; histone deacetylase activity [GO:0004407]; HLH domain binding [GO:0043398]; identical protein binding [GO:0042802]; keratin filament bin< ding [GO:1990254]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; NAD-dependent histone deacetylase activity (H3-K9 specific) [GO:0046969]; NAD-dependent protein deacetylase activity [GO:0034979]; nuclear hormone receptor binding [GO:0035257]; p53 binding [GO:0002039]; protein C-terminus binding [GO:0008022]; protein deacetylase activity [GO:0033558]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]chromatin silencing complex [GO:0005677]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear chromatin [GO:0000790]; nuclear envelope [GO:0005635]; nuclear euchromatin [GO:0005719]; nuclear heterochromatin [GO:0005720]; nuclear inner membrane [GO:0005637]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; rDNA heterochromatin [GO:0033553]0FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Modulates AP-1 transcription factor activity. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates ACSS2 leading to its activation, and HMGCS1. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellu< lar senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Isoform 2 is shown to deacetylate 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20975832, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21909281, PubMed:21947282, PubMed:22274616). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). {ECO:0000250|UniProtKB:Q923E4, ECO:0000269|PubMed:11672523, ECO:0000269|PubMed:12006491, ECO:0000269|PubMed:14976264, ECO:0000269|PubMed:14980222, ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:15152190, ECO:0000269|PubMed:15205477, ECO:0000269|PubMed:15469825, ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16166628, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:16998810, ECO:0000269|PubMed:17283066, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17334224, ECO:0000269|PubMed:17505061, ECO:0000269|PubMed:17612497, ECO:0000269|PubMed:17620057, ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18203716, ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19188449, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:19364925, ECO:0000269|PubMed:19690166, ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20097625, ECO:0000269|PubMed:20100829, ECO:0000269|PubMed:20203304, ECO:0000269|PubMed:20375098, ECO:0000269|PubMed:20620956, ECO:0000269|PubMed:20670893, ECO:0000269|PubMed:20817729, ECO:0000269|PubMed:20955178, ECO:0000269|PubMed:20975832, ECO:0000269|PubMed:21149730, ECO:0000269|PubMed:21245319, ECO:0000269|PubMed:21471201, ECO:0000269|PubMed:21504832, ECO:0000269|PubMed:21555002, ECO:0000269|PubMed:21698133, ECO:0000269|PubMed:21701047, ECO:0000269|PubMed:21775285, ECO:0000269|PubMed:21807113, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21890893, ECO:0000269|PubMed:21909281, ECO:0000269|PubMed:21947282, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780}.; FUNCTION: SirtT1 75 kDa fragment: catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000269|PubMed:21987377}.Q9BSJ5CQ080 Uncharacterized protein C17orf80Q9Y388RBMX2%RNA-binding motif protein, X-linked 2Q6PL18ATAD2-ATPase family AAA domain-containing protein 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17998543}.negative regulation of chromatin silencing [GO:0031936]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]tATPase activity [GO:0016887]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; histone binding [GO:0042393]FUNCTION: May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. {ECO:0000269|PubMed:17998543}.Q9BTL3RAMRNMT-activating mini protein<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22099306}.7-methylguanosine mRNA capping [GO:0006370]; methylation [GO:0032259]; recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex [GO:0036031];mRNA cap binding complex [GO:0005845]; nucleus [GO:0005634]FUNCTION: Required for efficient mRNA cap methylation. Regulates RNMT expression by a post-transcriptional stabilizing mechanism. {ECO:0000269|PubMed:22099306}.Q92828COR2A Coronin-2A\actin cytoskeleton organization [GO:0030036]; intracellular signal transduction [GO:0035556]Oactin cytoskeleton [GO:0015629]; transcriptional repressor complex [GO:0017053]O60488ACSL4#Long-chain-fatty-acid--CoA ligase 4cellular lipid metabolic process [GO:0044255]; dendritic spine development [GO:0060996]; embryonic process involved in female pregnancy [GO:0060136]; fatty acid transport [GO:0015908]; lipid biosynthetic process [GO:0008610]; lipid metabolic process [GO:0006629]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; negative regulation of prostaglandin secretion [GO:0032307]; positive regulation of cell growth [GO:0030307]; response to interleukin-15 [GO:0070672]; response to nutrient [GO:0007584]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; very long-chain fatty acid-CoA ligase activity [GO:0031957]lcytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; ER-mitochondrion membrane contact site [GO:0044233]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; lipid particle [GO:0005811]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuronal cell body [GO:0043025]; peroxisomal membrane [GO:0005778]FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arach< idonate and eicosapentaenoate as substrates.Q5T5P2SKTSickle tail protein homolog?SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AQ25}.2embryonic skeletal system development [GO:0048706]bFUNCTION: Required for normal development of intervertebral disks. {ECO:0000250|UniProtKB:A2AQ25}.Q8N999CL029 Uncharacterized protein C12orf29Q9H4G0E41L1Band 4.1-like protein 1Ycortical actin cytoskeleton organization [GO:0030866]; synaptic transmission [GO:0007268]cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; neuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]FUNCTION: May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases.Q96B54ZN428Zinc finger protein 428O95674CDS2$Phosphatidate cytidylyltransferase 2CDP-diacylglycerol biosynthetic process [GO:0016024]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid metabolic process [GO:0006644]; small molecule metabolic process [GO:0044281]endoplasmic reticulum membrane [GO:0005789]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]FUNCTION: Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin.Q8TEJ3SH3R3+SH3 domain-containing RING finger protein 3Q8IWY9CDAN1 Codanin-1SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Mainly detected as a cytoplasmic protein.chromatin assembly [GO:0031497]; chromatin organization [GO:0006325]; negative regulation of DNA replication [GO:0008156]; protein localization [GO:0008104]cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; integral component of membrane [GO:0016021]; nucleus [GO:0005634]; plasma membrane [GO:0005886]hFUNCTION: May acts as a negative regulator of ASF1 in chromatin assembly. {ECO:0000269|PubMed:22407294}.Q14739LBRLamin-B receptorJSUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein.chromo shadow domain binding [GO:0070087]; DNA binding [GO:0003677]; lamin binding [GO:0005521]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; poly(A) RNA binding [GO:0044822]integral component of membrane [GO:0016021]; integral component of nuclear inner membrane [GO:0005639]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]rFUNCTION: Anchors the lamina and the heterochromatin to the inner nuclear membrane. {ECO:0000269|PubMed:10828963}.Q9Y5S2MRCKB)Serine/threonine-protein kinase MRCK betajSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:21240187}; Peripheral membrane protein {ECO:0000269|PubMed:21240187}; Cytoplasmic side {ECO:0000269|PubMed:21240187}. Cell junction {ECO:0000269|PubMed:21240187}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). Detected at the leading edge of migrating cells. Localization at the leading edge of migrating cells requires interaction with catalytically active CDC42. {ECO:0000250}.Wactin cytoskeleton reorganization [GO:0031532]; actomyosin structure organization [GO:0031032]; cell migration [GO:0016477]; cytoskeleton organization [GO:0007010]; establishment or maintenance of cell polarity [GO:0007163]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]actomyosin [GO:0042641]; cell-cell junction [GO:0005911]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A. {ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:21949762}.Q9Y4R8TELO2/Telomere length regulation protein TEL2 homologWSUBCELLULAR LOCATION: Cytoplasm. Membrane. Nucleus. Chromosome, telomere {ECO:0000305}.(regulation of TOR signaling [GO:0032006]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; intracellular [GO:0005622]; membrane [GO:0016020]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation. {ECO:0000269|PubMed:12670948, ECO:0000269|PubMed:20810650}.Q96CB8INT12Integrator complex subunit 12Q7LBC6KDM3BLysine-specific demethylase 3Bchromatin modification [GO:0016568]; chromatin organization [GO:0006325]; regulation of transcription, DNA-templated [GO:0006355]; response to cisplatin [GO:0072718]; transcription, DNA-templated [GO:0006351]dantioxidant activity [GO:0016209]; dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872] FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. {ECO:0000269|PubMed:16603237}.Q1MX18INSCProtein inscuteable homologSUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to the apical cortex of mitotic epidermal cells and to the apical side of neuronal progenitor cells. {ECO:0000250}.establishment of mitotic spindle orientation [GO:0000132]; lung epithelial cell differentiation [GO:0060487]; nervous system development [GO:0007399]8apical part of cell [GO:0045177]; cytoplasm [GO:0005737]FUNCTION: May function as an adapter linking the Par3 complex to the GPSM1/GPSM2 complex. Involved in spindle orientation during mitosis it may regulate cell proliferation and differentiation in the developing nervous system. May play a role in the asymmetric division of fibroblasts and participate in the process of stratification of the squamous epithelium. {ECO:0000269|PubMed:16458856}.Q14573ITPR3,Inositol 1,4,5-trisphosphate receptor type 3Lactivation of phospholipase C activity [GO:0007202]; blood coagulation [GO:0007596]; calcium ion transport into cytosol [GO:0060402]; energy reserve metabolic process [GO:0006112]; epidermal growth factor receptor signaling pathway [GO:0007173]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G-protein coupled receptor signaling pathway [GO:0007186]; innate immune response [GO:0045087]; inositol phosphate-mediated signaling [GO:0048016]; long-term synaptic potentiation [GO:0060291]; memory [GO:0007613]; neurotrophin TRK receptor signaling pathway [GO:0048011]; platelet activation [GO:0030168]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; protein heterooligomerization [GO:0051291]; protein h< omooligomerization [GO:0051260]; regulation of insulin secretion [GO:0050796]; response to calcium ion [GO:0051592]; sensory perception of bitter taste [GO:0050913]; sensory perception of sweet taste [GO:0050916]; sensory perception of umami taste [GO:0050917]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]]inositol 1,3,4,5 tetrakisphosphate binding [GO:0043533]; inositol 1,4,5 trisphosphate binding [GO:0070679]; inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity [GO:0005220]; inositol hexakisphosphate binding [GO:0000822]; intracellular ligand-gated calcium channel activity [GO:0005218]; phosphatidylinositol binding [GO:0035091] apical part of cell [GO:0045177]; brush border [GO:0005903]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nuclear outer membrane [GO:0005640]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; platelet dense tubular network membrane [GO:0031095]; receptor complex [GO:0043235]{FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.Q9BQE5APOL2Apolipoprotein L2,acute-phase response [GO:0006953]; cholesterol metabolic process [GO:0008203]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; maternal process involved in female pregnancy [GO:0060135]; multicellular organismal development [GO:0007275]qhigh-density lipoprotein particle binding [GO:0008035]; lipid binding [GO:0008289]; receptor binding [GO:0005102]eendoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; membrane [GO:0016020]jFUNCTION: May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.Q14681KCTD2'BTB/POZ domain-containing protein KCTD2O14647CHD2+Chromodomain-helicase-DNA-binding protein 2bSUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binds to myogenic gene promoters. {ECO:0000250}.Ocellular response to DNA damage stimulus [GO:0006974]; chromatin modification [GO:0016568]; DNA duplex unwinding [GO:0032508]; hematopoietic stem cell differentiation [GO:0060218]; muscle organ development [GO:0007517]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; histone binding [GO:0042393]; poly(A) RNA binding [GO:0044822]extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. Involved in myogenesis via interaction with MYOD1: binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression (By similarity). {ECO:0000250}.O75379VAMP4%Vesicle-associated membrane protein 4SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles.exocytosis [GO:0006887]; Golgi ribbon formation [GO:0090161]; microtubule cytoskeleton organization [GO:0000226]; regulation of Golgi to plasma membrane protein transport [GO:0042996]; SNARE complex assembly [GO:0035493]; toxin transport [GO:1901998]; vesicle fusion [GO:0006906]cell surface [GO:0009986]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; lysosome [GO:0005764]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule.Q04656ATP7ACopper-transporting ATPase 1SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Cycles constitutively between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytosol {ECO:0000305}.; SUBCELLULAR LOCATION: Isoform 5: Endoplasmic reticulum.ATP metabolic process [GO:0046034]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; cartilage development [GO:0051216]; catecholamine metabolic process [GO:0006584]; cellular copper ion homeostasis [GO:0006878]; central nervous system neuron development [GO:0021954]; cerebellar Purkinje cell differentiation [GO:0021702]; collagen fibril organization [GO:0030199]; copper ion export [GO:0060003]; copper ion import [GO:0015677]; copper ion transport [GO:0006825]; dendrite morphogenesis [GO:0048813]; detoxification of copper ion [GO:0010273]; dopamine metabolic process [GO:0042417]; elastic fiber assembly [GO:0048251]; elastin biosynthetic process [GO:0051542]; epinephrine metabolic process [GO:0042414]; extracellular matrix organization [GO:0030198]; hair follicle morphogenesis [GO:0031069]; in utero embryonic development [GO:0001701]; ion transmembrane transport [GO:0034220]; lactation [GO:0007595]; locomotory behavior [GO:0007626]; lung alveolus development [GO:0048286]; mitochondrion organization [GO:0007005]; negative regulation of metalloenzyme activity [GO:0048553]; negative regulation of neuron apoptotic process [GO:0043524]; neuron projection morphogenesis [GO:0048812]; norepinephrine biosynthetic process [GO:0042421]; norepinephrine metabolic process [GO:0042415]; peptidyl-lysine modification [GO:0018205]; pigmentation [GO:0043473]; plasma membrane copper ion transport [GO:0015679]; positive regulation of catalytic activity [GO:0043085]; positive regulation of metalloenzyme activity [GO:0048554]; positive regulation of oxidoreductase activity [GO:0051353]; pyramidal neuron development [GO:0021860]; regulation of gene expression [GO:0010468]; regulation of oxidative phosphorylation [GO:0002082]; release of cytochrome c from mitochondria [GO:0001836]; removal of superoxide radicals [GO:0019430]; response to iron(III) ion [GO:0010041]; response to reactive oxygen species [GO:0000302]; response to zinc ion [GO:0010043]; serotonin metabolic process [GO:0042428]; skin development [GO:0043588]; T-helper cell differentiation [GO:0042093]; transmembrane transport [GO:0055085]; tryptophan metabolic process [GO:0006568]; tyrosine metabolic process [GO:0006570]ATP binding [GO:0005524]; copper-dependent protein binding [GO:0032767]; copper-exporting ATPase activity [GO:0004008]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; superoxide dismutase copper chaperone activity [GO:0016532]basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140]FUNCTION: < May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.P67870CSK2BCasein kinase II subunit betaadiponectin-activated signaling pathway [GO:0033211]; axon guidance [GO:0007411]; cellular protein complex assembly [GO:0043623]; endothelial tube morphogenesis [GO:0061154]; mitotic cell cycle [GO:0000278]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell proliferation [GO:0008285]; positive regulation of activin receptor signaling pathway [GO:0032927]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; protein phosphorylation [GO:0006468]; regulation of DNA binding [GO:0051101]; regulation of protein kinase activity [GO:0045859]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]chromatin binding [GO:0003682]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein kinase regulator activity [GO:0019887]; receptor binding [GO:0005102]; transcription factor binding [GO:0008134]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]FUNCTION: Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit. {ECO:0000250, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:16818610}.Q9H0C8ILKAPAIntegrin-linked kinase-associated serine/threonine phosphatase 2C>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331582}.FUNCTION: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation. {ECO:0000269|PubMed:14990992}.Q6QNY1BL1S2=Biogenesis of lysosome-related organelles complex 1 subunit 2SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15381421}. Note=Localizes to the centrosomes in a microtubule-dependent manner.anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; melanosome organization [GO:0032438]; microtubule nucleation [GO:0007020]; mitochondrial outer membrane permeabilization [GO:0097345]; neuron projection development [GO:0031175]; platelet dense granule organization [GO:0060155]; positive regulation of cell proliferation [GO:0008284]; positive regulation of transcription, DNA-templated [GO:0045893]Kgamma-tubulin binding [GO:0043015]; protein C-terminus binding [GO:0008022]BLOC-1 complex [GO:0031083]; centrosome [GO:0005813]; endosome [GO:0005768]; gamma-tubulin complex [GO:0000930]; mitochondrion [GO:0005739]; nucleus [GO:0005634]FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking. May play a role in cell proliferation. {ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:15381421, ECO:0000269|PubMed:17182842}.P42892ECE1Endothelin-converting enzyme 1\bradykinin catabolic process [GO:0010815]; calcitonin catabolic process [GO:0010816]; ear development [GO:0043583]; embryonic digit morphogenesis [GO:0042733]; endothelin maturation [GO:0034959]; heart development [GO:0007507]; hormone catabolic process [GO:0042447]; peptide hormone processing [GO:0016486]; pharyngeal system development [GO:0060037]; positive regulation of receptor recycling [GO:0001921]; protein processing [GO:0016485]; regulation of systemic arterial blood pressure by endothelin [GO:0003100]; regulation of vasoconstriction [GO:0019229]; substance P catabolic process [GO:0010814]endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptide hormone binding [GO:0017046]; protein homodimerization activity [GO:0042803]early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; integral component of membrane [GO:0016021]; intrinsic component of endosome membrane [GO:0031302]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle [GO:0031982]; Weibel-Palade body [GO:0033093]RFUNCTION: Converts big endothelin-1 to endothelin-1. {ECO:0000269|PubMed:9396733}.Q9H6Y7RN167"E3 ubiquitin-protein ligase RNF167SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:16314844}; Single-pass membrane protein {ECO:0000269|PubMed:16314844}. Note=Targeted to cytoplasmic membranes.Wnegative regulation of cell cycle [GO:0045786]; protein polyubiquitination [GO:0000209]ecytoplasm [GO:0005737]; endomembrane system [GO:0012505]; integral component of membrane [GO:0016021]BFUNCTION: May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition. {ECO:0000269|PubMed:16314844}.Q8IZ69TRM2A,tRNA (uracil-5-)-methyltransferase homolog Annucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA methyltransferase activity [GO:0008173]JFUNCTION: May be involved in nucleic acid metabolism and/or modifications.Q86U44MTA70-N6-adenosine-methyltransferase 70 kDa subunitSUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9409616}. Note=Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components. {ECO:0000269|PubMed:9409616}.adenosine to inosine editing [GO:0006382]; circadian rhythm [GO:0007623]; gene expression [GO:0010467]; mRNA destabilization [GO:0061157]; mRNA methylation [GO:0080009]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; primary miRNA methylation [GO:1990744]; primary miRNA processing [GO:0031053]; RNA methylation [GO:0001510]; stem cell maintenance [GO:0019827]mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity [GO:0016422]; RNA binding [GO:0003723]; RNA methyltransferase activity [GO:0008173]dMIS complex [GO:0036396]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]gFUNCTION: N6-methyltransferase that methylates adenosine residues of some RNAs and acts as a regulator of the circadian clock, differentiation of embryonic stem cells and primary miRNA processing. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing, processing, editing and mRNA stability (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:9409616). M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop (By similarity). M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization, < promoting differentiation of ESCs (By similarity). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (PubMed:25799998). Mediates methylation of pri-miRNAs, marking them for recognition and processing by DGCR8 (PubMed:25799998). {ECO:0000250|UniProtKB:Q8C3P7, ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25719671, ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:9409616}.P49069CAMLG,Calcium signal-modulating cyclophilin liganddefense response [GO:0006952]; epidermal growth factor receptor signaling pathway [GO:0007173]; receptor recycling [GO:0001881]; signal transduction [GO:0007165]; viral process [GO:0016032]FUNCTION: Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B.Q9GZY8MFFMitochondrial fission factorSUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. Peroxisome. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}.mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial fusion [GO:0008053]; mitochondrion morphogenesis [GO:0070584]; peroxisome fission [GO:0016559]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; protein homooligomerization [GO:0051260]; protein targeting to mitochondrion [GO:0006626]; regulation of mitochondrion organization [GO:0010821]; regulation of peroxisome organization [GO:1900063]; release of cytochrome c from mitochondria [GO:0001836]cell junction [GO:0030054]; integral component of mitochondrial membrane [GO:0032592]; mitochondrial outer membrane [GO:0005741]; peroxisome [GO:0005777]; synaptic vesicle [GO:0008021]zFUNCTION: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles. {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23530241}.O75131CPNE3Copine-35cellular response to calcium ion [GO:0071277]; glycerophospholipid biosynthetic process [GO:0046474]; lipid metabolic process [GO:0006629]; phospholipid metabolic process [GO:0006644]; protein phosphorylation [GO:0006468]; small molecule metabolic process [GO:0044281]; vesicle-mediated transport [GO:0016192]calcium-dependent phospholipid binding [GO:0005544]; poly(A) RNA binding [GO:0044822]; protein serine/threonine kinase activity [GO:0004674]; transporter activity [GO:0005215]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]Q7RTS9DYMDymeclin1SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Note=Sequence analysis programs clearly predict 1 transmembrane region. However, PubMed:18996921 shows that it is not a stably anchored transmembrane protein but it weakly associates with the Golgi apparatus and shuttles between the Golgi and the cytosol.>bone development [GO:0060348]; Golgi organization [GO:0007030]4cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]}FUNCTION: Necessary for correct organization of Golgi apparatus. Involved in bone development. {ECO:0000269|PubMed:21280149}.Q96E09F122AProtein FAM122AQ6P6B1ERIC5Glutamate-rich protein 5Q08397LOXL1Lysyl oxidase homolog 1BSUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.aorta development [GO:0035904]; extracellular matrix organization [GO:0030198]; oxidation-reduction process [GO:0055114]; protein deamination [GO:0018277]; response to lipopolysaccharide [GO:0032496]copper ion binding [GO:0005507]; oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor [GO:0016641]acrosomal vesicle [GO:0001669]; basement membrane [GO:0005604]; extracellular region [GO:0005576]; extracellular space [GO:0005615]CFUNCTION: Active on elastin and collagen substrates. {ECO:0000250}.Q68CP9ARID2/AT-rich interactive domain-containing protein 2chromatin modification [GO:0016568]; nucleosome disassembly [GO:0006337]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]UBAF-type complex [GO:0090544]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000269|PubMed:16782067}.Q9BW85CCD94(Coiled-coil domain-containing protein 94P04629NTRK1*High affinity nerve growth factor receptorSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15488758}; Single-pass type I membrane protein {ECO:0000269|PubMed:15488758}. Early endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Internalized to endosomes upon binding of NGF or NTF3 and further transported to the cell body via a retrograde axonal transport. Localized at cell membrane and early endosomes before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Colocalized with RAPGEF2 at late endosomes (By similarity). {ECO:0000250}.activation of adenylate cyclase activity [GO:0007190]; activation of MAPKK activity [GO:0000186]; activation of phospholipase C activity [GO:0007202]; aging [GO:0007568]; axon guidance [GO:0007411]; axonogenesis involved in innervation [GO:0060385]; B cell differentiation [GO:0030183]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to nicotine [GO:0071316]; circadian rhythm [GO:0007623]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; developmental programmed cell death [GO:0010623]; learning or memory [GO:0007611]; mechanoreceptor differentiation [GO:0042490]; negative regulation of cell proliferation [GO:0008285]; negative regulation of neuron apoptotic process [GO:0043524]; neurotrophin TRK receptor signaling pathway [GO:0048011]; olfactory nerve development [GO:0021553]; peptidyl-tyrosine phosphorylation [GO:0018108]; phosphatidylinositol-mediated signaling [GO:0048015]; positive regulation of angiogenesis [GO:0045766]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of programmed cell death [GO:0043068]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; Ras protein signal transduction [GO:0007265]; response to activity [GO:0014823]; response to axon injury [GO:0048678]; response to drug [GO:0042493]; response to electrical stimulus [GO:0051602]; response to ethanol [GO:0045471]; response to hydrostatic pressure [GO:0051599]; response to nutrient levels [GO:0031667]; response to radiation [GO:0009314]; Sertoli cell development [GO:0060009]; small GTPase mediated signal transduction [GO:0007264]; sympathetic nervous system development [GO:0048485]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]ATP binding [GO:0005524]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor activity [GO:0010465]; neurotrophin binding [GO:0043121]; protein homodimeri< zation activity [GO:0042803]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]axon [GO:0030424]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; integral component of plasma membrane [GO:0005887]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein complex [GO:0043234]; receptor complex [GO:0043235]FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.; FUNCTION: Isoform TrkA-III is resistant to NGF, constitutively activates AKT1 and NF-kappa-B and is unable to activate the Ras-MAPK signaling cascade. Antagonizes the anti-proliferative NGF-NTRK1 signaling that promotes neuronal precursors differentiation. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed.Q15326ZMY11-Zinc finger MYND domain-containing protein 11bSUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with chromatin and mitotic chromosomes.cell cycle [GO:0007049]; cell proliferation [GO:0008283]; chromatin modification [GO:0016568]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of JNK cascade [GO:0046329]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription elongation from RNA polymerase II promoter [GO:0034243]; transcription, DNA-templated [GO:0006351]; viral process [GO:0016032]DNA binding [GO:0003677]; methylated histone binding [GO:0035064]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]5FUNCTION: Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage. Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth. {ECO:0000250|UniProtKB:Q8R5C8, ECO:0000269|PubMed:10734313, ECO:0000269|PubMed:16565076}.Q01804OTUD4OTU domain-containing protein 40protein K48-linked deubiquitination [GO:0071108]Spoly(A) RNA binding [GO:0044822]; ubiquitin-specific protease activity [GO:0004843]|FUNCTION: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-48'-linked polyubiquitin. {ECO:0000269|PubMed:23827681}.P49754VPS416Vacuolar protein sorting-associated protein 41 homologvSUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:25445562}. Late endosome {ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:23322049}. Lysosome {ECO:0000269|PubMed:23167963}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23322049}. Early endosome {ECO:0000269|PubMed:21411634}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21411634}.5endosomal vesicle fusion [GO:0034058]; endosome to lysosome transport [GO:0008333]; Golgi vesicle transport [GO:0048193]; late endosome to lysosome transport [GO:1902774]; protein targeting to vacuole [GO:0006623]; regulation of SNARE complex assembly [GO:0035542]; vacuole fusion, non-autophagic [GO:0042144]:GTPase binding [GO:0051020]; zinc ion binding [GO:0008270]vclathrin-coated vesicle [GO:0030136]; CORVET complex [GO:0033263]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; Golgi-associated vesicle [GO:0005798]; HOPS complex [GO:0030897]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]yFUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a core component of the putative HOPS endosomal tethering complexe is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (PubMed:23351085). Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes implicated in degradation of endocytosed cargo (PubMed:9159129, PubMed:23167963, PubMed:25445562, PubMed:25908847). Required for fusion of autophagosomes with lysosomes (PubMed:25783203). May link the HOPS complex to endosomal Rab7 via its association with RILP and to lysosomal membranes via its association with ARL8B, suggesting that these interactions may bring the compartments to close proximity for fusion (PubMed:25445562, PubMed:25908847). Involved in the direct trans-Golgi network to late endosomes transport of lysosomal membrane proteins independently of HOPS (PubMed:23322049). Involved in sorting to the regulated secretory pathway presumably implicating the AP-3 adaptor complex (By similarity). May play a role in HOPS-independent function in the regulated secretory pathway (PubMed:24210660). {ECO:0000250|UniProtKB:D3ZVH6, ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:23322049, ECO:0000269|PubMed:25445562, ECO:0000269|PubMed:25783203, ECO:0000269|PubMed:25908847, ECO:0000269|PubMed:9159129, ECO:0000305|PubMed:23167963, ECO:0000305|PubMed:23351085, ECO:0000305|PubMed:24210660, ECO:0000305|PubMed:25445562}.P14923PLAKJunction plakoglobincSUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:22781308}. Cell junction, desmosome {ECO:0000269|PubMed:22781308}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22781308}. Membrane {ECO:0000269|PubMed:22781308}; Peripheral membrane protein {ECO:0000269|PubMed:22781308}. Note=Cytoplasmic in a soluble and membrane-associated form.adherens junction assembly [GO:0034333]; adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell junction organization [GO:0045216]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; cellular response to indole-3-methanol [GO:0071681]; cytoskeletal anchoring at plasma membrane [GO:0007016]; desmosome assembly [GO:0002159]; detection of mechanical stimulus [GO:0050982]; endothelial cell-cell adhesion [GO:0071603]; establishment of protein localization to plasma membrane [GO:0090002]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; regulation of cell fate specification [GO:0042659]; regulation of cell proliferati< on [GO:0042127]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell action potential [GO:0098911]; single organismal cell-cell adhesion [GO:0016337]; skin development [GO:0043588]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; cell adhesion molecule binding [GO:0050839]; cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication [GO:0086083]; protein homodimerization activity [GO:0042803]; protein phosphatase binding [GO:0019903]; signal transducer activity [GO:0004871]; structural constituent of cell wall [GO:0005199]; structural molecule activity [GO:0005198]; transcription coactivator activity [GO:0003713]3catenin complex [GO:0016342]; cell-cell adherens junction [GO:0005913]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; gamma-catenin-TCF7L2 complex [GO:0071665]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-DNA complex [GO:0032993]; Z disc [GO:0030018]; zonula adherens [GO:0005915]FUNCTION: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). {ECO:0000250}.Q96SB4SRPK1SRSF protein kinase 1SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Nucleus matrix. Microsome. Note=Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KAT5/TIP60 inhibits its nuclear translocation.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus matrix. Microsome. Note=Mainly localized in the microsomal fraction and the cytoplasm, and to a lesser extent in the nuclear matrix.chromosome segregation [GO:0007059]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; mRNA processing [GO:0006397]; negative regulation of viral genome replication [GO:0045071]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of mRNA processing [GO:0050684]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing [GO:0008380]; sperm chromatin condensation [GO:0035092]; viral process [GO:0016032]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; poly(A) RNA binding [GO:0044822]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. {ECO:0000269|PubMed:10049757, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757, ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240, ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675, ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298, ECO:0000269|PubMed:9237760}.Q05C16LRC63)Leucine-rich repeat-containing protein 63Q5XPI4RN123"E3 ubiquitin-protein ligase RNF123>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15531880}.FUNCTION: Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:16227581}.Q8N6R0MET13!Methyltransferase-like protein 13Q6ZVK8NUD188-oxo-dGDP phosphatase NUDT18%dADP catabolic process [GO:0046057]; dGDP catabolic process [GO:0046067]; GDP catabolic process [GO:0046712]; nucleobase-containing small molecule catabolic process [GO:0034656]; nucleobase-containing small molecule metabolic process [GO:0055086]; small molecule metabolic process [GO:0044281]8-hydroxy-dADP phosphatase activity [GO:0044717]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; magnesium ion binding [GO:0000287]FUNCTION: Mediates the hydrolyzis of oxidized nucleoside diphosphate derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies. Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal hydrolyzis activity against 8-oxo-dGTP, 8-oxo-GTP, dGTP, GTP, dGDP and GDP. Probably removes oxidized guanine nucleotides from both the DNA and RNA precursor pools. {ECO:0000269|PubMed:22556419}.P293723MGDNA-3-methyladenine glycosylaseSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23290262}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:23290262}. Nucleus {ECO:0000269|PubMed:23290262}.base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; depurination [GO:0045007]; DNA dealkylation involved i< n DNA repair [GO:0006307]; DNA repair [GO:0006281]/alkylbase DNA N-glycosylase activity [GO:0003905]; damaged DNA binding [GO:0003684]; DNA-3-methyladenine glycosylase activity [GO:0008725]; DNA-3-methylguanine glycosylase activity [GO:0052822]; DNA-7-methyladenine glycosylase activity [GO:0052821]; DNA-7-methylguanine glycosylase activity [GO:0043916]=mitochondrial nucleoid [GO:0042645]; nucleoplasm [GO:0005654]FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.O95239KIF4A#Chromosome-associated kinesin KIF4ASUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton, spindle. Midbody. Chromosome. Note=Not present in the nucleolus. In early mitosis, associated with the mitotic spindle, in anaphase, localized to the spindle midzone and, in telophase and cytokinesis, to the midbody. In late cytokinesis, found in the center of the midbody. Associated with chromosomes at all stages of mitosis.hanterograde axon cargo transport [GO:0008089]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; blood coagulation [GO:0007596]; microtubule-based movement [GO:0007018]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]; organelle organization [GO:0006996]yATPase activity [GO:0016887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; microtubule motor activity [GO:0003777]chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; midbody [GO:0030496]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; spindle microtubule [GO:0005876]FUNCTION: Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105}.Q32M45ANO4 Anoctamin-4SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:22946059}. Note=Shows an intracellular localization. {ECO:0000250|UniProtKB:Q8C5H1}.Ycalcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; calcium activated phosphatidylserine scrambling [GO:0061589]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; ion transmembrane transport [GO:0034220]; transmembrane transport [GO:0055085]uintracellular calcium activated chloride channel activity [GO:0005229]; phospholipid scramblase activity [GO:0017128]FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity. {ECO:0000250|UniProtKB:Q8C5H1}.Q9Y333LSM2(U6 snRNA-associated Sm-like protein LSm2.exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; RNA splicing [GO:0008380]`poly(A) RNA binding [GO:0044822]; Ral GTPase binding [GO:0017160]; U6 snRNA binding [GO:0017070]Ycatalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]jFUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing.Q99650OSMR+Oncostatin-M-specific receptor subunit betaoncostatin-M-mediated signaling pathway [GO:0038165]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of cell proliferation [GO:0008284]; response to cytokine [GO:0034097]Ogrowth factor binding [GO:0019838]; oncostatin-M receptor activity [GO:0004924]Oapical plasma membrane [GO:0016324]; oncostatin-M receptor complex [GO:0005900]FUNCTION: Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events. {ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:8999038}.P30876RPB2+DNA-directed RNA polymerase II subunit RPB27-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; mRNA splicing, via spliceosome [GO:0000398]; nucleotide-excision repair [GO:0006289]; piRNA metabolic process [GO:0034587]; positive regulation of viral transcription [GO:0050434]; RNA splicing [GO:0008380]; somatic stem cell maintenance [GO:0035019]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]; transcription initiation from RNA polymerase II promoter [GO:0006367]; viral process [GO:0016032]chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; poly(A) RNA binding [GO:0044822]; ribonucleoside binding [GO:0032549]DNA-directed RNA polymerase II, core complex [GO:0005665]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity). {ECO:0000250}.P07093GDNGlia-derived nexinblood coagulation [GO:0007596]; cerebellar granular layer morphogenesis [GO:0021683]; dense core granule biogenesis [GO:0061110]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; embryo implantation [GO:0007566]; innervation [GO:0060384]; long-term synaptic potentiation [GO:0060291]; mating plug formation [GO:0042628]; negative regulation of blood coagulation [GO:0030195]; negative regulation of cell growth [GO:0030308]; negative regulation of cell proliferation [GO:0008285]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of phosphatidylinositol 3-kinase signaling [GO:0014067]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of protein processing [GO:0010955]; negative regulation of proteolysis [GO:0045861]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of sodium ion transport [GO:0010766]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of neuron projection development [GO:0010976]; regulation of cell migration [GO:0030334]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of timing of cell differentiation [GO:0048505]; response to radiation [GO:0009314]; secretory granule organization [GO:0033363]; seminal vesicle epithelium development [GO:0061108]glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; receptor binding [GO:0005102]; serine-type endopeptidase inhibitor activity [GO:0004867]Qcytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; extrinsic component of external side of plasma membrane [GO:0031232]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; platelet alpha granule [< GO:0031091]FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.P25208NFYB+Nuclear transcription factor Y subunit betapositive regulation of transcription, DNA-templated [GO:0045893]; regulation of transcription, DNA-templated [GO:0006355]; small molecule metabolic process [GO:0044281]; transcription, DNA-templated [GO:0006351]DNA binding [GO:0003677]; repressing transcription factor binding [GO:0070491]; sequence-specific DNA binding [GO:0043565]; sequence-specific DNA binding transcription factor activity [GO:0003700]O94986CE152Centrosomal protein of 152 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20598275, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973, ECO:0000269|PubMed:21983783}. Note=Colocalizes with CEP63 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles. Localizes to the deuterosome.cell projection organization [GO:0030030]; centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; de novo centriole assembly [GO:0098535]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]acentrosome [GO:0005813]; cytosol [GO:0005829]; deuterosome [GO:0098536]; nucleoplasm [GO:0005654]FUNCTION: Necessary for centrosome duplication. Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation. Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Overexpression of CEP152 can drive amplification of centrioles. {ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973}.P51003PAPOAPoly(A) polymerase alphaSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic.zgene expression [GO:0010467]; mRNA 3'-end processing [GO:0031124]; mRNA polyadenylation [GO:0006378]; mRNA splicing, via spliceosome [GO:0000398]; regulation of mRNA 3'-end processing [GO:0031440]; RNA polyadenylation [GO:0043631]; RNA splicing [GO:0008380]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; polynucleotide adenylyltransferase activity [GO:0004652]; RNA binding [GO:0003723]7FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus. {ECO:0000269|PubMed:19224921}.Q96JK2DCAF5"DDB1- and CUL4-associated factor 5NCul4-RING E3 ubiquitin ligase complex [GO:0080008]; mitochondrion [GO:0005739]Q5TBB1RNH2BRibonuclease H2 subunit Bein utero embryonic development [GO:0001701]; negative regulation of gene expression [GO:0010629]; positive regulation of fibroblast proliferation [GO:0048146]; regulation of DNA damage checkpoint [GO:2000001]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; ribonucleotide metabolic process [GO:0009259]; RNA catabolic process [GO:0006401]1RNA-DNA hybrid ribonuclease activity [GO:0004523]Tnucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonuclease H2 complex [GO:0032299]Q5T0N5FBP1LFormin-binding protein 1-likeSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16757518}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.Vautophagy [GO:0006914]; cilium assembly [GO:0042384]; clathrin-mediated endocytosis [GO:0072583]; membrane budding [GO:0006900]; membrane invagination [GO:0010324]; membrane tubulation [GO:0097320]; positive regulation of filopodium assembly [GO:0051491]; vesicle organization [GO:0016050]; vesicle transport along actin filament [GO:0030050]cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]FUNCTION: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens. {ECO:0000269|PubMed:15260990, ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:19342671}.P49716CEBPD$CCAAT/enhancer-binding protein deltaRNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]FUNCTION: C/EBP is a DNA-binding protein that recognizes two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses, may play an important role in the regulation of the several genes associated with activation and/or differentiation of macrophages.Q9UBE0SAE1 SUMO-activating enzyme subunit 1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11481243}.[cellular protein metabolic process [GO:0044267]; positive regulation of catalytic activity [GO:0043085]; positive regulation of protein targeting to mitochondrion [GO:1903955]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein ubiquitination [GO:0016567]; regulation of mitotic cell cycle [GO:0007346]ATP-dependent protein binding [GO:0043008]; enzyme activator activity [GO:0008047]; protein C-terminus binding [GO:0008022]; protein heterodimerization activity [GO:0046982]; ubiquitin activating enzyme activity [GO:0004839]cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SUMO activating enzyme complex [GO:0031510]FUNCTION: The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. {ECO:0000269|PubMed:10187858, ECO:0000269|PubMed:10217437, ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:11481243, ECO:0000269|PubMed:15660128, ECO:0000269|PubMed:20164921, ECO:0000269|PubMed:9920803}.P08174DAF$Complement decay-accelerating factorSUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: Isoform 5: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: Isoform 6: Cell membrane {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.; SUBCELLULAR LOCATION: Isoform 7: Cell membrane {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.CD4-positive, alpha-beta T cell cytokine production [GO:0035743]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of co< mplement activation [GO:0045916]; positive regulation of CD4-positive, alpha-beta T cell activation [GO:2000516]; positive regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000563]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of complement activation [GO:0030449]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; respiratory burst [GO:0045730]; viral entry into host cell [GO:0046718]@lipid binding [GO:0008289]; virus receptor activity [GO:0001618]anchored component of membrane [GO:0031225]; cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; integral component of plasma membrane [GO:0005887]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. {ECO:0000269|PubMed:7525274}.O15078CE290Centrosomal protein of 290 kDatSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Nucleus. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Connecting cilium of photoreceptor cells, base of cilium in kidney intramedullary collecting duct cells. Localizes at the transition zone, a region between the basal body and the ciliary axoneme (By similarity). Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock. {ECO:0000250}.cilium assembly [GO:0042384]; cilium morphogenesis [GO:0060271]; establishment or maintenance of cell polarity [GO:0007163]; eye photoreceptor cell development [GO:0042462]; G2/M transition of mitotic cell cycle [GO:0000086]; hindbrain development [GO:0030902]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; otic vesicle formation [GO:0030916]; photoreceptor cell maintenance [GO:0045494]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of transcription, DNA-templated [GO:0045893]; pronephros development [GO:0048793]; protein transport [GO:0015031]; regulation of cAMP metabolic process [GO:0030814]; regulation of establishment of protein localization [GO:0070201]; retina development in camera-type eye [GO:0060041]Pcentriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; photoreceptor connecting cilium [GO:0032391]; photoreceptor outer segment [GO:0001750]; protein complex [GO:0043234]; TCTN-B9D complex [GO:0036038]FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Activates ATF4-mediated transcription. Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes. {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:16682973}.Q99590SCAFBProtein SCAF11;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9447963}.mRNA processing [GO:0006397]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]yFUNCTION: Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly. {ECO:0000269|PubMed:9447963}.P53999TCP4;Activated RNA polymerase II transcriptional coactivator p15wregulation of transcription from RNA polymerase II promoter [GO:0006357]; SMAD protein signal transduction [GO:0060395]poly(A) RNA binding [GO:0044822]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; single-stranded DNA binding [GO:0003697]; transcription coactivator activity [GO:0003713]{extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; nucleus [GO:0005634]; transcription factor complex [GO:0005667]"FUNCTION: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). {ECO:0000269|PubMed:16605275, ECO:0000269|PubMed:16689930, ECO:0000269|PubMed:7628453, ECO:0000269|PubMed:8062391, ECO:0000269|PubMed:8062392, ECO:0000269|PubMed:9360603, ECO:0000269|PubMed:9482861}.Q8IUR5TMTC11Transmembrane and TPR repeat-containing protein 1O60331PI51C6Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaSUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junction, focal adhesion. Cell junction, adherens junction. Cell projection, ruffle membrane. Cell projection, phagocytic cup. Cell projection, uropodium. Note=Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.Sactin cytoskeleton organization [GO:0030036]; adherens junction assembly [GO:0034333]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; cytoskeletal anchoring at plasma membrane [GO:0007016]; neutrophil chemotaxis [GO:0030593]; phagocytosis [GO:0006909]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid metabolic process [GO:0006644]; platelet aggregation [GO:0070527]; single organismal cell-cell adhesion [GO:0016337]; small molecule metabolic process [GO:0044281]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle exocytosis [GO:0016079]cytosol [GO:0005829]; endomembrane system [GO:0012505]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; phagocytic cup [GO:0001891]; ruffle membrane [GO:0032587]; uropod [GO:0001931]FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion.< Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth. {ECO:0000269|PubMed:12422219, ECO:0000269|PubMed:12847086, ECO:0000269|PubMed:17261850, ECO:0000269|PubMed:17635937}.Q6UWZ7F175ABRCA1-A complex subunit AbraxasSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).chromatin modification [GO:0016568]; double-strand break repair [GO:0006302]; G2 DNA damage checkpoint [GO:0031572]; positive regulation of DNA repair [GO:0045739]; response to ionizing radiation [GO:0010212]FUNCTION: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:18077395, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:22357538}.Q14767LTBP28Latent-transforming growth factor beta-binding protein 2SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers. {ECO:0000250}.protein secretion [GO:0009306]; protein targeting [GO:0006605]; transforming growth factor beta receptor signaling pathway [GO:0007179]cell [GO:0005623]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intracellular [GO:0005622]; proteinaceous extracellular matrix [GO:0005578]kFUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly.Q2TAC2CCD57(Coiled-coil domain-containing protein 57Q86US8EST1A Telomerase-binding protein EST1ASUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, telomere {ECO:0000305}. Cytoplasm, cytosol. Note=Particularly enriched in the nucleolus.(gene expression [GO:0010467]; mRNA export from nucleus [GO:0006406]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of dephosphorylation [GO:0035303]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; telomere maintenance [GO:0000723]jendoribonuclease activity [GO:0004521]; metal ion binding [GO:0046872]; telomeric DNA binding [GO:0042162]chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]qFUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER).; FUNCTION: Plays a role in nonsense-mediated mRNA decay. Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA.Q8TDL5BPIB1%BPI fold-containing family B member 1yinnate immune response in mucosa [GO:0002227]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]FUNCTION: May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS. {ECO:0000269|PubMed:21900486}.Q96GX9MTNB*Methylthioribulose-1-phosphate dehydratase|SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:23285211}.apoptotic process [GO:0006915]; cellular nitrogen compound metabolic process [GO:0034641]; L-methionine biosynthetic process from methylthioadenosine [GO:0019509]; L-methionine biosynthetic process from S-adenosylmethionine [GO:0019284]; negative regulation of apoptotic process [GO:0043066]; polyamine metabolic process [GO:0006595]; regulation of ERK1 and ERK2 cascade [GO:0070372]; small molecule metabolic process [GO:0044281]; sulfur amino acid metabolic process [GO:0000096]identical protein binding [GO:0042802]; methylthioribulose 1-phosphate dehydratase activity [GO:0046570]; zinc ion binding [GO:0008270]1FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death. {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:22837397, ECO:0000269|PubMed:23285211}.Q96PZ2F111AProtein FAM111ASUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly localizes to nucleus: colocalizes with PCNA on replication sites. {ECO:0000269|PubMed:24561620}.defense response to virus [GO:0051607]; DNA replication [GO:0006260]; negative regulation of viral genome replication [GO:0045071]; viral process [GO:0016032]mFUNCTION: Chromatin-associated protein required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis (PubMed:24561620). May directly function at replication forks, explaining why Simian virus 40 (SV40) interacts with FAM111A to overcome host range restriction (PubMed:23093934). {ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:24561620}.Q96S38KS6C1#Ribosomal protein S6 kinase delta-1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12077123}. Membrane {ECO:0000269|PubMed:12077123}. Note=Also found in some small dot-like or ring-shaped early endosome structures.zATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]; protein serine/threonine kinase activity [GO:0004674]cytoplasm [GO:0005737]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]iFUNCTION: May be involved in transmitting sphingosine-1 phosphate (SPP)-mediated signaling into the cell.Q96CM4NXNL1Nucleoredoxin-like protein 1+photoreceptor cell maintenance [GO:0045494]?mitochondrion [GO:0005739]; nuclear outer membrane [GO:0005640]FUNCTION: May play a role in cone cell viability, slowing down cone degeneration, does not seem to play a role in degenerating rods. {ECO:0000250}.Q99575POP1(Ribonucleases P/MRP protein subunit POP1RNA phosphodiester bond hydrolysis [GO:0090501]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; tRNA 5'-leader removal [GO:0001682]; tRNA catabolic process [GO:0016078]; tRNA processing [GO:0008033]npoly(A) RNA binding [GO:0044822]; ribonuclease MRP activity [GO:0000171]; ribonuclease P activity [GO:0004526]vextracellular space [GO:0005615]; nucleolar ribonuclease P complex [GO:0005655]; ribonuclease MRP complex [GO:0000172]FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP.Q96C86DCPSm7GpppX diphosphataseSUBCELLULAR LO< CATION: Cytoplasm. Nucleus. Note=Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.cellular response to menadione [GO:0036245]; deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; mRNA cis splicing, via spliceosome [GO:0045292]; negative regulation of programmed cell death [GO:0043069]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]_m7G(5')pppN diphosphatase activity [GO:0050072]; RNA 7-methylguanosine cap binding [GO:0000340]FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death. {ECO:0000269|PubMed:11747811, ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:14523240, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:15769464, ECO:0000269|PubMed:16140270, ECO:0000269|PubMed:18426921, ECO:0000269|PubMed:22985415}.O94964SOGA1 Protein SOGA1SUBCELLULAR LOCATION: C-terminal 80 kDa form: Secreted {ECO:0000250}. Note=Secreted in primary hepatocyte-conditioned media. {ECO:0000250}.insulin receptor signaling pathway [GO:0008286]; negative regulation of gluconeogenesis [GO:0045721]; regulation of autophagy [GO:0010506]FUNCTION: Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner. {ECO:0000250}.Q9Y2V7COG6,Conserved oligomeric Golgi complex subunit 6hSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.oglycosylation [GO:0070085]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]Q9ULJ7ANR50+Ankyrin repeat domain-containing protein 50^protein transport [GO:0015031]; retrograde transport, endosome to plasma membrane [GO:1990126]FUNCTION: Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1 (PubMed:25278552).Q6ICB4SESQ2Sesquipedalian-2SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, clathrin-coated vesicle. Note=Also found on macropinosomes. Not detected in late endosomes, nor in lysosomes.yendosome organization [GO:0007032]; receptor recycling [GO:0001881]; retrograde transport, endosome to Golgi [GO:0042147]clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]FUNCTION: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. {ECO:0000269|PubMed:21233288}.Q06033ITIH3,Inter-alpha-trypsin inhibitor heavy chain H3Eextracellular exosome [GO:0070062]; extracellular region [GO:0005576]A8MVW0F1712Protein FAM171A2Q9H0J9PAR12Poly [ADP-ribose] polymerase 12P19387RPB3+DNA-directed RNA polymerase II subunit RPB3cytoplasm [GO:0005737]; DNA-directed RNA polymerase II, core complex [GO:0005665]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]*FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity). {ECO:0000250}.O14777NDC80!Kinetochore protein NDC80 homologattachment of mitotic spindle microtubules to kinetochore [GO:0051315]; attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; establishment of mitotic spindle orientation [GO:0000132]; mitotic cell cycle [GO:0000278]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle organization [GO:0007052]; small GTPase mediated signal transduction [GO:0007264][identical protein binding [GO:0042802]; structural constituent of cytoskeleton [GO:0005200]Gchromosome, centromeric region [GO:0000775]; condensed chromosome kinetochore [GO:0000777]; condensed nuclear chromosome kinetochore [GO:0000778]; condensed nuclear chromosome outer kinetochore [GO:0000942]; cytosol [GO:0005829]; kinetochore [GO:0000776]; membrane [GO:0016020]; Ndc80 complex [GO:0031262]; nucleus [GO:0005634]+FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. {ECO:0000269|PubMed:12351790, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:14699129, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:9315664}.Q6NW34CC017Uncharacterized protein C3orf17wnegative regulation of neuron differentiation [GO:0045665]; positive regulation of Notch signaling pathway [GO:0045747]Q8WXX5DNJC9!DnaJ homolog subfamily C member 9social behavior [GO:0035176]P34931HS71L Heat shock 70 kDa protein 1-like binding of sperm to zona pellucida [GO:0007339]; cellular response to heat [GO:0034605]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein refolding [GO:0042026]; regulation of cellular response to heat [GO:1900034]; response to unfolded protein [GO:0006986]blood microparticle [GO:0072562]; cell body [GO:0044297]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; zona pellucida receptor complex [GO:0002199]FUNCTION: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). Positive regulator of PARK2 translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.Q17RY6LY6KLymphocyte antigen 6KSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18089789}. Cytoplasm {ECO:0000269|PubMed:18089789}. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.anchored component of membrane [GO:0031225]; cytoplasm [GO:0005737]; ex< tracellular region [GO:0005576]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]HFUNCTION: May play a role in cell growth. {ECO:0000269|PubMed:18089789}.Q8WV44TRI41"E3 ubiquitin-protein ligase TRIM41eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16022281}. Nucleus {ECO:0000269|PubMed:16022281}.FUNCTION: Functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. {ECO:0000269|PubMed:17893151}.Q96EP5DAZP1DAZ-associated protein 1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22001406}. Nucleus {ECO:0000269|PubMed:22001406}. Note=Predominantly cytoplasmic (By similarity). Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm (By similarity). {ECO:0000250}.cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; maternal placenta development [GO:0001893]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; spermatogenesis [GO:0007283]nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; RNA stem-loop binding [GO:0035613]LFUNCTION: RNA-binding protein, which may be required during spermatogenesis.O00165HAX1HCLS1-associated protein X-1SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum. Nucleus membrane. Cytoplasmic vesicle {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}.;cellular response to cytokine stimulus [GO:0071345]; negative regulation of apoptotic process [GO:0043066]; positive regulation of actin cytoskeleton reorganization [GO:2000251]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein kinase B signaling [GO:0051897]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of actin filament polymerization [GO:0030833]; regulation of apoptotic process [GO:0042981]; regulation of mitochondrion degradation [GO:1903146]; regulation of protein targeting to mitochondrion [GO:1903214]Kinterleukin-1 binding [GO:0019966]; protein N-terminus binding [GO:0047485]actin cytoskeleton [GO:0015629]; cytoplasmic membrane-bounded vesicle [GO:0016023]; endoplasmic reticulum [GO:0005783]; lamellipodium [GO:0030027]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; sarcoplasmic reticulum [GO:0016529]; transcription factor complex [GO:0005667]FUNCTION: Promotes cell survival. Potentiates GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. May regulate intracellular calcium pools. {ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965, ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:18319618, ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}.P63027VAMP2%Vesicle-associated membrane protein 2SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell junction, synapse, synaptosome. Cell membrane {ECO:0000250|UniProtKB:P63045}. Note=Neuronal synaptic vesicles.ocalcium ion-dependent exocytosis [GO:0017156]; cellular protein metabolic process [GO:0044267]; cellular response to insulin stimulus [GO:0032869]; energy reserve metabolic process [GO:0006112]; eosinophil degranulation [GO:0043308]; exocytosis [GO:0006887]; glutamate secretion [GO:0014047]; Golgi to plasma membrane protein transport [GO:0043001]; long-term synaptic potentiation [GO:0060291]; membrane fusion [GO:0061025]; membrane organization [GO:0061024]; neurotransmitter secretion [GO:0007269]; positive regulation of intracellular protein transport [GO:0090316]; post-Golgi vesicle-mediated transport [GO:0006892]; protein complex assembly [GO:0006461]; protein transport [GO:0015031]; regulation of delayed rectifier potassium channel activity [GO:1902259]; regulation of exocytosis [GO:0017157]; regulation of insulin secretion [GO:0050796]; regulation of vesicle-mediated transport [GO:0060627]; response to glucose [GO:0009749]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; synaptic vesicle exocytosis [GO:0016079]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]calcium-dependent protein binding [GO:0048306]; calmodulin binding [GO:0005516]; phospholipid binding [GO:0005543]; protein self-association [GO:0043621]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin-1 binding [GO:0017075]; syntaxin binding [GO:0019905]bcell junction [GO:0030054]; clathrin-coated vesicle [GO:0030136]; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202]; clathrin-sculpted glutamate transport vesicle membrane [GO:0060203]; clathrin-sculpted monoamine transport vesicle membrane [GO:0070083]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuron projection terminus [GO:0044306]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; secretory granule membrane [GO:0030667]; SNARE complex [GO:0031201]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; synaptobrevin 2-SNAP-25-syntaxin-1a complex [GO:0070044]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex [GO:0070033]; trans-Golgi network [GO:0005802]; zymogen granule membrane [GO:0042589]FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. {ECO:0000250|UniProtKB:P63045}.Q96NW4ANR27+Ankyrin repeat domain-containing protein 27SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:16525121, ECO:0000269|PubMed:24856514}. Late endosome {ECO:0000269|PubMed:23104059}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23104059}. Lysosome {ECO:0000269|PubMed:23104059}. Cell membrane {ECO:0000269|PubMed:23104059}. Melanosome {ECO:0000250|UniProtKB:Q3UMR0}. Note=Colocalizes with VAMP7 in transport vesicles in the shaft of hippoocampal neurons (By similarity). {ECO:0000250|UniProtKB:Q3UMR0}.early endosome to late endosome transport [GO:0045022]; endosome to melanosome transport [GO:0035646]; negative regulation of SNARE complex assembly [GO:0035544]; neuron projection morphogenesis [GO:0048812]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of GTPase activity [GO:0043547]; protein transport [GO:0015031]; retrograde transport, endosome to plasma membrane [GO:1990126]GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; Rab GTPase binding [GO:0017137]>cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; late endosome [GO:0005770]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]; tubular endosome [GO:0097422]8FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and regulate endosome dynamics (PubMed:16525121, PubMed:18477474). May regulate the participation of VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed, fusogenically inactive conformat< ion (PubMed:23104059). Involved in peripheral melanosomal distribution of TYRP1 in melanocytes; the function, which probably is implicating vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7 (By similarity). Involved in the regulation of neurite growth; the function seems to require its GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38 (By similarity). Proposed to be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell surface; the function seems to implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and MACF1 (PubMed:22705394). Required for the colocalization of VAMP7 and Rab21, probably on TGN sites (PubMed:19745841). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with VPS29 (PubMed:24856514). {ECO:0000250|UniProtKB:Q3UMR0, ECO:0000269|PubMed:23104059, ECO:0000269|PubMed:24856514, ECO:0000305|PubMed:16525121, ECO:0000305|PubMed:18477474, ECO:0000305|PubMed:22705394}.Q562R1ACTBLBeta-actin-like protein 2wcytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. {ECO:0000250}.Q6ZU35K1211 Uncharacterized protein KIAA1211Q9UMR5PPT2Lysosomal thioesterase PPT2<SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9341199}.+macromolecule depalmitoylation [GO:0098734]palmitoyl-(protein) hydrolase activity [GO:0008474]; palmitoyl hydrolase activity [GO:0098599]; thiolester hydrolase activity [GO:0016790]FUNCTION: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins. {ECO:0000269|PubMed:10417332, ECO:0000269|PubMed:12855696, ECO:0000269|PubMed:9341199}.P14209CD99 CD99 antigencytoplasm [GO:0005737]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; plasma membrane [GO:0005886]^FUNCTION: Involved in T-cell adhesion processes and in spontaneous rosette formation with erythrocytes. Plays a role in a late step of leukocyte extravasation helping leukocytes to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Involved in T-cell adhesion processes (By similarity). {ECO:0000250}.Q13873BMPR2*Bone morphogenetic protein receptor type-2gSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25187962}; Single-pass type I membrane protein.activin receptor signaling pathway [GO:0032924]; anterior/posterior pattern specification [GO:0009952]; artery development [GO:0060840]; blood vessel remodeling [GO:0001974]; BMP signaling pathway [GO:0030509]; brain development [GO:0007420]; cellular response to BMP stimulus [GO:0071773]; cellular response to starvation [GO:0009267]; chondrocyte development [GO:0002063]; endochondral bone morphogenesis [GO:0060350]; endothelial cell apoptotic process [GO:0072577]; endothelial cell proliferation [GO:0001935]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymphangiogenesis [GO:0001946]; lymphatic endothelial cell differentiation [GO:0060836]; maternal placenta development [GO:0001893]; mesoderm formation [GO:0001707]; negative regulation of cell growth [GO:0030308]; negative regulation of chondrocyte proliferation [GO:1902731]; negative regulation of DNA biosynthetic process [GO:2000279]; negative regulation of systemic arterial blood pressure [GO:0003085]; negative regulation of vasoconstriction [GO:0045906]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cartilage development [GO:0061036]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of pathway-restricted SMAD protein phosphorylation [GO:0010862]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; proteoglycan biosynthetic process [GO:0030166]; regulation of cell proliferation [GO:0042127]; regulation of lung blood pressure [GO:0014916]; retina vasculature development in camera-type eye [GO:0061298]; transcription from RNA polymerase II promoter [GO:0006366]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; venous blood vessel development [GO:0060841]activin receptor activity, type II [GO:0016362]; ATP binding [GO:0005524]; BMP binding [GO:0036122]; metal ion binding [GO:0046872]; receptor signaling protein serine/threonine kinase activity [GO:0004702]apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; caveola [GO:0005901]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular space [GO:0005615]; integral component of plasma membrane [GO:0005887]; neuronal cell body [GO:0043025]; neuronal postsynaptic density [GO:0097481]; plasma membrane [GO:0005886]; spanning component of plasma membrane [GO:0044214]FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.Q8N9N7LRC57)Leucine-rich repeat-containing protein 57P81605DCD Dermcidindefense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of other organism [GO:0031640]Apeptidase activity [GO:0008233]; poly(A) RNA binding [GO:0044822]FUNCTION: DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity.; FUNCTION: Survival-promoting peptide promotes survival of neurons and displays phosphatase activity. It may bind IgG.P36969GPX4@Phospholipid hydroperoxide glutathione peroxidase, mitochondrialyarachidonic acid metabolic process [GO:0019369]; chromatin organization [GO:0006325]; lipoxygenase pathway [GO:0019372]; multicellular organismal development [GO:0007275]; oxidation-reduction process [GO:0055114]; phospholipid metabolic process [GO:0006644]; response to oxidative stress [GO:0006979]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]uglutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]ZFUNCTION: Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage (By similarity). {ECO:0000250}.Q9P003CNIH4Protein cornichon homolog 4SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:24405750}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:24405750}.ER to Golgi vesicle-mediated tr< ansport [GO:0006888]; intracellular signal transduction [GO:0035556]; protein transport [GO:0015031],CCR5 chemokine receptor binding [GO:0031730]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; integral component of membrane [GO:0016021]FUNCTION: Involved in G protein-coupled receptors (GPCRs) trafficking from the endoplasmic reticulum to the cell surface; it promotes the exit of GPCRs from the early secretory pathway, likely through interaction with the COPII machinery (PubMed:24405750). {ECO:0000269|PubMed:24405750}.Q9UIH9KLF15Krueppel-like factor 15YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982849, ECO:0000269|PubMed:17438289}.cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to peptide [GO:1901653]; glial cell differentiation [GO:0010001]; glomerular visceral epithelial cell differentiation [GO:0072112]; glucose transport [GO:0015758]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription from RNA polymerase II promoter [GO:0006366]metal ion binding [GO:0046872]; RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001077]; transcription regulatory region DNA binding [GO:0044212]FUNCTION: Transcriptional regulator that binds to the GA element of the CLCNKA promoter. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart (By similarity). Is a repressor of CTGF expression, involved in the control of cardiac fibrosis. It is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A and GATA4 (By similarity). Involved in podocyte differentiation (By similarity). Inhibits MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation. {ECO:0000250, ECO:0000269|PubMed:18586263, ECO:0000269|PubMed:20375365, ECO:0000269|PubMed:20566642, ECO:0000269|PubMed:23999430}.Q9Y6Y0NS1BP$Influenza virus NS1A-binding proteinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9696811}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9696811}. Nucleus, nucleoplasm {ECO:0000269|PubMed:9696811}. Note=Associated with actin filaments (By similarity). Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing. Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm. {ECO:0000250}.negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; response to virus [GO:0009615]; RNA splicing [GO:0008380]; transcription from RNA polymerase III promoter [GO:0006383]; viral process [GO:0016032]actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; spliceosomal complex [GO:0005681]; transcription factor complex [GO:0005667]2FUNCTION: Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines (By similarity). May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription. {ECO:0000250, ECO:0000269|PubMed:16582008}.O00418EF2K%Eukaryotic elongation factor 2 kinaseinsulin receptor signaling pathway [GO:0008286]; protein autophosphorylation [GO:0046777]; regulation of protein autophosphorylation [GO:0031952]; translational elongation [GO:0006414]ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; protein kinase activity [GO:0004672]; translation factor activity, RNA binding [GO:0008135]FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:9144159}.P32456GBP2.Interferon-induced guanylate-binding protein 2QSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Golgi apparatus membrane; Lipid-anchor.cytokine-mediated signaling pathway [GO:0019221]; immune response [GO:0006955]; interferon-gamma-mediated signaling pathway [GO:0060333]; type I interferon signaling pathway [GO:0060337]2FUNCTION: Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). {ECO:0000250}.P27658CO8A1Collagen alpha-1(VIII) chainangiogenesis [GO:0001525]; camera-type eye morphogenesis [GO:0048593]; cell adhesion [GO:0007155]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; epithelial cell proliferation [GO:0050673]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; positive regulation of cell-substrate adhesion [GO:0010811]collagen type VIII trimer [GO:0005591]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]]FUNCTION: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis. {ECO:0000269|PubMed:11708810}.; FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis. {ECO:0000269|PubMed:11708810}.Q75QN2INT8Integrator complex subunit 8P05455LALupus La proteinKhistone mRNA metabolic process [GO:0008334]; tRNA modification [GO:0006400]wmRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; tRNA binding [GO:0000049]FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. {ECO:0000269|PubMed:2470590, ECO:0000269|PubMed:3192525}.O75952CABYR:Calcium-binding tyrosine phosphorylation-regulated proteinSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Localized to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella.; SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.; SUBCELLULAR LOCATION: Isoform 5: Nucleus. Cytoplasm. Cell projection, cilium, flagellum. Note=According to PubMed:15752768, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic.Hepithelial cilium movement [GO:0003351]; sperm capacitation [GO:0048240]calcium ion binding< [GO:0005509]; enzyme binding [GO:0019899]; protein heterodimerization activity [GO:0046982]; SH3 domain binding [GO:0017124]cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; motile cilium [GO:0031514]; nucleolus [GO:0005730]; nucleus [GO:0005634]; sperm end piece [GO:0097229]; sperm fibrous sheath [GO:0035686]; sperm principal piece [GO:0097228]6FUNCTION: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.Q6PI48SYDM%Aspartate--tRNA ligase, mitochondrialgene expression [GO:0010467]; mitochondrial asparaginyl-tRNA aminoacylation [GO:0070145]; tRNA aminoacylation [GO:0043039]; tRNA aminoacylation for protein translation [GO:0006418]aspartate-tRNA(Asn) ligase activity [GO:0050560]; aspartate-tRNA ligase activity [GO:0004815]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]Q9UNE7CHIP E3 ubiquitin-protein ligase CHIPSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:23973223}. Nucleus {ECO:0000269|PubMed:23973223}. Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg). {ECO:0000269|PubMed:23973223}.cellular response to misfolded protein [GO:0071218]; DNA repair [GO:0006281]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; misfolded or incompletely synthesized protein catabolic process [GO:0006515]; negative regulation of protein binding [GO:0032091]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of chaperone-mediated protein complex assembly [GO:0090035]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein maturation [GO:0051604]; protein polyubiquitination [GO:0000209]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; regulation of glucocorticoid metabolic process [GO:0031943]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent SMAD protein catabolic process [GO:0030579]enzyme binding [GO:0019899]; G-protein coupled receptor binding [GO:0001664]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; kinase binding [GO:0019900]; ligase activity [GO:0016874]; misfolded protein binding [GO:0051787]; protein binding, bridging [GO:0030674]; protein homodimerization activity [GO:0042803]; SMAD binding [GO:0046332]; TPR domain binding [GO:0030911]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase activity involved in ERAD pathway [GO:1904264]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; ubiquitin-ubiquitin ligase activity [GO:0034450]\cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; nuclear inclusion body [GO:0042405]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ubiquitin conjugating enzyme complex [GO:0031371]; ubiquitin ligase complex [GO:0000151]FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). {ECO:0000269|PubMed:10330192, ECO:0000269|PubMed:11146632, ECO:0000269|PubMed:11557750, ECO:0000269|PubMed:15466472, ECO:0000269|PubMed:19103148, ECO:0000269|PubMed:19567782, ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462}.O95562SFT2BVesicle transport protein SFT2BO60637TSN3 Tetraspanin-3FUNCTION: Regulates the proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair. {ECO:0000250}.Q8N5L8RP25L/Ribonuclease P protein subunit p25-like protein6FUNCTION: May be a component of ribonuclease P or MRP.P0DMQ5INAM2%Putative transmembrane protein INAFM2YSUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.Q92688AN32B=Acidic leucine-rich nuclear phosphoprotein 32 family member BSUBCELLULAR LOCATION: Isoform 1: Nucleus. Note=Accumulates in the nuclei at the S phase. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks a nuclear localization signal.activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; inner ear development [GO:0048839]; negative regulation of cell differentiation [GO:0045596]; nucleosome assembly [GO:0006334]; palate development [GO:0060021]; positive regulation of protein export from nucleus [GO:0046827]; vasculature development [GO:0001944]; ventricular system development [GO:0021591]Ahistone binding [GO:0042393]; RNA polymerase binding [GO:0070063]FUNCTION: Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity (By similarity). Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome. {ECO:0000250, ECO:0000269|PubMed:20538007}.Q92879CELF1CUGBP Elav-like family member 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8948631}. Cytoplasm {ECO:0000269|PubMed:8948631}. Note=RNA-binding activity is detected in both nuclear and cytoplasmic compartments.jembryo development [GO:0009790]; germ cell development [GO:0007281]; mRNA processing [GO:0006397]; mRNA splice site selection [GO:0006376]; negative regulation of translation [GO:0017148]; positive regulation of multicellular organism growth [GO:0040018]; regulation of RNA splicing [GO:0043484]; RNA interference [GO:0016246]; spermatid development [GO:0007286]BRE binding [GO:0042835]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; translation repressor activity, nucleic acid binding [GO:0000900]cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of T< NNT2 during heart remodeling at the juvenile to adult transition. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. {ECO:0000250, ECO:0000269|PubMed:10536163, ECO:0000269|PubMed:11124939, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:12799066, ECO:0000269|PubMed:14726956, ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:16946708}.O60704TPST2#Protein-tyrosine sulfotransferase 2fusion of sperm to egg plasma membrane [GO:0007342]; peptidyl-tyrosine sulfation [GO:0006478]; prevention of polyspermy [GO:0060468]endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]Q9UK23NAGPABN-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidaseSUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12058031}; Single-pass type I membrane protein {ECO:0000269|PubMed:12058031}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12058031}. Note=Cis/medial Golgi.carbohydrate metabolic process [GO:0005975]; cellular protein modification process [GO:0006464]; lysosome organization [GO:0007040]; protein glycosylation [GO:0006486]; protein targeting to lysosome [GO:0006622]XN-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity [GO:0003944]QGolgi cisterna membrane [GO:0032580]; integral component of membrane [GO:0016021]`FUNCTION: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases. {ECO:0000269|PubMed:23572527}.Q9NZR1TMOD2Tropomodulin-2qactin filament organization [GO:0007015]; learning or memory [GO:0007611]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; nervous system development [GO:0007399]; neuron-neuron synaptic transmission [GO:0007270]; pointed-end actin filament capping [GO:0051694]; positive regulation of G-protein coupled receptor protein signaling pathway [GO:0045745]wcytoskeleton [GO:0005856]; growth cone [GO:0030426]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]Q13557KCC2DACalcium/calmodulin-dependent protein kinase type II subunit deltaSUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. calcium ion transport [GO:0006816]; cardiac muscle cell contraction [GO:0086003]; cell growth involved in cardiac muscle cell development [GO:0061049]; cellular potassium ion homeostasis [GO:0030007]; cellular response to calcium ion [GO:0071277]; cellular response to heat [GO:0034605]; cytokine-mediated signaling pathway [GO:0019221]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; G1/S transition of mitotic cell cycle [GO:0000082]; interferon-gamma-mediated signaling pathway [GO:0060333]; negative regulation of sodium ion transmembrane transport [GO:1902306]; negative regulation of sodium ion transmembrane transporter activity [GO:2000650]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of Rac protein signal transduction [GO:0035022]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; protein autophosphorylation [GO:0046777]; protein oligomerization [GO:0051259]; protein phosphorylation [GO:0006468]; regulation of cardiac muscle cell action potential [GO:0098901]; regulation of cardiac muscle cell action potential involved in regulation of contraction [GO:0098909]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cell communication by electrical coupling [GO:0010649]; regulation of cell communication by electrical coupling involved in cardiac conduction [GO:1901844]; regulation of cell growth [GO:0001558]; regulation of cellular localization [GO:0060341]; regulation of cellular response to heat [GO:1900034]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of generation of L-type calcium current [GO:1902514]; regulation of heart contraction [GO:0008016]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of histone deacetylase activity [GO:1901725]; regulation of membrane depolarization [GO:0003254]; regulation of relaxation of cardiac muscle [GO:1901897]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; regulation of the force of heart contraction [GO:0002026]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; relaxation of cardiac muscle [GO:0055119]; response to hypoxia [GO:0001666]; synaptic transmission [GO:0007268]IATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; ion channel binding [GO:0044325]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase activity [GO:0004674]; sodium channel inhibitor activity [GO:0019871]; titin binding [GO:0031432]axon initial segment [GO:0043194]; calcium channel complex [GO:0034704]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor< HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. {ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:17179159}.P36873PP1G@Serine/threonine-protein phosphatase PP1-gamma catalytic subunituSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus speckle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Mitochondrion. Note=Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase. {ECO:0000250}.cell division [GO:0051301]; circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; glycogen metabolic process [GO:0005977]; mitotic cell cycle [GO:0000278]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neuron differentiation [GO:0030182]; protein dephosphorylation [GO:0006470]; regulation of circadian rhythm [GO:0042752]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; transforming growth factor beta receptor signaling pathway [GO:0007179]; triglyceride catabolic process [GO:0019433]metal ion binding [GO:0046872]; phosphatase activity [GO:0016791]; phosphoprotein phosphatase activity [GO:0004721]; poly(A) RNA binding [GO:0044822]; protein kinase binding [GO:0019901]; protein N-terminus binding [GO:0047485]; protein serine/threonine phosphatase activity [GO:0004722]cleavage furrow [GO:0032154]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; focal adhesion [GO:0005925]; midbody [GO:0030496]; mitochondrion [GO:0005739]; MLL5-L complex [GO:0070688]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein complex [GO:0043234]; PTW/PP1 phosphatase complex [GO:0072357]FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208}.Q6UVY6MOXD1 DBH-like monooxygenase protein 1copper ion binding [GO:0005507]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen [GO:0016715]Q9Y6J9TAF6LZTAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6LXSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.Cchromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription, initiation [GO:0006352]; histone H3 acetylation [GO:0043966]; regulation of sequence-specific DNA binding transcription factor activity [GO:0051090]; regulation of transcription from RNA polymerase II promoter [GO:0006357]hextracellular exosome [GO:0070062]; histone deacetylase complex [GO:0000118]; STAGA complex [GO:0030914]FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex.Q9NXC5MIO WD repeat-containing protein miocellular protein complex localization [GO:0034629]; cellular response to amino acid starvation [GO:0034198]; positive regulation of TOR signaling [GO:0032008]cell junction [GO:0030054]; cytoplasm [GO:0005737]; GATOR2 complex [GO:0061700]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]Q9BSL1UBAC10Ubiquitin-associated domain-containing protein 1[SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10857748, ECO:0000269|PubMed:15531880}.vcytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] FUNCTION: Non-catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:15746103}.Q9UKF6CPSF39Cleavage and polyadenylation specificity factor subunit 3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15037765}.5'-3' exonuclease activity [GO:0008409]; endoribonuclease activity [GO:0004521]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:0030529]FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. T< he U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:15037765, ECO:0000269|PubMed:17128255, ECO:0000269|PubMed:18688255}.Q7Z478DHX29 ATP-dependent RNA helicase DHX29ATP binding [GO:0005524]; ATP-dependent RNA helicase activity [GO:0004004]; poly(A) RNA binding [GO:0044822]; ribosomal small subunit binding [GO:0043024]; translation initiation factor activity [GO:0003743]ecytoplasm [GO:0005737]; eukaryotic 43S preinitiation complex [GO:0016282]; mitochondrion [GO:0005739]FUNCTION: ATP-binding RNA helicase involved in translation initiation. Part of the 43S preinitiation complex that is required for efficient initiation on mammalian mRNAs with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity. {ECO:0000269|PubMed:19109895, ECO:0000269|PubMed:23706745}.P23511NFYA,Nuclear transcription factor Y subunit alphapositive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of stem cell maintenance [GO:2000036]; regulation of transcription, DNA-templated [GO:0006355]; rhythmic process [GO:0048511]; small molecule metabolic process [GO:0044281]; transcription from RNA polymerase II promoter [GO:0006366]core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; sequence-specific DNA binding transcription factor activity [GO:0003700]FUNCTION: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component ARNTL/BMAL1. {ECO:0000269|PubMed:12741956}.P09603CSF1&Macrophage colony-stimulating factor 1#SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1531650, ECO:0000269|PubMed:3264877}; Single-pass type I membrane protein {ECO:0000269|PubMed:1531650, ECO:0000269|PubMed:3264877}.; SUBCELLULAR LOCATION: Processed macrophage colony-stimulating factor 1: Secreted, extracellular space.branching involved in mammary gland duct morphogenesis [GO:0060444]; cell differentiation [GO:0030154]; cell proliferation [GO:0008283]; developmental process involved in reproduction [GO:0003006]; hemopoiesis [GO:0030097]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; macrophage colony-stimulating factor signaling pathway [GO:0038145]; macrophage differentiation [GO:0030225]; mammary duct terminal end bud growth [GO:0060763]; mammary gland fat development [GO:0060611]; monocyte activation [GO:0042117]; osteoclast differentiation [GO:0030316]; osteoclast proliferation [GO:0002158]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of cellular protein metabolic process [GO:0032270]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage colony-stimulating factor signaling pathway [GO:1902228]; positive regulation of macrophage derived foam cell differentiation [GO:0010744]; positive regulation of macrophage differentiation [GO:0045651]; positive regulation of microglial cell migration [GO:1904141]; positive regulation of monocyte differentiation [GO:0045657]; positive regulation of mononuclear cell proliferation [GO:0032946]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of odontogenesis of dentin-containing tooth [GO:0042488]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of Ras protein signal transduction [GO:0046579]; regulation of macrophage derived foam cell differentiation [GO:0010743]; regulation of ossification [GO:0030278]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; macrophage colony-stimulating factor receptor binding [GO:0005157]; protein homodimerization activity [GO:0042803]CSF1-CSF1R complex [GO:1990682]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]WFUNCTION: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance. {ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:19934330, ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061}.O60318GANP*Germinal-center associated nuclear proteinSUBCELLULAR LOCATION: Isoform GANP: Cytoplasm. Nucleus envelope. Nucleus, nuclear pore complex. Note=In B-cells nuclear import depends on interaction with AICDA/AID, and GANP is selectively targeted to the IgV-region gene. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform MCM3AP: Cytoplasm {ECO:0000269|PubMed:11258703}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11258703}. Note=Binding to MCM3 is required for nuclear import, associates with chromatin.DNA replication [GO:0006260]; immune system process [GO:0002376]; mRNA transport [GO:0051028]; protein import into nucleus [GO:0006606]UDNA binding [GO:0003677]; transferase activity, transferring acyl groups [GO:0016746]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Isoform GANP: Essential for the generation of high-affinity B-cells against T-cell-dependent antigens by affecting somatic hypermutation at the IgV-regions. May have stimulation-dependent DNA primase activity that would generate extra RNA primers in very rapidely proliferating cells and would support clonal expansion of differentiating B-cells (By similarity). Involved in the nuclear export of poly(A)-containing mRNAs by acting as a scaffold for the TREX-2 complex. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. {ECO:0000250, ECO:0000269|PubMed:22307388}.; FUNCTION: Isoform MCM3AP: Acetyltransferase targeting MCM3. Inhibits initiation of DNA replication, but not elongation. {ECO:0000269|PubMed:22307388}.Q96L58B3GT6 Beta-1,3-galactosyltransferase 6SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11551958}; Single-pass type II membrane protein {ECO:0000269|PubMed:11551958}.carbohydrate metabolic process [GO:0005975]; chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate metabolic process [GO:0030204]; glycosaminoglycan biosynthetic process [GO:0006024]; glycosaminoglycan metabolic pro< cess [GO:0030203]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; protein glycosylation [GO:0006486]; small molecule metabolic process [GO:0044281]galactosylxylosylprotein 3-beta-galactosyltransferase activity [GO:0047220]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]; UDP-galactosyltransferase activity [GO:0035250]Golgi cisterna membrane [GO:0032580]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. Has a preference for galactose-beta-1,4-xylose that is found in the linker region of glycosaminoglycans, such as heparan sulfate and chondroitin sulfate. Has no activity towards substrates with terminal glucosamine or galactosamine residues. {ECO:0000269|PubMed:11551958}.O94929ABLM3Actin-binding LIM protein 3Qactin cytoskeleton organization [GO:0030036]; axon guidance [GO:0007411]; cilium assembly [GO:0042384]; lamellipodium assembly [GO:0030032]; positive regulation of protein targeting to mitochondrion [GO:1903955]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; transcription, DNA-templated [GO:0006351]Mcytoplasm [GO:0005737]; lamellipodium [GO:0030027]; stress fiber [GO:0001725]FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. {ECO:0000269|PubMed:17194709}.Q6NUQ4TM214Transmembrane protein 214SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23661706}; Multi-pass membrane protein {ECO:0000269|PubMed:23661706}.cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; integral component of membrane [GO:0016021]FUNCTION: Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress. {ECO:0000269|PubMed:23661706}.Q86WJ1CHD1L0Chromodomain-helicase-DNA-binding protein 1-likeSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19661379}. Note=Localizes at sites of DNA damage. Probably recruited to DNA damage sites by PARylated PARP1.cellular response to DNA damage stimulus [GO:0006974]; chromatin remodeling [GO:0006338]; DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]ATPase activity [GO:0016887]; ATP binding [GO:0005524]; ATP-dependent DNA helicase activity [GO:0004003]; nucleic acid binding [GO:0003676]; nucleotide binding [GO:0000166]FUNCTION: DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding. {ECO:0000269|PubMed:18023026, ECO:0000269|PubMed:19661379}.Q9BRR3TM246Transmembrane protein 246Q9H2P9DPH5Diphthine synthase(diphthine synthase activity [GO:0004164]FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis. {ECO:0000250|UniProtKB:P32469, ECO:0000269|PubMed:23486472}.P02462CO4A1Collagen alpha-1(IV) chain^axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; cellular response to amino acid stimulus [GO:0071230]; collagen catabolic process [GO:0030574]; epithelial cell differentiation [GO:0030855]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; neuromuscular junction development [GO:0007528]; patterning of blood vessels [GO:0001569]; receptor-mediated endocytosis [GO:0006898]; renal tubule morphogenesis [GO:0061333]; retinal blood vessel morphogenesis [GO:0061304]extracellular matrix constituent conferring elasticity [GO:0030023]; extracellular matrix structural constituent [GO:0005201]; platelet-derived growth factor binding [GO:0048407]basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]?FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.Q96G25MED85Mediator of RNA polymerase II transcription subunit 8gene expression [GO:0010467]; protein ubiquitination [GO:0016567]; regulation of transcription, DNA-templated [GO:0006355]; transcription initiation from RNA polymerase II promoter [GO:0006367]RNA polymerase II core promoter proximal region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription cofactor activity [GO:0001104][core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. May play a role as a target recruitment subunit in E3 ubiquitin-protein ligase complexes and thus in ubiquitination and subsequent proteasomal degradation of target proteins.O60870KIN17DNA/RNA-binding protein KIN17SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}. Cytoplasm {ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}. Note=During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids. {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}.cellular response to DNA damage stimulus [GO:0006974]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; mRNA processing [GO:0006397]; viral process [GO:0016032]|DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]FUNCTION: Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal doma< in to RNA in vitro. {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485, ECO:0000269|PubMed:17045609}.P35475IDUAAlpha-L-iduronidase9carbohydrate metabolic process [GO:0005975]; cell morphogenesis [GO:0000902]; chemical homeostasis [GO:0048878]; chondroitin sulfate catabolic process [GO:0030207]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate catabolic process [GO:0030209]; disaccharide metabolic process [GO:0005984]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; limb morphogenesis [GO:0035108]; lysosome organization [GO:0007040]; skeletal system morphogenesis [GO:0048705]; small molecule metabolic process [GO:0044281]#L-iduronidase activity [GO:0003940]]coated vesicle [GO:0030135]; extracellular exosome [GO:0070062]; lysosomal lumen [GO:0043202]Q96AE4FUBP1&Far upstream element-binding protein 1opositive regulation of gene expression [GO:0010628]; transcription from RNA polymerase II promoter [GO:0006366]1poly(A) RNA binding [GO:0044822]; RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [GO:0001205]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]FUNCTION: Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription. {ECO:0000269|PubMed:8125259}.Q8N5H3FA89BProtein FAM89BwSUBCELLULAR LOCATION: Isoform 3: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cell surface {ECO:0000250}.negative regulation of SMAD protein import into nucleus [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512].transcription corepressor binding [GO:0001222]1cell surface [GO:0009986]; cytoplasm [GO:0005737]FUNCTION: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. {ECO:0000250}.P19021AMD.Peptidyl-glycine alpha-amidating monooxygenaseFSUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 2: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Secreted from secretory granules.; SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Secreted from secretory granules.peptide amidation [GO:0001519]copper ion binding [GO:0005507]; L-ascorbic acid binding [GO:0031418]; peptidylamidoglycolate lyase activity [GO:0004598]; peptidylglycine monooxygenase activity [GO:0004504]; zinc ion binding [GO:0008270]FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.P53778MK12#Mitogen-activated protein kinase 12SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma (By similarity). {ECO:0000250}.cell cycle arrest [GO:0007050]; DNA damage induced protein phosphorylation [GO:0006975]; MAPK cascade [GO:0000165]; mitochondrion organization [GO:0007005]; muscle cell differentiation [GO:0042692]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; neurotrophin TRK receptor signaling pathway [GO:0048011]; organelle organization [GO:0006996]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of peptidase activity [GO:0010952]; Ras protein signal transduction [GO:0007265]; regulation of transcription, DNA-templated [GO:0006355]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine/threonine kinase activity [GO:0004674]bcytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. {ECO:0000269|PubMed:10848581, ECO:0000269|PubMed:14592936, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:20605917, ECO:0000269|PubMed:21172807, ECO:0000269|PubMed:8633070, ECO:0000269|PubMed:9430721}.Q03001DYSTDystoninSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Note=Associates with intermediate filaments, acin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic actin filaments. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton. Cell junction, hemidesmosome. Note=Localizes to actin and intermediate filaments cytoskeletons (By similarity). Colocalizes with the epidermal KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with ITGB4 at the leading edge of migrating keratinocytes. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 6: Nucleus {ECO:0000250}. Nucleus envelope {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}; Single-pass membrane protein {ECO:0000269|< PubMed:10428034}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Note=Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. {ECO:0000250}.; SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10428034}. Cell projection, axon {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}. Note=Associates with axonal microtubules and intermediate filaments, but not with actin cytoskeleton, in sensory neurons.; SUBCELLULAR LOCATION: Isoform 8: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.cell adhesion [GO:0007155]; cell cycle arrest [GO:0007050]; cell motility [GO:0048870]; cytoskeleton organization [GO:0007010]; extracellular matrix organization [GO:0030198]; hemidesmosome assembly [GO:0031581]; integrin-mediated signaling pathway [GO:0007229]; intermediate filament cytoskeleton organization [GO:0045104]; maintenance of cell polarity [GO:0030011]; microtubule cytoskeleton organization [GO:0000226]; response to wounding [GO:0009611]calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; microtubule plus-end binding [GO:0051010]; protein C-terminus binding [GO:0008022]; protein homodimerization activity [GO:0042803]actin cytoskeleton [GO:0015629]; axon [GO:0030424]; basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoplasmic membrane-bounded vesicle [GO:0016023]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; hemidesmosome [GO:0030056]; H zone [GO:0031673]; integral component of membrane [GO:0016021]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; microtubule cytoskeleton [GO:0015630]; microtubule plus-end [GO:0035371]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; Z disc [GO:0030018]FUNCTION: Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh.; FUNCTION: Isoform 3: plays a structural role in the assembly of hemidesmosomes of epithelial cells; anchors keratin-containing intermediate filaments to the inner plaque of hemidesmosomes. Required for the regulation of keratinocyte polarity and motility; mediates integrin ITGB4 regulation of RAC1 activity.; FUNCTION: Isoform 6: required for bundling actin filaments around the nucleus. {ECO:0000250}.; FUNCTION: Isoform 7: regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport.Q6ZNA5FRRS1Ferric-chelate reductase 1Nferric-chelate reductase activity [GO:0000293]; metal ion binding [GO:0046872]FUNCTION: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. {ECO:0000250}.Q14684RRP1B,Ribosomal RNA processing protein 1 homolog BVnegative regulation of phosphatase activity [GO:0010923]; rRNA processing [GO:0006364]cytosol [GO:0005829]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleolus [GO:0005730]; nucleus [GO:0005634]; preribosome, small subunit precursor [GO:0030688]Q96DX4RSPRY0RING finger and SPRY domain-containing protein 1Q15046SYKLysine--tRNA ligaseSUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Secreted. Note=Secretion is induced by TNF-alpha.; SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.diadenosine tetraphosphate biosynthetic process [GO:0015966]; gene expression [GO:0010467]; lysyl-tRNA aminoacylation [GO:0006430]; tRNA aminoacylation for protein translation [GO:0006418]; tRNA processing [GO:0008033]; viral process [GO:0016032]amino acid binding [GO:0016597]; ATP binding [GO:0005524]; lysine-tRNA ligase activity [GO:0004824]; metal ion binding [GO:0046872]; tRNA binding [GO:0000049]%aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; microtubule cytoskeleton [GO:0015630]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation. {ECO:0000269|PubMed:15851690, ECO:0000269|PubMed:5338216}.Q63HR2TENC1,Tensin-like C1 domain-containing phosphataseSUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:11792844, ECO:0000269|PubMed:22019427}. Cell membrane {ECO:0000269|PubMed:11792844}; Peripheral membrane protein {ECO:0000269|PubMed:11792844}; Cytoplasmic side {ECO:0000269|PubMed:11792844}. Note=Detected at the end of actin stress fibers. Detected in cytoplasmic punctate bodies (PubMed:22019427). {ECO:0000269|PubMed:22019427}.\cellular homeostasis [GO:0019725]; collagen metabolic process [GO:0032963]; intracellular signal transduction [GO:0035556]; kidney development [GO:0001822]; multicellular organismal homeostasis [GO:0048871]; multicellular organism growth [GO:0035264]; negative regulation of cell proliferation [GO:0008285]; response to muscle activity [GO:0014850]mkinase binding [GO:0019900]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]Ufocal adhesion [GO:0005925]; intracellular [GO:0005622]; plasma membrane [GO:0005886]FUNCTION: Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling. {ECO:0000269|PubMed:15817639}.P02792FRILFerritin light chaincellular iron ion homeostasis [GO:0006879]; iron ion homeostasis [GO:0055072]; iron ion transport [GO:0006826]; membrane organization [GO:0061024]; post-Golgi vesicle-mediated transport [GO:0006892]; receptor-mediated endocytosis [GO:0006898]; transmembrane transport [GO:0055085]gferric iron binding [GO:0008199]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]|cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular ferritin complex [GO:0008043]; membrane [GO:0016020]NFUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). {ECO:0000250}.Q5T280CI114#Putative methyltransferase C9orf114SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}. Note=Associated with the outer kinetochore. {ECO:0000269|PubMed:20813266}.FUNCTION: Required both for chromosome alignment and for association of the centrosomes with the poles of the bipolar spindle during metaphase. {ECO:0000269|PubMed:20813266}.Q96PV6LENG8#Leukocyte receptor cluster member 8Q9Y5Q8TF3C5-General transcription factor 3C polypeptide 5K5S class rRNA transcriptio< n from RNA polymerase III type 1 promoter [GO:0042791]; gene expression [GO:0010467]; skeletal muscle cell differentiation [GO:0035914]; transcription, DNA-templated [GO:0006351]; transcription from RNA polymerase III promoter [GO:0006383]; tRNA transcription from RNA polymerase III promoter [GO:0042797]Q9UJX5APC4$Anaphase-promoting complex subunit 4]protein phosphatase binding [GO:0019903]; ubiquitin-protein transferase activity [GO:0004842]Q9Y3C4TPRKBEKC/KEOPS complex subunit TPRKBFUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification (By similarity). {ECO:0000250}.Q9HB40RISC*Retinoid-inducible serine carboxypeptidasenegative regulation of blood pressure [GO:0045776]; positive regulation of vasodilation [GO:0045909]; retinoic acid metabolic process [GO:0042573]QFUNCTION: May be involved in vascular wall and kidney homeostasis. {ECO:0000250}.Q7Z5H3RHG22 Rho GTPase-activating protein 22SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic. Some fraction is nuclear (By similarity). {ECO:0000250}.angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of transcription, DNA-templated [GO:0006355]; small GTPase mediated signal transduction [GO:0007264]; transcription, DNA-templated [GO:0006351]Gcytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]FUNCTION: Rho GTPase-activating protein involved in the signal transduction pathway that regulates endothelial cell capillary tube formation during angiogenesis. Acts as a GTPase activator for the RAC1 by converting it to an inactive GDP-bound state. Inhibits RAC1-dependent lamellipodia formation. May also play a role in transcription regulation via its interaction with VEZF1, by regulating activity of the endothelin-1 (EDN1) promoter (By similarity). {ECO:0000250}.P48960CD97 CD97 antigenSUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.; SUBCELLULAR LOCATION: CD97 antigen subunit alpha: Secreted, extracellular space.]cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cell surface receptor signaling pathway [GO:0007166]; G-protein coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; movement of cell or subcellular component [GO:0006928]; positive regulation of synapse assembly [GO:0051965]calcium ion binding [GO:0005509]; G-protein coupled receptor activity [GO:0004930]; transmembrane signaling receptor activity [GO:0004888]extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; plasma membrane [GO:0005886]FUNCTION: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration (By similarity). {ECO:0000250}.P62304RUXE!Small nuclear ribonucleoprotein ESUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.gene expression [GO:0010467]; hair cycle [GO:0042633]; histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; mRNA splicing, via spliceosome [GO:0000398]; ncRNA metabolic process [GO:0034660]; RNA splicing [GO:0008380]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]; termination of RNA polymerase II transcription [GO:0006369]; transcription from RNA polymerase II promoter [GO:0006366]Ccatalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pICln-Sm protein complex [GO:0034715]; precatalytic spliceosome [GO:0071011]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U4 snRNP [GO:0005687]; U5 snRNP [GO:0005682]; U7 snRNP [GO:0005683]FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing. May indirectly play a role in hair development. {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23246290, ECO:0000269|PubMed:23333303}.P50897PPT1 Palmitoyl-protein thioesterase 1adult locomotory behavior [GO:0008344]; associative learning [GO:0008306]; brain development [GO:0007420]; cellular protein catabolic process [GO:0044257]; cofactor metabolic process [GO:0051186]; cofactor transport [GO:0051181]; grooming behavior [GO:0007625]; lipid catabolic process [GO:0016042]; lysosomal lumen acidification [GO:0007042]; membrane raft organization [GO:0031579]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; neuron development [GO:0048666]; neurotransmitter secretion [GO:0007269]; pinocytosis [GO:0006907]; positive regulation of pinocytosis [GO:0048549]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein catabolic process [GO:0030163]; protein depalmitoylation [GO:0002084]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; regulation of phospholipase A2 activity [GO:0032429]; regulation of synapse structure or activity [GO:0050803]; response to stimulus [GO:0050896]; sphingolipid catabolic process [GO:0030149]; visual perception [GO:0007601]bpalmitoyl-(protein) hydrolase activity [GO:0008474]; palmitoyl-CoA hydrolase activity [GO:0016290]eaxon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; synaptic vesicle [GO:0008021]FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.Q9NS87KIF15Kinesin-like protein KIF15SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Detected during the interphase in the cytoplasm as finely punctuate pattern and irregularly shaped dots. Detected during mitosis on the mitotic spindle. Colocalizes with TPX2 in mitosis. Localizes at the central spindle at anaphase (By similarity). Localizes at the sites of invaginating cell membranes, a position that corresponds to the location of the contractile actomyosin ring of dividing cells (By similarity). Colocalizes with actin in interphase (By similarity). Colocalizes in dendrites and in growth cone of axons with microtubules (By similarity). {ECO:0000250}.antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; blood coagulation [GO:0007596]; cell proliferation [GO:0008283]; microtubule-based movement [GO:0007018]; mitotic nuclear division [GO:0007067]ATPase activity [GO:001< 6887]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; microtubule motor activity [GO:0003777]; motor activity [GO:0003774]centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]; plus-end kinesin complex [GO:0005873]; spindle [GO:0005819]jFUNCTION: Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}.Q96JM3CHAP11Chromosome alignment-maintaining phosphoprotein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21063390}. Chromosome {ECO:0000269|PubMed:21063390}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21063390}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21063390}.attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; protein localization to kinetochore [GO:0034501]; protein localization to microtubule [GO:0035372]; sister chromatid biorientation [GO:0031134]condensed chromosome [GO:0000793]; condensed chromosome kinetochore [GO:0000777]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]:FUNCTION: Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269|PubMed:21063390}.O43805SSNA1'Sjoegren syndrome nuclear autoantigen 1bSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.ciliary receptor clustering involved in smoothened signaling pathway [GO:0060830]; G2/M transition of mitotic cell cycle [GO:0000086]; intraciliary transport [GO:0042073]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]dcentrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; nucleus [GO:0005634]Q9H9F9ARP5Actin-related protein 5SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear but undergoes nucleo-cytoplasmic shuttling. Localized to interphase nuclei, but not nucleoli; excluded from chromosomes as mitosis progresses.DNA recombination [GO:0006310]; double-strand break repair [GO:0006302]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]; UV-damage excision repair [GO:0070914]Hcytoplasm [GO:0005737]; Ino80 complex [GO:0031011]; nucleus [GO:0005634]+FUNCTION: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair. {ECO:0000269|PubMed:19014934, ECO:0000269|PubMed:20855601}.P21397AOFA#Amine oxidase [flavin-containing] AkSUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.cellular biogenic amine metabolic process [GO:0006576]; dopamine catabolic process [GO:0042420]; neurotransmitter biosynthetic process [GO:0042136]; neurotransmitter catabolic process [GO:0042135]; neurotransmitter secretion [GO:0007269]; phenylethylamine metabolic process [GO:0042443]; serotonin metabolic process [GO:0042428]; small molecule metabolic process [GO:0044281]; synaptic transmission [GO:0007268]; xenobiotic metabolic process [GO:0006805]}flavin adenine dinucleotide binding [GO:0050660]; primary amine oxidase activity [GO:0008131]; serotonin binding [GO:0051378]IFUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.P62633CNBP%Cellular nucleic acid-binding proteinSSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.^cholesterol biosynthetic process [GO:0006695]; positive regulation of cell proliferation [GO:0008284]; positive regulation of transcription, DNA-templated [GO:0045893]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]; single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO:0008270]Ncytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]FUNCTION: Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression.Q15003CND2Condensin complex subunit 2SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11694586}. Cytoplasm {ECO:0000269|PubMed:11694586}. Chromosome {ECO:0000269|PubMed:11694586}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.ycondensin complex [GO:0000796]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]Q9Y6R9CCD61(Coiled-coil domain-containing protein 61Q9NVR0KLH11Kelch-like protein 11FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. {ECO:0000250}.Q13510ASAH1Acid ceramidase ceramidaseceramide metabolic process [GO:0006672]; glycosphingolipid metabolic process [GO:0006687]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]Acatalytic activity [GO:0003824]; ceramidase activity [GO:0017040]TFUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.Q13895BYSTBystinSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17381424}. Nucleus, nucleolus {ECO:0000269|PubMed:17381424}. Note=Associated with 40S ribosomal subunits.brain development [GO:0007420]; cell adhesion [GO:0007155]; cell proliferation [GO:0008283]; cellular response to growth factor stimulus [GO:0071363]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to organic cyclic compound [GO:0071407]; female pregnancy [GO:0007565]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; neuron differentiation [GO:0030182]; trophectodermal cell differentiation [GO:0001829]&apical part of cell [GO:0045177]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] FUNCTION: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos. {ECO:0000269|PubMed:17360433, ECO:0000269|PubMed:17381424}.Q9Y3D6FIS1Mitochondrial fission 1 proteinSUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane; Single-pass membrane protein.2calcium-mediated signaling using intracellular calcium source [GO:0035584]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial fusion [GO:0008053]; mitochondrion degradation [GO:0000422]; mitochondrion morphogenesis [GO:0070584]; negative regulation of endoplasmic reticulum calcium i< on concentration [GO:0032471]; peroxisome fission [GO:0016559]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of protein targeting to membrane [GO:0090314]; protein homooligomerization [GO:0051260]; protein targeting to mitochondrion [GO:0006626]; regulation of mitochondrion organization [GO:0010821]; release of cytochrome c from mitochondria [GO:0001836]cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; integral component of mitochondrial outer membrane [GO:0031307]; integral component of peroxisomal membrane [GO:0005779]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]; protein complex [GO:0043234]dFUNCTION: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. {ECO:0000269|PubMed:12783892, ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:14996942, ECO:0000269|PubMed:16107562, ECO:0000269|PubMed:16118244, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241}.Q14966ZN638Zinc finger protein 638SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:8647861}.}regulation of transcription, DNA-templated [GO:0006355]; RNA splicing [GO:0008380]; transcription, DNA-templated [GO:0006351]double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]'FUNCTION: Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). Binds to cytidine clusters in double-stranded DNA. {ECO:0000250, ECO:0000269|PubMed:8647861}.P23921RIR12Ribonucleoside-diphosphate reductase large subunitAcell proliferation in forebrain [GO:0021846]; deoxyribonucleotide biosynthetic process [GO:0009263]; DNA replication [GO:0006260]; male gonad development [GO:0008584]; mitotic cell cycle [GO:0000278]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; protein heterotetramerization [GO:0051290]; pyrimidine nucleobase metabolic process [GO:0006206]; response to ionizing radiation [GO:0010212]; retina development in camera-type eye [GO:0060041]; small molecule metabolic process [GO:0044281]wATP binding [GO:0005524]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.Q53EU6GPAT3&Glycerol-3-phosphate acyltransferase 3SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:19318427}; Multi-pass membrane protein {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:19318427}.CDP-diacylglycerol biosynthetic process [GO:0016024]; cellular lipid metabolic process [GO:0044255]; glycerophospholipid biosynthetic process [GO:0046474]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; regulation of TOR signaling [GO:0032006]; small molecule metabolic process [GO:0044281]; triglyceride biosynthetic process [GO:0019432]1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; glycerol-3-phosphate O-acyltransferase activity [GO:0004366]FUNCTION: May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA). {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135, ECO:0000269|PubMed:19318427}.Q9Y2H6FND3A1Fibronectin type-III domain-containing protein 3AiSUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.fertilization [GO:0009566]; Sertoli cell development [GO:0060009]; single organismal cell-cell adhesion [GO:0016337]; spermatid development [GO:0007286]acrosomal vesicle [GO:0001669]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; vesicle membrane [GO:0012506]TFUNCTION: Mediates spermatid-Sertoli adhesion during spermatogenesis. {ECO:0000250}.P31350RIR2/Ribonucleoside-diphosphate reductase subunit M2'deoxyribonucleoside diphosphate metabolic process [GO:0009186]; deoxyribonucleotide biosynthetic process [GO:0009263]; DNA replication [GO:0006260]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic cell cycle [GO:0000278]; nucleobase-containing small molecule interconversion [GO:0015949]; nucleobase-containing small molecule metabolic process [GO:0055086]; protein heterotetramerization [GO:0051290]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; small molecule metabolic process [GO:0044281]cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoside-diphosphate reductase complex [GO:0005971]FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.Q969S2NEIL2Endonuclease 8-like 2<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12097317}.base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; depyrimidination [GO:0045008]; DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289]damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) lyase activity [GO:0003906]; hydrolase activity, hydrolyzing N-glycosyl compounds [GO:0016799]; zinc ion binding [GO:0008270]Rcytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; spindle microtubule [GO:0005876]FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000269|PubMed:12097317, ECO:0000269|PubMed:14522990, ECO:0000269|PubMed:15175427, ECO:0000269|PubMed:15339932}.Q14332FZD2 Frizzled-2lcanonical Wnt signaling pathway [GO:0060070]; cell-cell signaling [GO:0007267]; cochlea morphogenesis [GO:0090103]; epithelial cell differentiation [GO:0030855]; hard palate development [GO:0060022]; inner ear receptor cell development [GO:0060119]; membranous septum morphogenesis [GO:0003149]; muscular septum morphogenesis [GO:0003150]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive reg< ulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cGMP metabolic process [GO:0030825]; positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091]; positive regulation of transcription, DNA-templated [GO:0045893]; sensory perception of smell [GO:0007608]G-protein coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]; Wnt-activated receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; integral component of membrane [GO:0016021]; plasma membrane [GO:0005886]Q9Y5W8SNX13Sorting nexin-13SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:11729322}; Peripheral membrane protein {ECO:0000269|PubMed:11729322}; Cytoplasmic side {ECO:0000269|PubMed:11729322}.intracellular protein transport [GO:0006886]; positive regulation of GTPase activity [GO:0043547]; termination of G-protein coupled receptor signaling pathway [GO:0038032]`phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol binding [GO:0035091]Aearly endosome [GO:0005769]; early endosome membrane [GO:0031901]FUNCTION: May be involved in several stages of intracellular trafficking. May play a role in endosome homeostasis (By similarity). Acts as a GAP for Galphas. {ECO:0000250, ECO:0000269|PubMed:11729322}.Q9UKB1FBW1B%F-box/WD repeat-containing protein 11Ci-R-SlimFBXW11/BTRCnG2/M transition of mitotic cell cycle [GO:0000086]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; negative regulation of NF-kappaB import into nucleus [GO:0042347]; negative regulation of transcription, DNA-templated [GO:0045892]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of proteolysis [GO:0045862]; positive regulation of transcription, DNA-templated [GO:0045893]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein dephosphorylation [GO:0006470]; protein destabilization [GO:0031648]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; rhythmic process [GO:0048511]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; Wnt signaling pathway [GO:0016055]cubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]centrosome [GO:0005813]; cytosol [GO:0005829]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005]; ubiquitin ligase complex [GO:0000151]FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. Is target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action. {ECO:0000269|PubMed:10321728, ECO:0000269|PubMed:10437795, ECO:0000269|PubMed:10644755, ECO:0000269|PubMed:10648623, ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323, ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18575781, ECO:0000269|PubMed:19730691, ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:20347421}.O75781PALM Paralemmin-1tSUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}; Cytoplasmic side {ECO:0000269|PubMed:14978216}. Cell projection, filopodium membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity.cellular response to electrical stimulus [GO:0071257]; cytoskeleton organization [GO:0007010]; movement of cell or subcellular component [GO:0006928]; negative regulation of adenylate cyclase activity [GO:0007194]; negative regulation of dopamine receptor signaling pathway [GO:0060160]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of filopodium assembly [GO:0051491]; protein targeting to plasma membrane [GO:0072661]; regulation of cell shape [GO:0008360]; synapse maturation [GO:0060074]apicolateral plasma membrane [GO:0016327]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic membrane-bounded vesicle [GO:0016023]; dendrite membrane [GO:0032590]; dendritic spine membrane [GO:0032591]; filopodium membrane [GO:0031527]; integral component of plasma membrane [GO:0005887]; intracellular membrane-bounded organelle [GO:0043231]; neuronal postsynaptic density [GO:0097481]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. {ECO:0000269|PubMed:14978216}.Q96PY5FMNL2Formin-like protein 2cortical actin cytoskeleton organization [GO:0030866]; cytoskeleton organization [GO:0007010]; regulation of cell morphogenesis [GO:0022604]; small GTPase mediated signal transduction [GO:0007264]FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics. {ECO:0000269|PubMed:21834987}.Q16637SMNSurvival motor neuron proteinSUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Nucleus, Cajal body. Cytoplasmic granule. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Colocalizes with Actn at the Z-line of skeletal muscle (By similarity). Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules. Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies. {ECO:0000250}.gene expression [GO:0010467]; ncRNA metabolic process [GO:0034660]; nervous system development [GO:0007399]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]; Z disc [GO:0030018]iFUNCTION: The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of cor< e snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:9845364}.Q96CW1AP2M1AP-2 complex subunit muantigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; axon guidance [GO:0007411]; clathrin-mediated endocytosis [GO:0072583]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular protein transport [GO:0006886]; membrane organization [GO:0061024]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of protein localization to plasma membrane [GO:1903077]; neurotrophin TRK receptor signaling pathway [GO:0048011]; regulation of defense response to virus by virus [GO:0050690]; synaptic transmission [GO:0007268]; viral process [GO:0016032]lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; signal sequence binding [GO:0005048]; transporter activity [GO:0005215]AP-2 adaptor complex [GO:0030122]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). {ECO:0000250}.Q6NYC1JMJD6=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle.cell surface receptor signaling pathway [GO:0007166]; erythrocyte development [GO:0048821]; heart development [GO:0007507]; histone H3-R2 demethylation [GO:0070078]; histone H4-R3 demethylation [GO:0070079]; kidney development [GO:0001822]; lung development [GO:0030324]; macrophage activation [GO:0042116]; mRNA processing [GO:0006397]; peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine [GO:0018395]; recognition of apoptotic cell [GO:0043654]; regulation of mRNA splicing, via spliceosome [GO:0048024]; regulation of transcription, DNA-templated [GO:0006355]; retina development in camera-type eye [GO:0060041]; RNA splicing [GO:0008380]; sprouting angiogenesis [GO:0002040]; T cell differentiation in thymus [GO:0033077]; transcription, DNA-templated [GO:0006351]Vhistone demethylase activity (H3-R2 specific) [GO:0033746]; histone demethylase activity (H4-R3 specific) [GO:0033749]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; peptidyl-lysine 5-dioxygenase activity [GO:0070815]; receptor activity [GO:0004872]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]dnucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses. {ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:20684070, ECO:0000269|PubMed:21060799}.Q9P016THYN1Thymocyte nuclear protein 1FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. {ECO:0000250}.Q96P53WDFY2.WD repeat and FYVE domain-containing protein 2Q52LD8RFTN2 Raftlin-2FdsRNA transport [GO:0033227]; response to exogenous dsRNA [GO:0043330]P43251BTD Biotinidasebiotin metabolic process [GO:0006768]; central nervous system development [GO:0007417]; small molecule metabolic process [GO:0044281]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]ubiotinidase activity [GO:0047708]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrial matrix [GO:0005759]nFUNCTION: Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.Q96GY0ZC21A-Zinc finger C2HC domain-containing protein 1AQ14314FGL2 FibroleukinCextracellular exosome [GO:0070062]; fibrinogen complex [GO:0005577]OFUNCTION: May play a role in physiologic lymphocyte functions at mucosal sites.P31483TIA1Nucleolysin TIA-1 isoform p40SUBCELLULAR LOCATION: Cytoplasmic granule. Nucleus. Note=Accumulates in cytoplasmic stress granules (SG) following cellular damage.apoptotic process [GO:0006915]; negative regulation of cytokine biosynthetic process [GO:0042036]; negative regulation of translation [GO:0017148]; regulation of mRNA splicing, via spliceosome [GO:0048024]AU-rich element binding [GO:0017091]; nucleotide binding [GO:0000166]; poly(A) binding [GO:0008143]; poly(A) RNA binding [GO:0044822]~cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nuclear stress granule [GO:0097165]; nucleoplasm [GO:0005654]< FUNCTION: Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.Q86UK7ZN598Zinc finger protein 598O75167PHAR2!Phosphatase and actin regulator 2P304601B087HLA class I histocompatibility antigen, B-8 alpha chainantigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent [GO:0002480]; antigen processing and presentation of peptide antigen via MHC class I [GO:0002474]; cytokine-mediated signaling pathway [GO:0019221]; immune response [GO:0006955]; interferon-gamma-mediated signaling pathway [GO:0060333]; regulation of immune response [GO:0050776]; type I interferon signaling pathway [GO:0060337]; viral process [GO:0016032]^chaperone binding [GO:0051087]; peptide antigen binding [GO:0042605]; TAP binding [GO:0046977]cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; integral component of plasma membrane [GO:0005887]; membrane [GO:0016020]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]Q7Z3C6ATG9AAutophagy-related protein 9ASUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Under amino acid starvation or rapamycin treatment, redistributes from a juxtanuclear clustered pool to a dispersed peripheral cytosolic pool. The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1.autophagosome assembly [GO:0000045]; innate immune response [GO:0045087]; late nucleophagy [GO:0044805]; mitochondrion degradation [GO:0000422]; negative regulation of interferon-beta production [GO:0032688]; piecemeal microautophagy of nucleus [GO:0034727]; protein localization to Golgi apparatus [GO:0034067]; protein localization to pre-autophagosomal structure [GO:0034497]; protein transport [GO:0015031]sautophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; membrane [GO:0016020]; pre-autophagosomal structure [GO:0000407]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]FUNCTION: Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H. {ECO:0000269|PubMed:16940348}.Q92804RBP56)TATA-binding protein-associated factor 2NSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19124016}. Cytoplasm {ECO:0000269|PubMed:19124016}. Note=Shuttles from the nucleus to the cytoplasm.@positive regulation of transcription, DNA-templated [GO:0045893]zDNA binding [GO:0003677]; nucleotide binding [GO:0000166]; poly(A) RNA binding [GO:0044822]; zinc ion binding [GO:0008270]FUNCTION: RNA and ssDNA-binding protein that may play specific roles during transcription initiation at distinct promoters. Can enter the preinitiation complex together with the RNA polymerase II (Pol II). {ECO:0000269|PubMed:19124016}.Q96AG3S2546"Solute carrier family 25 member 46Q9Y2H5PKHA67Pleckstrin homology domain-containing family A member 6O00562PITM1;Membrane-associated phosphatidylinositol transfer protein 1SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Lipid droplet. Cleavage furrow. Midbody. Note=Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis.brain development [GO:0007420]; lipid metabolic process [GO:0006629]; phospholipid transport [GO:0015914]; phototransduction [GO:0007602]; protein transport [GO:0015031]Vmetal ion binding [GO:0046872]; phosphatidylinositol transporter activity [GO:0008526]cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; lipid particle [GO:0005811]; membrane [GO:0016020]; midbody [GO:0030496]FUNCTION: Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions. {ECO:0000250, ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057}.Q8IY37DHX37)Probable ATP-dependent RNA helicase DHX37Q9HB65ELL3(RNA polymerase II elongation factor ELL3<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882741}.DNA-templated transcription, elongation [GO:0006354]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of neural precursor cell proliferation [GO:2000179]; positive regulation of neurogenesis [GO:0050769]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of epithelial to mesenchymal transition [GO:0010717]; snRNA transcription from RNA polymerase II promoter [GO:0042795]; spermatogenesis [GO:0007283]; stem cell differentiation [GO:0048863]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription from RNA polymerase II promoter [GO:0006366]enhancer binding [GO:0035326]|nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription elongation factor complex [GO:0008023]FUNCTION: Enhancer-binding elongation factor that specifically binds enhancers in embryonic stem cells (ES cells), marks them, and is required for their future activation during stem cell specification. Does not only bind to enhancer regions of active genes, but also marks the enhancers that are in a poised or inactive state in ES cells and is required for establishing proper RNA polymerase II occupancy at developmentally regulated genes in a cohesin-dependent manner. Probably required for priming developmentally regulated genes for later recruitment of the super elongation complex (SEC), for transcriptional activation during differentiation. Required for recruitment of P-TEFb within SEC during differentiation. Probably preloaded on germ cell chromatin, suggesting that it may prime gene activation by marking enhancers as early as in the germ cells. Promoting epithelial-mesenchymal transition (EMT) (By similarity). Elongation factor component of the super elongation complex (SEC), a complex requi< red to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). {ECO:0000250, ECO:0000269|PubMed:10882741, ECO:0000269|PubMed:22195968}.Q9HCH5SYTL2Synaptotagmin-like protein 2PSUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cell membrane. Note=Recruited on vesicular structures in cytotoxic T-lymphocytes (CTL) by RAB27A.; SUBCELLULAR LOCATION: Isoform 4: Cell membrane. Note=In the pancreatic alpha cells distributed in both peripheral and anterior regions. Localizes on the glucagon granules in the cell periphery.<exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; negative regulation of phosphatase activity [GO:0010923]; positive regulation of mucus secretion [GO:0070257]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192]Hcalcium-dependent phospholipid binding [GO:0005544]; calcium ion binding [GO:0005509]; clathrin binding [GO:0030276]; neurexin family protein binding [GO:0042043]; phosphatase binding [GO:0019902]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; syntaxin binding [GO:0019905]cytoplasm [GO:0005737]; exocytic vesicle [GO:0070382]; extrinsic component of plasma membrane [GO:0019897]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]0FUNCTION: Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon-containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca(2+) while binding to PIP2 is Ca(2+) insensitive. {ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782, ECO:0000269|PubMed:18812475}.Q9BWU0NADAP KanadaptinSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15764369}. Cytoplasm {ECO:0000269|PubMed:15764369}. Note=Mainly nuclear. Small amounts are found in the cytoplasm.cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]O60268K0513 Uncharacterized protein KIAA0513>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17010949}.P29762RABP1(Cellular retinoic acid-binding protein 1>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11909957}.Smulticellular organismal development [GO:0007275]; signal transduction [GO:0007165]kFUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.Q8NDZ4DIA1Deleted in autism protein 1ZSUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle. Golgi apparatus. Secreted.rcardiac muscle cell proliferation [GO:0060038]; regulation of phosphatidylinositol 3-kinase signaling [GO:0014066]]COPI vesicle coat [GO:0030126]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]FUNCTION: May play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PPI3K-AKT-CDK7 signaling cascade. {ECO:0000269|PubMed:23784961}.Q96PZ0PUS7"Pseudouridylate synthase 7 homologBpseudouridine synthesis [GO:0001522]; tRNA processing [GO:0008033]kenzyme binding [GO:0019899]; poly(A) RNA binding [GO:0044822]; pseudouridine synthase activity [GO:0009982]Q92759TF2H4*General transcription factor IIH subunit 47-methylguanosine mRNA capping [GO:0006370]; DNA repair [GO:0006281]; gene expression [GO:0010467]; negative regulation of gene expression, epigenetic [GO:0045814]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage removal [GO:0000718]; positive regulation of viral transcription [GO:0050434]; protein phosphorylation [GO:0006468]; regulation of gene expression, epigenetic [GO:0040029]; termination of RNA polymerase I transcription [GO:0006363]; transcription-coupled nucleotide-excision repair [GO:0006283]; transcription elongation from RNA polymerase II promoter [GO:0006368]; transcription elongation from RNA polymerase I promoter [GO:0006362]; transcription from RNA polymerase II promoter [GO:0006366]; transcription from RNA polymerase I promoter [GO:0006360]; transcription initiation from RNA polymerase II promoter [GO:0006367]; transcription initiation from RNA polymerase I promoter [GO:0006361]; viral process [GO:0016032]zATP-dependent DNA helicase activity [GO:0004003]; sequence-specific DNA binding transcription factor activity [GO:0003700]Q96G74OTUD5OTU domain-containing protein 5innate immune response [GO:0045087]; negative regulation of type I interferon production [GO:0032480]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; response to lipopolysaccharide [GO:0032496]FUNCTION: Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). {ECO:0000269|PubMed:17991829, ECO:0000269|PubMed:22245969, ECO:0000269|PubMed:23827681}.Q9NZW5MPP6MAGUK p55 subfamily member 6Q10588BST11ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2humoral immune response [GO:0006959]; multicellular organismal development [GO:0007275]; positive regulation of B cell proliferation [GO:0030890]NAD(P)+ nucleosidase activity [GO:0050135]; NAD+ nucleosidase activity [GO:0003953]; phosphorus-oxygen lyase activity [GO:0016849]; transferase activity [GO:0016740]FUNCTION: Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth. {ECO:0000269|PubMed:11866528}.O43303CP110)Centriolar coiled-coil protein of 110 kDaSUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:21620453}. Note=Recruited early and then associates with the growing distal tips. Recruited to the mother centriole by KIF24. Removed from centrioles by TTBK2, leading to initiation of ciliogenesis.cell projection organization [GO:0030030]; centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; organelle organization [GO:0006996]; regulation of cytokinesis [GO:0032465] FUNCTION: Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation. Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2. {ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:23486064}.O95470SGPL1Sphingosine-1-phosphate lyase 1\SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein.androgen metabolic process [GO:0008209]; apoptotic signaling pathway [GO:0097190]; ceramide metabolic process [GO:0006672]; estrogen metabolic process [GO:0008210]; face morphogenesis [GO:0060325]; fatty acid metabolic process [GO:0006631]; fibroblast migration [GO:0010761]; hemopoiesis [GO:0030097]; kidney < development [GO:0001822]; Leydig cell differentiation [GO:0033327]; luteinization [GO:0001553]; palate development [GO:0060021]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; post-embryonic development [GO:0009791]; regulation of multicellular organism growth [GO:0040014]; skeletal system morphogenesis [GO:0048705]; small molecule metabolic process [GO:0044281]; spermatogenesis [GO:0007283]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid catabolic process [GO:0030149]; sphingolipid metabolic process [GO:0006665]; vasculogenesis [GO:0001570]carboxy-lyase activity [GO:0016831]; pyridoxal phosphate binding [GO:0030170]; sphinganine-1-phosphate aldolase activity [GO:0008117]endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; integral component of endoplasmic reticulum membrane [GO:0030176]FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. {ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:14570870, ECO:0000269|PubMed:24809814}.Q16875F26366-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3Sbrain development [GO:0007420]; canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]6-phosphofructo-2-kinase activity [GO:0003873]; ATP binding [GO:0005524]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]AFUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.P35227PCGF2$Polycomb group RING finger protein 27anterior/posterior pattern specification [GO:0009952]; cellular protein metabolic process [GO:0044267]; cellular response to hydrogen peroxide [GO:0070301]; embryonic skeletal system morphogenesis [GO:0048704]; histone acetylation [GO:0016573]; in utero embryonic development [GO:0001701]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; transcription, DNA-templated [GO:0006351]nuclear body [GO:0016604]; nuclear chromatin [GO:0000790]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]; sex chromatin [GO:0001739]FUNCTION: Transcriptional repressor. Binds specifically to the DNA sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a role in control of cell proliferation and/or neural cell development. Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a role in antero-posterior specification of the axial skeleton and negative regulation of the self-renewal activity of hematopoietic stem cells. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Is not functionally redundant with BMI1; unlike BMI1 does not stimulate the E3 ubiquitin-protein ligase activity in a reconstituted PRC1-like complex (By similarity). {ECO:0000250}.A4D1P6WDR91WD repeat-containing protein 91P78537BL1S1=Biogenesis of lysosome-related organelles complex 1 subunit 1SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22309213}. Mitochondrion matrix {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol {ECO:0000269|PubMed:22309213}.activation of mitophagy in response to mitochondrial depolarization [GO:0098779]; aerobic respiration [GO:0009060]; anterograde axon cargo transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; endosomal transport [GO:0016197]; melanosome organization [GO:0032438]; membrane organization [GO:0061024]; neuron projection development [GO:0031175]; peptidyl-lysine acetylation [GO:0018394]; platelet dense granule organization [GO:0060155]; post-Golgi vesicle-mediated transport [GO:0006892]BLOC-1 complex [GO:0031083]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5A1 and NDUFA9. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:22309213}.P14210HGFHepatocyte growth factorblood coagulation [GO:0007596]; cell chemotaxis [GO:0060326]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; epithelial to mesenchymal transition [GO:0001837]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; hyaluronan metabolic process [GO:0030212]; mitotic nuclear division [GO:0007067]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of hydrogen peroxide-mediated programmed cell death [GO:1901299]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; organ regeneration [GO:0031100]; platelet activation [GO:0030168]; platelet degranulation [GO:0002576]; positive chemotaxis [GO:0050918]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of cell proliferation [GO:0008284]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of myelination [GO:0031643]; positive regulation of neuron projection regeneration [GO:0070572]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling [GO:0060665]rchemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; platelet alpha granule lumen [GO:0031093]UFUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. {ECO:0000269|PubMed:15167892, ECO:0000269|PubMed:20624990}.O95248MTMR5Myotubularin-related protein 5;SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9537414}.ypositive regulation of GTPase activity [GO:0043547]; protein dephosphorylation [GO:0006470]; spermatogenesis [GO:0007283]phosphatase regulator activity [GO:0019208]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; Rab guanyl-nucleotide exchange factor activity [GO:0017112]FUNCTION: Probable pseudophosphatase. Lacks several amino acids in the catalytic pocket which renders it catalytically inactive as a phosphatase. The pocket is however sufficiently preserve< d to bind phosphorylated substrates, and maybe protect them from phosphatases. Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts. According to PubMed:20937701, may function as a guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. {ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9537414}.Q15059BRD3 Bromodomain-containing protein 3WSUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Detected on chromatin. {ECO:0000250}.chromatin modification [GO:0016568]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; transcription, DNA-templated [GO:0006351]uFUNCTION: Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene. {ECO:0000250, ECO:0000269|PubMed:18406326}.Q6ZVC0NYAP1DNeuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1bneuron projection morphogenesis [GO:0048812]; phosphatidylinositol 3-kinase signaling [GO:0014065]FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis. {ECO:0000250}.Q9NQW6ANLNActin-binding protein anillinSUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody.glomerular visceral epithelial cell migration [GO:0090521]; hematopoietic progenitor cell differentiation [GO:0002244]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0007067]; regulation of exit from mitosis [GO:0007096]; septin ring assembly [GO:0000921]actin cytoskeleton [GO:0015629]; actomyosin contractile ring [GO:0005826]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]FUNCTION: Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. May play a significant role in podocyte cell migration (PubMed:24676636). {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:12479805, ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16357138, ECO:0000269|PubMed:24676636}.Q16877F26466-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 43canonical glycolysis [GO:0061621]; carbohydrate metabolic process [GO:0005975]; carbohydrate phosphorylation [GO:0046835]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; glucose metabolic process [GO:0006006]; small molecule metabolic process [GO:0044281]Q5TCS8KAD9Adenylate kinase 9eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23416111}. Nucleus {ECO:0000269|PubMed:23416111}.ADP phosphorylation [GO:0006757]; AMP phosphorylation [GO:0006756]; CDP phosphorylation [GO:0061508]; CMP phosphorylation [GO:0061566]; dADP phosphorylation [GO:0006174]; dAMP phosphorylation [GO:0061565]; dCDP phosphorylation [GO:0061570]; dCMP phosphorylation [GO:0061567]; dGDP phosphorylation [GO:0006186]; GDP phosphorylation [GO:0061568]; TDP phosphorylation [GO:0061571]; UDP phosphorylation [GO:0061569]ATP binding [GO:0005524]; nucleoside diphosphate kinase activity [GO:0004550]; nucleoside phosphate kinase activity [GO:0050145]HFUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has both nucleoside monophosphate and diphosphate kinase activities. Catalyzes the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as phosphate donor and of CMP with GTP as phosphate donor. Also catalyzes the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor. Shows substrate preference of CDP > UDP > ADP > GDP > TDP. {ECO:0000269|PubMed:23416111}.Q9UIV1CNOT7(CCR4-NOT transcription complex subunit 7SUBCELLULAR LOCATION: Nucleus. Cytoplasm, P-body {ECO:0000250}. Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.carbohydrate metabolic process [GO:0005975]; cytoplasmic mRNA processing body assembly [GO:0033962]; deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay [GO:0043928]; gene expression [GO:0010467]; gene silencing by miRNA [GO:0035195]; gene silencing by RNA [GO:0031047]; negative regulation of cell proliferation [GO:0008285]; negative regulation of gene expression [GO:0010629]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cell proliferation [GO:0008284]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; regulation of translation [GO:0006417]; RNA phosphodiester bond hydrolysis, exonucleolytic [GO:0090503]; signal transduction [GO:0007165]; transcription, DNA-templated [GO:0006351]43'-5'-exoribonuclease activity [GO:0000175]; exoribonuclease activity [GO:0004532]; metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]; sequence-specific DNA binding transcription factor activity [GO:0003700]; signal transducer activity [GO:0004871]FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity. {ECO:0000269|PubMed:19605561, ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:20634287, ECO:0000269|PubMed:23236473}.Q9GZP4PITH1 PITH domain-containing protein 1P103211C078HLA class I histocompatibility antigen, Cw-7 alpha chain$peptide antigen binding [GO:0042605]cell surface [GO:0009986]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]Q6XE24RBMS38RNA-binding motif, single-stranded-interacting protein 3>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10675610}.AmRNA 3'-UTR binding [GO:0003730]; nucleotide binding [GO:0000166]XFUNCTION: Binds poly(A) and poly(U) oligoribonucleotides. {ECO:0000269|PubMed:10675610}.O14939PLD2Phospholipase D2cell motility [GO:0048870]; cytoskeleton organization [GO:0007010]; exocytosis [GO:0006887]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; glycerophospholipid biosynthetic process [GO:00464< 74]; G-protein coupled receptor internalization [GO:0002031]; innate immune response [GO:0045087]; inositol lipid-mediated signaling [GO:0048017]; membrane lipid metabolic process [GO:0006643]; phosphatidic acid biosynthetic process [GO:0006654]; phosphatidic acid metabolic process [GO:0046473]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395]; phospholipid metabolic process [GO:0006644]; regulation of cell migration [GO:0030334]; regulation of phagocytosis [GO:0050764]; regulation of vesicle-mediated transport [GO:0060627]; small GTPase mediated signal transduction [GO:0007264]; small molecule metabolic process [GO:0044281]; synaptic vesicle recycling [GO:0036465]brush border membrane [GO:0031526]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; vesicle [GO:0031982]fFUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis. {ECO:0000250}.P50607TUBTubby protein homologaSUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase C. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway (By similarity). {ECO:0000250}.multicellular organismal macromolecule metabolic process [GO:0044259]; phagocytosis, recognition [GO:0006910]; photoreceptor cell maintenance [GO:0045494]; positive regulation of phagocytosis [GO:0050766]; protein localization to photoreceptor outer segment [GO:1903546]; receptor localization to nonmotile primary cilium [GO:0097500]; response to hormone [GO:0009725]; retina development in camera-type eye [GO:0060041]; sensory perception of sound [GO:0007605]Ophosphatidylinositol binding [GO:0035091]; protein complex binding [GO:0032403]cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886]FUNCTION: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:19837063}.Q9BVI4NOC4L#Nucleolar complex protein 4 homologSUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:12429849}; Multi-pass membrane protein {ECO:0000269|PubMed:12429849}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.integral component of membrane [GO:0016021]; Noc4p-Nop14p complex [GO:0030692]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleus [GO:0005634]; small-subunit processome [GO:0032040]Q16576RBBP7Histone-binding protein RBBP7cell proliferation [GO:0008283]; cellular heat acclimation [GO:0070370]; CENP-A containing nucleosome assembly [GO:0034080]; chromatin organization [GO:0006325]; DNA replication [GO:0006260]; gene expression [GO:0010467]; multicellular organismal development [GO:0007275]; negative regulation of cell growth [GO:0030308]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; nucleosome assembly [GO:0006334]; regulation of gene expression, epigenetic [GO:0040029]; response to steroid hormone [GO:0048545]; transcription, DNA-templated [GO:0006351]hESC/E(Z) complex [GO:0035098]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]|FUNCTION: Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. {ECO:0000269|PubMed:10866654}.P38432COILCoilinmSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7679389}. Nucleus, Cajal body {ECO:0000269|PubMed:7679389}.Oidentical protein binding [GO:0042802]; protein C-terminus binding [GO:0008022]Cajal body [GO:0015030]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. {ECO:0000269|PubMed:7679389}.Q70Z53F10C1Protein FRA10AC1<SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15203205}.Q9NRG0CHRC1)Chromatin accessibility complex protein 1Hchromatin remodeling [GO:0006338]; DNA biosynthetic process [GO:0071897]wDNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; sequence-specific DNA binding [GO:0043565]?CHRAC [GO:0008623]; epsilon DNA polymerase complex [GO:0008622]FUNCTION: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1.P16278BGALBeta-galactosidaseSUBCELLULAR LOCATION: Isoform 1: Lysosome.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, perinuclear region. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes.carbohydrate metabolic process [GO:0005975]; cellular carbohydrate metabolic process [GO:0044262]; cellular protein metabolic process [GO:0044267]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; galactose catabolic process [GO:0019388]; glycosaminoglycan catabolic process [GO:0006027]; glycosaminoglycan metabolic process [GO:0030203]; glycosphingolipid metabolic process [GO:0006687]; keratan sulfate catabolic process [GO:0042340]; keratan sulfate metabolic process [GO:0042339]; post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]; small molecule metabolic process [GO:0044281]; sphingolipid metabolic process [GO:0006665]Jbeta-galactosidase activity [GO:0004565]; galactoside binding [GO:0016936]cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.; FUNCTION: Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.Q8N448LNX2Ligand of Numb protein X 2O60336MABP12Mitogen-activated protein kinase-binding protein 1(activation of JNKK activ< ity [GO:0007256];FUNCTION: Involved in JNK signaling pathway. {ECO:0000250}.O00472ELL2(RNA polymerase II elongation factor ELL2regulation of transcription, DNA-templated [GO:0006355]; snRNA transcription from RNA polymerase II promoter [GO:0042795]; transcription elongation from RNA polymerase II promoter [GO:0006368]centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; transcription elongation factor complex [GO:0008023]FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23251033}.Q8NEZ5FBX22F-box only protein 22LSUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.cellular protein modification process [GO:0006464]; cellular response to starvation [GO:0009267]; nucleocytoplasmic transport [GO:0006913]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:2000060]; protein polyubiquitination [GO:0000209]; regulation of skeletal muscle fiber development [GO:0048742]; ubiquitin-dependent protein catabolic process [GO:0006511])nucleus [GO:0005634]; Z disc [GO:0030018]GFUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. {ECO:0000269|PubMed:22972877}.P27695APEX1)DNA-(apurinic or apyrimidinic site) lyaseUSUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm. Note=Detected in the cytoplasm of B-cells stimulated to switch (By similarity). Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. {ECO:0000250}.; SUBCELLULAR LOCATION: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial: Mitochondrion. Note=The cleaved APEX2 is only detected in mitochondria (By similarity). Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. {ECO:0000250}.[base-excision repair [GO:0006284]; cell redox homeostasis [GO:0045454]; DNA demethylation [GO:0080111]; DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; mismatch repair [GO:0006298]; mitotic cell cycle [GO:0000278]; negative regulation of nucleic acid-templated transcription [GO:1903507]; nucleic acid phosphodiester bond hydrolysis [GO:0090305]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA gap filling [GO:0006297]; oxidation-reduction process [GO:0055114]; positive regulation of DNA repair [GO:0045739]; regulation of mRNA stability [GO:0043488]; regulation of transcription, DNA-templated [GO:0006355]; RNA phosphodiester bond hydrolysis, endonucleolytic [GO:0090502]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via semi-conservative replication [GO:0032201]; transcription, DNA-templated [GO:0006351]; transcription-coupled nucleotide-excision repair [GO:0006283]A3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) lyase activity [GO:0003906]; DNA binding [GO:0003677]; double-stranded DNA 3'-5' exodeoxyribonuclease activity [GO:0008311]; endodeoxyribonuclease activity [GO:0004520]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphodiesterase I activity [GO:0004528]; phosphoric diester hydrolase activity [GO:0008081]; poly(A) RNA binding [GO:0044822]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; uracil DNA N-glycosylase activity [GO:0004844]centrosome [GO:0005813]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ribosome [GO:0005840] FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease invol< ved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. {ECO:0000269|PubMed:10023679, ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:11452037, ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:11832948, ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:16617147, ECO:0000269|PubMed:1719477, ECO:0000269|PubMed:18179823, ECO:0000269|PubMed:18439621, ECO:0000269|PubMed:18579163, ECO:0000269|PubMed:18809583, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:19401441, ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20699270, ECO:0000269|PubMed:21496894, ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:8355688, ECO:0000269|PubMed:8621488, ECO:0000269|PubMed:8932375, ECO:0000269|PubMed:9108029, ECO:0000269|PubMed:9207062, ECO:0000269|PubMed:9560228, ECO:0000269|PubMed:9804799}.P47974TISD(Zinc finger protein 36, C3H1 type-like 2qcell proliferation [GO:0008283]; definitive hemopoiesis [GO:0060216]; hemopoiesis [GO:0030097]; mRNA catabolic process [GO:0006402]; negative regulation of stem cell differentiation [GO:2000737]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; regulation of mRNA stability [GO:0043488]; regulation of transcription, DNA-templated [GO:0006355]; somatic stem cell division [GO:0048103]; somatic stem cell maintenance [GO:0035019]; T cell differentiation in thymus [GO:0033077]AU-rich element binding [GO:0017091]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; poly(A) RNA binding [GO:0044822]; sequence-specific DNA binding transcription factor activity [GO:0003700]DFUNCTION: mRNA-binding protein that plays a key role in self-renewal of erythroid cells in response to glucocorticoids. Specifically binds to the AU-rich element (ARE) in the 3'-UTR of target mRNAs, promoting their deadenylation and degradation (PubMed:14981510). Specifically expressed in burst-forming unit-erythroid (BFU-E) progenitors in response to glucocorticoids and acts as a negative regulator of erythroid cell differentiation: promotes self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. Down-regulated during erythroid differentiation from the BFU-E stage, stabilizing mRNAs required for terminal differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:14981510}.Q9BPY3F118BProtein FAM118BHSUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000269|PubMed:24569877}.Cajal body [GO:0015030]SFUNCTION: May play a role in Cajal bodies formation. {ECO:0000269|PubMed:24569877}.A3KN83SBNO1"Protein strawberry notch homolog 1Q9ULH0KDIS)Kinase D-interacting substrate of 220 kDaSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Late endosome {ECO:0000250}. Note=Localized at late endosome before or after nerve growth factor (NGF) stimulation.activation of MAPKK activity [GO:0000186]; cellular response to nerve growth factor stimulus [GO:1990090]; cytoplasmic transport [GO:0016482]; dendrite morphogenesis [GO:0048813]; in utero embryonic development [GO:0001701]; nerve growth factor signaling pathway [GO:0038180]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of neuron projection development [GO:0010976]; regulation of protein kinase activity [GO:0045859]OPDZ domain binding [GO:0030165]; protein kinase regulator activity [GO:0019887]cytosol [GO:0005829]; integral component of membrane [GO:0016021]; late endosome [GO:0005770]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; protein complex [GO:0043234]sFUNCTION: Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway. {ECO:0000250, ECO:0000269|PubMed:18089783}.Q86UA1PRP39Pre-mRNA-processing factor 397FUNCTION: Involved in pre-mRNA splicing. {ECO:0000250}.O15085ARHGB)Rho guanine nucleotide exchange factor 11SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900204}. Membrane {ECO:0000269|PubMed:10900204}. Note=Translocated to the membrane upon stimulation.actin cytoskeleton organization [GO:0030036]; apoptotic signaling pathway [GO:0097190]; axon guidance [GO:0007411]; cytokinesis [GO:0000910]; establishment of cell polarity [GO:0030010]; G-protein coupled receptor signaling pathway [GO:0007186]; movement of cell or subcellular component [GO:0006928]; neurotrophin TRK receptor signaling pathway [GO:0048011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; positive regulation of transcription, DNA-templated [GO:0045893]; regulation of cell growth [GO:0001558]; regulation of Rho protein signal transduction [GO:0035023]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; small GTPase mediated signal transduction [GO:0007264]; striated muscle contraction [GO:0006941]; termination of G-protein coupled receptor signaling pathway [GO:0038032]_cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular [GO:0005622]; membrane [GO:0016020]WFUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}.O94992HEXI1Protein HEXIM1ZSUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Binds alpha-importin and is mostly nuclear.heart development [GO:0007507]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; transcription, DNA-templated [GO:0006351]lcyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; snRNA binding [GO:0017069]xFUNCTION: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. {ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:12941847, ECO:0000269|PubMed:14580347, ECO:0000269|PubMed:15201869, ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15940264, ECO:0000269|PubMed:15941832, ECO:0000269|PubMed:17088550}.Q9GZR1SENP6Sentrin-specific protease 6YSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875}.protein desumoylation [GO:0016926]; protein modifica< tion by small protein removal [GO:0070646]; protein sumoylation [GO:0016925]; regulation of kinetochore assembly [GO:0090234]; regulation of spindle assembly [GO:0090169],SUMO-specific protease activity [GO:0016929]bFUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875, ECO:0000269|PubMed:18799455, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20705237, ECO:0000269|PubMed:21148299}.Q9BQP7MGME1.Mitochondrial genome maintenance exonuclease 1SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03030, ECO:0000269|PubMed:23313956, ECO:0000269|PubMed:23358826}.mitochondrial DNA repair [GO:0043504]; mitochondrial DNA replication [GO:0006264]; mitochondrial genome maintenance [GO:0000002]>single-stranded DNA exodeoxyribonuclease activity [GO:0008297]FUNCTION: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair. Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells. {ECO:0000255|HAMAP-Rule:MF_03030, ECO:0000269|PubMed:23313956, ECO:0000269|PubMed:23358826}.Q8WVT3TPC12/Trafficking protein particle complex subunit 12iSUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:21525244}.Aproteolysis [GO:0006508]; vesicle-mediated transport [GO:0016192]Aendoplasmic reticulum-Golgi intermediate compartment [GO:0005793]P09234RU1C$U1 small nuclear ribonucleoprotein CmRNA 5'-splice site recognition [GO:0000395]; mRNA splicing, via spliceosome [GO:0000398]; spliceosomal snRNP assembly [GO:0000387]mRNA binding [GO:0003729]; poly(A) RNA binding [GO:0044822]; protein homodimerization activity [GO:0042803]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO:0008270]Cajal body [GO:0015030]; commitment complex [GO:0000243]; nucleoplasm [GO:0005654]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004]bFUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates E complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. {ECO:0000269|PubMed:1826349, ECO:0000269|PubMed:2136774, ECO:0000269|PubMed:8798632}.Q13610PWP1%Periodic tryptophan protein 1 homologJGolgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]IFUNCTION: May play an important role in cell growth and/or transcription.Q9BQN2MT1P3Putative metallothionein MT1P3Q9H2J7S6A157Sodium-dependent neutral amino acid transporter B(0)AT2Vamino acid transport [GO:0006865]; ion transport [GO:0006811]; leucine transport [GO:0015820]; neurotransmitter transport [GO:0006836]; neutral amino acid transport [GO:0015804]; proline transmembrane transport [GO:0035524]; proline transport [GO:0015824]; sodium ion transmembrane transport [GO:0035725]; transmembrane transport [GO:0055085]neurotransmitter:sodium symporter activity [GO:0005328]; neurotransmitter transporter activity [GO:0005326]; proline:sodium symporter activity [GO:0005298]FUNCTION: Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent. {ECO:0000269|PubMed:16226721}.Q9Y5Z7HCFC2Host cell factor 2eSUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10196288}. Nucleus {ECO:0000269|PubMed:10196288}.negative regulation of transcription from RNA polymerase II promoter [GO:0000122]; regulation of transcription from RNA polymerase II promoter [GO:0006357]; viral process [GO:0016032]O43924PDE6DQRetinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta?SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:9712853}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9712853}; Peripheral membrane protein {ECO:0000269|PubMed:9712853}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24166846}.forganelle organization [GO:0006996]; response to stimulus [GO:0050896]; visual perception [GO:0007601]3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; GTPase inhibitor activity [GO:0005095]; Rab GTPase binding [GO:0017137]cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; primary cilium [GO:0072372]MFUNCTION: Promotes the release of prenylated target proteins from cellular membranes (PubMed:9712853). Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (PubMed:22002721, PubMed:23698361). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (PubMed:24166846). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity). {ECO:0000250|UniProtKB:O55057, ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23559067, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24166846, ECO:0000269|PubMed:9712853}.Q96GW9SYMM&Methionine--tRNA ligase, mitochondrialFATP binding [GO:0005524]; methionine-tRNA ligase activity [GO:0004825]Q9NWR8MCUB8Calcium uniporter regulatory subunit MCUb, mitochondrialSUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:24231807}; Multi-pass membrane protein {ECO:0000269|PubMed:24231807}.dmitochondrial calcium ion homeostasis [GO:0051560]; mitochondrial calcium ion transport [GO:0006851]/calcium channel inhibitor activity [GO:0019855]calcium channel complex [GO:0034704]; integral component of mitochondrial inner membrane [GO:0031305]; intrinsic component of membrane [GO:0031224]; mitochondrion [GO:0005739]; uniplex complex [GO:1990246]FUNCTION: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. {ECO:0000250|UniProtKB:Q810S1}.P00374DYRDihydrofolate reductasefolic acid metabolic process [GO:0046655]; G1/< S transition of mitotic cell cycle [GO:0000082]; glycine biosynthetic process [GO:0006545]; mitotic cell cycle [GO:0000278]; nitric oxide metabolic process [GO:0046209]; nucleotide biosynthetic process [GO:0009165]; one-carbon metabolic process [GO:0006730]; regulation of nitric-oxide synthase activity [GO:0050999]; regulation of transcription involved in G1/S transition of mitotic cell cycle [GO:0000083]; response to methotrexate [GO:0031427]; small molecule metabolic process [GO:0044281]; tetrahydrofolate biosynthetic process [GO:0046654]; tetrahydrofolate metabolic process [GO:0046653]; vitamin metabolic process [GO:0006766]; water-soluble vitamin metabolic process [GO:0006767]~dihydrofolate reductase activity [GO:0004146]; drug binding [GO:0008144]; mRNA binding [GO:0003729]; NADP binding [GO:0050661]CFUNCTION: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1. {ECO:0000269|PubMed:12096917, ECO:0000269|PubMed:21876188}.Q9BWF2TRAIP!E3 ubiquitin-protein ligase TRAIPSUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Nucleus, nucleolus. Note=Occasionally observed at nuclear puncta.apoptotic process [GO:0006915]; cell proliferation [GO:0008283]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; signal transduction [GO:0007165]ligase activity [GO:0016874]; receptor signaling protein activity [GO:0005057]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]Dnucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]FUNCTION: Inhibits activation of NF-kappa-B mediated by TNF (By similarity). Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFN-beta production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation. May mediate assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN to facilitate bypass of DNA lesions and preserve genomic integrity. {ECO:0000250, ECO:0000269|PubMed:22945920, ECO:0000269|PubMed:24553286}.Q8IX30SCUB3<Signal peptide, CUB and EGF-like domain-containing protein 3iSUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15234972}. Cell surface {ECO:0000269|PubMed:15234972}.Tprotein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]<cell surface [GO:0009986]; extracellular region [GO:0005576]&FUNCTION: Binds to TGFBR2 and activates TGFB signaling. In lung cancer cells, could serve as an endogenous autocrine and paracrine ligand of TGFBR2, which could regulate TGFBR2 signaling and hence modulate epithelial-mesenchymal transition and cancer progression. {ECO:0000269|PubMed:21441952}.Q99719Septin-5SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In platelets, found in areas surrounding alpha-granules.cytokinesis [GO:0000910]; regulation of exocytosis [GO:0017157]; regulation of synaptic vesicle exocytosis [GO:2000300]; synaptic vesicle targeting [GO:0016080]cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity). {ECO:0000250, ECO:0000305}.Q15139KPCD1"Serine/threonine-protein kinase D1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18076381}. Cell membrane {ECO:0000269|PubMed:18076381}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Translocation to the cell membrane is required for kinase activation.~angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell proliferation [GO:0008283]; cellular response to oxidative stress [GO:0034599]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; negative regulation of cell death [GO:0060548]; negative regulation of endocytosis [GO:0045806]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of endothelial cell chemotaxis [GO:2001028]; positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [GO:0038033]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of histone deacetylase activity [GO:1901727]; positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123]; positive regulation of neuron projection development [GO:0010976]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of transcription from RNA polymerase II promoter [GO:0045944]; protein autophosphorylation [GO:0046777]; protein kinase D signaling [GO:0089700]; regulation of integrin-mediated signaling pathway [GO:2001044]; regulation of keratinocyte proliferation [GO:0010837]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; signal transduction [GO:0007165]; small molecule metabolic process [GO:0044281]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein kinase C activity [GO:0004697]; protein serine/threonine kinase activity [GO:0004674]cell-cell junction [GO:0005911]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; integral component of plasma membrane [GO:0005887]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carr< iers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. {ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:10764790, ECO:0000269|PubMed:12505989, ECO:0000269|PubMed:12637538, ECO:0000269|PubMed:15471852, ECO:0000269|PubMed:17442957, ECO:0000269|PubMed:18332134, ECO:0000269|PubMed:18509061, ECO:0000269|PubMed:19135240, ECO:0000269|PubMed:19211839}.O95714HERC2!E3 ubiquitin-protein ligase HERC2SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus. Note=Recruited to sites of DNA damage in response to ionizing radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis.cellular protein metabolic process [GO:0044267]; cellular response to DNA damage stimulus [GO:0006974]; DNA repair [GO:0006281]; intracellular protein transport [GO:0006886]; positive regulation of GTPase activity [GO:0043547]; post-translational protein modification [GO:0043687]; protein sumoylation [GO:0016925]; protein ubiquitination [GO:0016567]; protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787]; spermatogenesis [GO:0007283]guanyl-nucleotide exchange factor activity [GO:0005085]; ligase activity [GO:0016874]; SUMO binding [GO:0032183]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]centriole [GO:0005814]; cytoplasm [GO:0005737]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. {ECO:0000269|PubMed:20023648, ECO:0000269|PubMed:20304803, ECO:0000269|PubMed:22508508}.Q9H0X9OSBL5+Oxysterol-binding protein-related protein 5SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21220512}; Single-pass membrane protein {ECO:0000269|PubMed:21220512}.cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; Golgi to plasma membrane transport [GO:0006893]@cholesterol binding [GO:0015485]; oxysterol binding [GO:0008142]FUNCTION: May cooperate with NPC1 to mediate the exit of cholesterol from endosomes/lysosomes (PubMed:21220512). Binds 25-hydroxycholesterol and cholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:21220512}.Q96EI5TCAL40Transcription elongation factor A protein-like 4Q86YT6MIB1 E3 ubiquitin-protein ligase MIB1SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24121310}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24121310}. Cell membrane {ECO:0000250}. Note=Localizes to the plasma membrane (By similarity). According to PubMed:15048887, it is mitochondrial, however such localization remains unclear. Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock. {ECO:0000250}.blood vessel development [GO:0001568]; endocytosis [GO:0006897]; heart looping [GO:0001947]; in utero embryonic development [GO:0001701]; negative regulation of neuron differentiation [GO:0045665]; neural tube formation [GO:0001841]; Notch signaling pathway [GO:0007219]; positive regulation of endocytosis [GO:0045807]; protein ubiquitination [GO:0016567]; somitogenesis [GO:0001756]centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity). Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation. {ECO:0000250, ECO:0000269|PubMed:24121310}.Q9C005DPY30Protein dpy-30 homologbSUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19651892}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19651892}. Note=Associated with chromatin at regions enriched in histone H3 trimethylated at 'Lys-4. Highly enriched in gene promoter regions and 5' UTRs, but not in downstream regions of genes or 3' UTRs (By similarity). {ECO:0000250}.chromatin organization [GO:0006325]; endosomal transport [GO:0016197]; histone H3-K4 methylation [GO:0051568]; regulation of transcription, DNA-templated [GO:0006355]; transcription, DNA-templated [GO:0006351]Golgi apparatus [GO:0005794]; histone methyltransferase complex [GO:0035097]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188]; trans-Golgi network [GO:0005802]lFUNCTION: As part of <the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport. {ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:19651892, ECO:0000269|PubMed:21335234}.Q8IX05CD302 CD302 antigentSUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, filopodium {ECO:0000269|PubMed:17947679}. Cytoplasm, cell cortex {ECO:0000269|PubMed:17947679}. Cell projection, microvillus {ECO:0000269|PubMed:17947679}. Note=Colocalizes with F-actin in filopodia, cellular cortex and microvilli of the apical cell surface.phagocytosis [GO:0006909]cell cortex [GO:0005938]; filopodium [GO:0030175]; integral component of membrane [GO:0016021]; membrane [GO:0016020]; microvillus [GO:0005902]FUNCTION: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration. {ECO:0000269|PubMed:17947679}.Q08257QORQuinone oxidoreductase>SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20103721}.sprotein homotetramerization [GO:0051289]; visual perception [GO:0007601]; xenobiotic catabolic process [GO:0042178]mRNA 3'-UTR binding [GO:0003730]; NADPH:quinone reductase activity [GO:0003960]; NADPH binding [GO:0070402]; zinc ion binding [GO:0008270]cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding. {ECO:0000269|PubMed:17497241, ECO:0000269|PubMed:20103721}.Q6DN12MCTP29Multiple C2 and transmembrane domain-containing protein 2Zcalcium-mediated signaling [GO:0019722]; multicellular organismal development [GO:0007275]^integral component of membrane [GO:0016021]; intracellular [GO:0005622]; membrane [GO:0016020]gFUNCTION: Might play a role in the development of cardiac outflow tract. {ECO:0000269|PubMed:23773997}.Q9H0G5NSRP1-Nuclear speckle splicing regulatory protein 1SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21296756}. Nucleus speckle {ECO:0000269|PubMed:21296756}. Note=Colocalizes with splicing factors SRSF1 and SRSF2 in speckles.developmental process [GO:0032502]; mRNA processing [GO:0006397]; nucleocytoplasmic transport [GO:0006913]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]Xnuclear speck [GO:0016607]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:0030529]tFUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. {ECO:0000269|PubMed:21296756}.Q8IW41MAPK5%MAP kinase-activated protein kinase 5YSUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.activation of MAPK activity [GO:0000187]; cell surface receptor signaling pathway [GO:0007166]; MAPK cascade [GO:0000165]; negative regulation of TOR signaling [GO:0032007]; peptidyl-serine phosphorylation [GO:0018105]; protein autophosphorylation [GO:0046777]; Ras protein signal transduction [GO:0007265]; regulation of translation [GO:0006417]; signal transduction [GO:0007165]; stress-induced premature senescence [GO:0090400]ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; MAP kinase kinase activity [GO:0004708]; mitogen-activated protein kinase binding [GO:0051019]; p53 binding [GO:0002039]; protein serine/threonine kinase activity [GO:0004674]; signal transducer activity [GO:0004871]FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement. {ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17728103, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:9628874}.193IDs150IRS.ID193IDs150IRS.Sort-ID193IDs150IRS.GeneSymbol Ratio(S/P)ySupplementary Table 1. Proteomics analysis of proliferating and senescent cells (Replicative exhaustion and IR-induced). 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